A post-translational modification of proteins by the attachment of an isoprenoid to the C-terminal cysteine residue. The isoprenoids used, farnesyl diphosphate or geranylgeranyl diphosphate, are derived from the same biochemical pathway that produces cholesterol.
Attachment of isoprenoids (TERPENES) to other compounds, especially PROTEINS and FLAVONOIDS.
A somewhat heterogeneous class of enzymes that catalyze the transfer of alkyl or related groups (excluding methyl groups). EC 2.5.
An enzyme that, in the pathway of cholesterol biosynthesis, catalyzes the condensation of isopentenyl pyrophosphate and dimethylallylpyrophosphate to yield pyrophosphate and geranylpyrophosphate. The enzyme then catalyzes the condensation of the latter compound with another molecule of isopentenyl pyrophosphate to yield pyrophosphate and farnesylpyrophosphate. EC 2.5.1.1.
An enzyme that catalyzes the synthesis of geranylgeranyl diphosphate from trans, trans-farnesyl diphosphate and isopentenyl diphosphate.
Mevalonic acid is a crucial intermediate compound in the HMG-CoA reductase pathway, which is a metabolic route that produces cholesterol, other steroids, and isoprenoids in cells.
Phosphoric or pyrophosphoric acid esters of polyisoprenoids.
A colorless liquid extracted from oils of plants such as citronella, neroli, cyclamen, and tuberose. It is an intermediate step in the biological synthesis of cholesterol from mevalonic acid in vertebrates. It has a delicate odor and is used in perfumery. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.
An X chromosome-linked abnormality characterized by atrophy of the choroid and degeneration of the retinal pigment epithelium causing night blindness.
A fungal metabolite isolated from cultures of Aspergillus terreus. The compound is a potent anticholesteremic agent. It inhibits 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It also stimulates the production of low-density lipoprotein receptors in the liver.
A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.
Twenty-carbon compounds derived from MEVALONIC ACID or deoxyxylulose phosphate.
A GTP-BINDING PROTEIN involved in regulating a signal transduction pathway that controls assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC 3.6.1.47.
Acyclic branched or unbranched hydrocarbons having two carbon-carbon double bonds.
An enzyme involved in the MEVALONATE pathway, it catalyses the synthesis of farnesyl diphosphate from isopentenyl diphosphate and dimethylallyl diphosphate.
A genus of ascomycetous fungi, family Clavicipitaceae, order Hypocreales, parasitic on various grasses (POACEAE). The sclerotia contain several toxic alkaloids. Claviceps purpurea on rye causes ergotism.
Protein factors that inhibit the dissociation of GDP from GTP-BINDING PROTEINS.
A metallic element with the atomic symbol Ir, atomic number 77, and atomic weight 192.22.
A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS and through early Golgi compartments. This enzyme was formerly listed as EC 3.6.1.47.
Small, monomeric GTP-binding proteins encoded by ras genes (GENES, RAS). The protooncogene-derived protein, PROTO-ONCOGENE PROTEIN P21(RAS), plays a role in normal cellular growth, differentiation and development. The oncogene-derived protein (ONCOGENE PROTEIN P21(RAS)) can play a role in aberrant cellular regulation during neoplastic cell transformation (CELL TRANSFORMATION, NEOPLASTIC). This enzyme was formerly listed as EC 3.6.1.47.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
A class of monomeric, low molecular weight (20-25 kDa) GTP-binding proteins that regulate a variety of intracellular processes. The GTP bound form of the protein is active and limited by its inherent GTPase activity, which is controlled by an array of GTPase activators, GDP dissociation inhibitors, and guanine nucleotide exchange factors. This enzyme was formerly listed as EC 3.6.1.47
A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in transport from the cell membrane to early endosomes. This enzyme was formerly listed as EC 3.6.1.47.
Naphthalene derivatives carrying one or more hydroxyl (-OH) groups at any ring position. They are often used in dyes and pigments, as antioxidants for rubber, fats, and oils, as insecticides, in pharmaceuticals, and in numerous other applications.
Organic compounds which contain P-C-P bonds, where P stands for phosphonates or phosphonic acids. These compounds affect calcium metabolism. They inhibit ectopic calcification and slow down bone resorption and bone turnover. Technetium complexes of diphosphonates have been used successfully as bone scanning agents.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Cellular proteins encoded by the H-ras, K-ras and N-ras genes. The proteins have GTPase activity and are involved in signal transduction as monomeric GTP-binding proteins. Elevated levels of p21 c-ras have been associated with neoplasia. This enzyme was formerly listed as EC 3.6.1.47.
Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
A large family of MONOMERIC GTP-BINDING PROTEINS that are involved in regulation of actin organization, gene expression and cell cycle progression. This enzyme was formerly listed as EC 3.6.1.47.
A plant genus of the family FABACEAE.
A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC 3.6.1.47.
The five-carbon building blocks of TERPENES that derive from MEVALONIC ACID or deoxyxylulose phosphate.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Sesquiterpenes are a class of terpenes consisting of three isoprene units, forming a 15-carbon skeleton, which can be found in various plant essential oils and are known for their diverse chemical structures and biological activities, including anti-inflammatory, antimicrobial, and cytotoxic properties.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
A class of compounds composed of repeating 5-carbon units of HEMITERPENES.
A defective virus, containing particles of RNA nucleoprotein in virion-like form, present in patients with acute hepatitis B and chronic hepatitis. It requires the presence of a hepadnavirus for full replication. This is the lone species in the genus Deltavirus.
A cyclic nucleotide phosphodiesterase subfamily that is activated by the binding of CYCLIC GMP to an allosteric domain found on the enzyme. Multiple enzyme variants of this subtype can be produced due to multiple alternative mRNA splicing. The subfamily is expressed in a broad variety of tissues and may play a role in mediating cross-talk between CYCLIC GMP and CYCLIC CMP pathways. Although the type 2 enzymes are classified as 3',5'-cyclic-AMP phosphodiesterases (EC 3.1.4.17), members of this class have additional specificity for CYCLIC GMP.
A derivative of LOVASTATIN and potent competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HYDROXYMETHYLGLUTARYL COA REDUCTASES), which is the rate-limiting enzyme in cholesterol biosynthesis. It may also interfere with steroid hormone production. Due to the induction of hepatic LDL RECEPTORS, it increases breakdown of LDL CHOLESTEROL.
Transforming protein encoded by ras oncogenes. Point mutations in the cellular ras gene (c-ras) can also result in a mutant p21 protein that can transform mammalian cells. Oncogene protein p21(ras) has been directly implicated in human neoplasms, perhaps accounting for as much as 15-20% of all human tumors. This enzyme was formerly listed as EC 3.6.1.47.
Addition of hydrogen to a compound, especially to an unsaturated fat or fatty acid. (From Stedman, 26th ed)
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.
Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.
A sulfur-containing essential L-amino acid that is important in many body functions.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
A genetically related subfamily of RAP GTP-BINDING PROTEINS that share homology with RAS PROTEINS. They bind to Ras effectors but do not activate them, therefore they may antagonize the effects of RAS PROTEINS. This enzyme was formerly listed as EC 3.6.1.47.
INFLAMMATION of the LIVER in humans caused by HEPATITIS DELTA VIRUS, a defective RNA virus that can only infect HEPATITIS B patients. For its viral coating, hepatitis delta virus requires the HEPATITIS B SURFACE ANTIGENS produced by these patients. Hepatitis D can occur either concomitantly with (coinfection) or subsequent to (superinfection) hepatitis B infection. Similar to hepatitis B, it is primarily transmitted by parenteral exposure, such as transfusion of contaminated blood or blood products, but can also be transmitted via sexual or intimate personal contact.
Inorganic salts of phosphoric acid that contain two phosphate groups.
An abnormal congenital condition, associated with defects in the LAMIN TYPE A gene, which is characterized by premature aging in children, where all the changes of cell senescence occur. It is manifested by premature greying; hair loss; hearing loss (DEAFNESS); cataracts (CATARACT); ARTHRITIS; OSTEOPOROSIS; DIABETES MELLITUS; atrophy of subcutaneous fat; skeletal hypoplasia; elevated urinary HYALURONIC ACID; and accelerated ATHEROSCLEROSIS. Many affected individuals develop malignant tumors, especially SARCOMA.
A hard, brittle, grayish-white rare earth metal with an atomic symbol Ru, atomic number 44, and atomic weight 101.07. It is used as a catalyst and hardener for PLATINUM and PALLADIUM.
Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1.
A subcategory of guanine nucleotide dissociation inhibitors that are specific for RHO GTP-BINDING PROTEINS.
BENZOIC ACID amides.
A common saturated fatty acid found in fats and waxes including olive oil, palm oil, and body lipids.
A guanine nucleotide containing two phosphate groups esterified to the sugar moiety.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Compounds that contain a 1-dimethylaminonaphthalene-5-sulfonyl group.
Heterotrimeric GTP-binding protein subunits that tightly associate with GTP-BINDING PROTEIN BETA SUBUNITS. A dimer of beta and gamma subunits is formed when the GTP-BINDING PROTEIN ALPHA SUBUNIT dissociates from the GTP-binding protein heterotrimeric complex. The beta-gamma dimer can play an important role in signal transduction by interacting with a variety of second messengers.
Established cell cultures that have the potential to propagate indefinitely.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.
Family of retrovirus-associated DNA sequences (ras) originally isolated from Harvey (H-ras, Ha-ras, rasH) and Kirsten (K-ras, Ki-ras, rasK) murine sarcoma viruses. Ras genes are widely conserved among animal species and sequences corresponding to both H-ras and K-ras genes have been detected in human, avian, murine, and non-vertebrate genomes. The closely related N-ras gene has been detected in human neuroblastoma and sarcoma cell lines. All genes of the family have a similar exon-intron structure and each encodes a p21 protein.
The addition of an organic acid radical into a molecule.
Compounds containing 1,3-diazole, a five membered aromatic ring containing two nitrogen atoms separated by one of the carbons. Chemically reduced ones include IMIDAZOLINES and IMIDAZOLIDINES. Distinguish from 1,2-diazole (PYRAZOLES).
A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OXIDASE. This enzyme was formerly listed as EC 3.6.1.47.

Therapy of breast cancer with molecular targeting agents. (1/167)

Invasive breast cancer is a heterogeneous disease sustained by intercorrelated and complex growth pathways. Classically, human breast carcinoma has been classified for therapeutic purposes in two distinct categories: one hormone-correlated, the other hormone-uncorrelated. However, the recent advancements of the technology applied to molecular biology by genomic and proteomic analyses have suggested that many more factors are involved in breast cancer growth and progression and that some clusters of these distinguish subgroups of patients at different prognosis. The knowledge of the diversities between tumor and normal tissue of origin is the key to identify novel targets for new selective therapeutic strategies. In fact, the principal goal of molecular-targeted therapy is the suppression of the transformed phenotype minimally affecting normal cells. This review focuses on the molecular targeting compounds directed against the known molecular pathways involved in breast cancer such as: type I growth factors (HER-2/neu; epidermal growth factor receptor [EGFR]), angiogenesis, cyclooxigenase-2 (COX-2) and farnesylation. Presently, trastuzumab is the first agent approved for therapy of HER-2/neu overexpressing tumors. Several other compounds directed against different targets have entered clinical evaluation and the preliminary results are here presented and commented. The major challenges on the clinical development of targeted therapy include the proper selection of patients, the identification of the optimal dosage and schedule of administration, the combinations with conventional treatments and the more appropriate therapeutic strategy.  (+info)

A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: overproduction, purification and biochemical characterization. (2/167)

A putative prenyltransferase gene, Afu3g12930, was identified in the genome sequence of Aspergillus fumigatus. EAL92290, encoded by Afu3g12930, consists of 472 aa, with a molecular mass of about 53 kDa. The coding sequence of Afu3g12930 was cloned in pQE60, and overexpressed in Escherichia coli. The soluble His(6)-fusion protein was purified to apparent homogeneity, and characterized biochemically. The enzyme was found to catalyse the prenylation of Trp at the C-7 position of the indole moiety, in the presence of dimethylallyl diphosphate (DMAPP); therefore, it functions as a 7-dimethylallyltryptophan synthase (7-DMATS). The structure of the enzymic product was elucidated by NMR and MS analysis. K(m) values were 67 microM for DMAPP, and 137 microM for l-Trp. Geranyl diphosphate was not accepted as prenyl donor, while Trp-containing dipeptides were found to be aromatic substrates of 7-DMATS. 7-DMATS did not need divalent metal ions for its enzymic reaction, although Ca(2+) enhanced the reaction velocity slightly. The enzyme is the second dimethylallyltryptophan synthase identified in A. fumigatus. Interestingly, it shares a sequence identity of only 31 % at the amino acid level with another known dimethylallyltryptophan synthase, FgaPT2, from the same fungus; FgaPT2 prenylates l-Trp at the C-4 position of the indole ring. Afu3g12930 belongs to a putative biosynthetic gene cluster consisting of eight genes. Orthologous clusters were also identified in the genome sequences of Neosartorya fischeri and Aspergillus terreus. The putative roles of the genes in the cluster are discussed.  (+info)

Selective inhibition of growth of tuberous sclerosis complex 2 null cells by atorvastatin is associated with impaired Rheb and Rho GTPase function and reduced mTOR/S6 kinase activity. (3/167)

Inactivating mutations in the tuberous sclerosis complex 2 (TSC2) gene, which encodes tuberin, result in the development of TSC and lymphangioleiomyomatosis (LAM). The tumor suppressor effect of tuberin lies in its GTPase-activating protein activity toward Ras homologue enriched in brain (Rheb), a Ras GTPase superfamily member. The statins, 3-hydroxy-3-methylglutaryl CoA reductase inhibitors, have pleiotropic effects which may involve interference with the isoprenylation of Ras and Rho GTPases. We show that atorvastatin selectively inhibits the proliferation of Tsc2-/- mouse embryo fibroblasts and ELT-3 smooth muscle cells in response to serum and estrogen, and under serum-free conditions. The isoprenoids farnesylpyrophosphate (FPP) and geranylgeranylpyrophosphate (GGPP) significantly reverse atorvastatin-induced inhibition of Tsc2-/- cell growth, suggesting that atorvastatin dually targets a farnesylated protein, such as Rheb, and a geranylgeranylated protein, such as Rho, both of which have elevated activity in Tsc2-/- cells. Atorvastatin reduced Rheb isoprenylation, GTP loading, and membrane localization. Atorvastatin also inhibited the constitutive phosphorylation of mammalian target of rapamycin, S6 kinase, and S6 found in Tsc2-/- cells in an FPP-reversible manner and attenuated the high levels of phosphorylated S6 in Tsc2-heterozygous mice. Atorvastatin, but not rapamycin, attenuated the increased levels of activated RhoA in Tsc2-/- cells, and this was reversed by GGPP. These results suggest that atorvastatin may inhibit both rapamycin-sensitive and rapamycin-insensitive mechanisms of tuberin-null cell growth, likely via Rheb and Rho inhibition, respectively. Atorvastatin may have potential therapeutic benefit in TSC syndromes, including LAM.  (+info)

Geranylgeranylation but not GTP loading determines rho migratory function in T cells. (4/167)

Rho GTPases orchestrate signaling pathways leading to cell migration. Their function depends on GTP loading and isoprenylation by geranylgeranyl pyrophosphate (GGpp). In this study, we show that in human T cells, geranylgeranylation-and not GTP loading-is necessary for RhoA-mediated downstream events. As a result of GGpp depletion with the 3-hydroxy-3-methylglutaryl-CoA reductase inhibitor atorvastatin, RhoA was sequestered from the membrane to the cytosol and, notwithstanding increased GTP loading, the constitutive activation of its substrate Rho-associated coiled-coil protein kinase-1 was blocked. In line with this, T cells expressing increased GTP-RhoA failed to form an intact cytoskeleton and to migrate toward a chemokine gradient. In vivo treatment with atorvastatin in the rodent model of multiple sclerosis markedly decreased the capacity of activated T cells to traffic within the brain, as demonstrated by multiphoton analysis. Thus, tethering of RhoA to the membrane by GGpp is determinant for T cell migration and provides a mechanism for preventing T cell infiltration into inflamed compartments by 3-hydroxy-3-methylglutaryl-CoA reductase inhibitors.  (+info)

Prenylated anthraquinones and other constituents from the seeds of Vismia laurentii. (5/167)

Two new prenylated anthraquinones, laurenquinone A (1) and B (2) were isolated from the seeds of Vismia laurentii together with four known compounds; xanthone V(1) (3), physcion (4), 3-geranyloxyemodin anthrone (5) and friedelin (6). The structures of the new metabolites were determined with the help of spectroscopic data including extensive 2D-NMR spectroscopy. The known compounds were identified by comparison of their physical and spectroscopic data with those reported in the literature. Compounds 1, 4 and 5 exhibited moderate algicidal activity against Chlorella fusca and 3 showed moderate activity against the gram-positive bacterium Bacillus megaterium.  (+info)

Voltage-dependent dynamic FRET signals from the transverse tubules in mammalian skeletal muscle fibers. (6/167)

Two hybrid voltage-sensing systems based on fluorescence resonance energy transfer (FRET) were used to record membrane potential changes in the transverse tubular system (TTS) and surface membranes of adult mice skeletal muscle fibers. Farnesylated EGFP or ECFP (EGFP-F and ECFP-F) were used as immobile FRET donors, and either non-fluorescent (dipicrylamine [DPA]) or fluorescent (oxonol dye DiBAC(4)(5)) lipophilic anions were used as mobile energy acceptors. Flexor digitorum brevis (FDB) muscles were transfected by in vivo electroporation with pEGFP-F and pECFP-F. Farnesylated fluorescent proteins were efficiently expressed in the TTS and surface membranes. Voltage-dependent optical signals resulting from resonance energy transfer from fluorescent proteins to DPA were named QRET transients, to distinguish them from FRET transients recorded using DiBAC(4)(5). The peak DeltaF/F of QRET transients elicited by action potential stimulation is twice larger in fibers expressing ECFP-F as those with EGFP-F (7.1% vs. 3.6%). These data provide a unique experimental demonstration of the importance of the spectral overlap in FRET. The voltage sensitivity of QRET and FRET signals was demonstrated to correspond to the voltage-dependent translocation of the charged acceptors, which manifest as nonlinear components in current records. For DPA, both electrical and QRET data were predicted by radial cable model simulations in which the maximal time constant of charge translocation was 0.6 ms. FRET signals recorded in response to action potentials in fibers stained with DiBAC(4)(5) exhibit DeltaF/F amplitudes as large as 28%, but their rising phase was slower than those of QRET signals. Model simulations require a time constant for charge translocation of 1.6 ms in order to predict current and FRET data. Our results provide the basis for the potential use of lipophilic ions as tools to test for fast voltage-dependent conformational changes of membrane proteins in the TTS.  (+info)

Iridium-catalyzed hydrocarboxylation of 1,1-dimethylallene: byproduct-free reverse prenylation of carboxylic acids. (7/167)

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Oxidation of guanine in G, GG, and GGG sequence contexts by aromatic pyrenyl radical cations and carbonate radical anions: relationship between kinetics and distribution of alkali-labile lesions. (8/167)

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Protein prenylation is a post-translational modification process in which a lipophilic group, such as a farnesyl or geranylgeranyl moiety, is covalently attached to specific cysteine residues near the carboxy-terminus of proteins. This modification plays a crucial role in membrane targeting and protein-protein interactions, particularly for proteins involved in signal transduction pathways, such as Ras family GTPases. The enzymes responsible for prenylation are called protein prenyltransferases, and their dysfunction has been implicated in various diseases, including cancer and neurodegenerative disorders.

Prenylation is a post-translational modification process in which a prenyl group, such as a farnesyl or geranylgeranyl group, is added to a protein covalently. This modification typically occurs at a cysteine residue within a CAAX motif (C is cysteine, A is an aliphatic amino acid, and X is any amino acid) found at the carboxyl-terminus of the protein. Prenylation plays a crucial role in membrane association, protein-protein interactions, and intracellular trafficking of proteins, particularly those involved in signal transduction pathways.

Alkyl and aryl transferases are a group of enzymes that catalyze the transfer of alkyl or aryl groups from one molecule to another. These enzymes play a role in various biological processes, including the metabolism of drugs and other xenobiotics, as well as the biosynthesis of certain natural compounds.

Alkyl transferases typically catalyze the transfer of methyl or ethyl groups, while aryl transferases transfer larger aromatic rings. These enzymes often use cofactors such as S-adenosylmethionine (SAM) or acetyl-CoA to donate the alkyl or aryl group to a recipient molecule.

Examples of alkyl and aryl transferases include:

1. Methyltransferases: enzymes that transfer methyl groups from SAM to various acceptor molecules, such as DNA, RNA, proteins, and small molecules.
2. Histone methyltransferases: enzymes that methylate specific residues on histone proteins, which can affect chromatin structure and gene expression.
3. N-acyltransferases: enzymes that transfer acetyl or other acyl groups to amino groups in proteins or small molecules.
4. O-acyltransferases: enzymes that transfer acyl groups to hydroxyl groups in lipids, steroids, and other molecules.
5. Arylsulfatases: enzymes that remove sulfate groups from aromatic rings, releasing an alcohol and sulfate.
6. Glutathione S-transferases (GSTs): enzymes that transfer the tripeptide glutathione to electrophilic centers in xenobiotics and endogenous compounds, facilitating their detoxification and excretion.

Dimethylallyltranstransferase (DMAT) is an enzyme that plays a crucial role in the biosynthesis of various natural compounds, including terpenoids and alkaloids. These compounds have diverse functions in nature, ranging from serving as pigments and fragrances to acting as defense mechanisms against predators or pathogens.

The primary function of DMAT is to catalyze the head-to-tail condensation of dimethylallyl pyrophosphate (DMAPP) with various diphosphate-bound prenyl substrates, forming prenylated products. This reaction represents the first committed step in the biosynthesis of many terpenoids and alkaloids.

The enzyme's catalytic mechanism involves the formation of a covalent bond between the pyrophosphate group of DMAPP and a conserved cysteine residue within the DMAT active site, followed by the transfer of the dimethylallyl moiety to the diphosphate-bound prenyl substrate.

DMAT is found in various organisms, including bacteria, fungi, plants, and animals. In humans, DMAT is involved in the biosynthesis of steroids, which are essential components of cell membranes and precursors to important hormones such as cortisol, aldosterone, and sex hormones.

In summary, dimethylallyltranstransferase (DMAT) is an enzyme that catalyzes the condensation of dimethylallyl pyrophosphate (DMAPP) with various prenyl substrates, playing a critical role in the biosynthesis of diverse natural compounds, including terpenoids and alkaloids.

Farnesyltranstransferase (FTase) is an enzyme that plays a role in the post-translational modification of proteins, specifically by adding a farnesyl group to certain protein substrates. This process, known as farnesylation, is essential for the proper localization and function of many proteins, including Ras family GTPases, which are involved in signal transduction pathways that regulate cell growth, differentiation, and survival.

FTase catalyzes the transfer of a farnesyl group from farnesyl pyrophosphate (FPP) to a cysteine residue near the C-terminus of its protein substrates. This modification allows the protein to interact with membranes and other cellular structures, which is critical for their function. Inhibitors of FTase have been developed as potential therapeutic agents for cancer and other diseases associated with aberrant Ras signaling.

Mevalonic acid is not a term that is typically used in medical definitions, but rather it is a biochemical concept. Mevalonic acid is a key intermediate in the biosynthetic pathway for cholesterol and other isoprenoids. It is formed from 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) by the enzyme HMG-CoA reductase, which is the target of cholesterol-lowering drugs known as statins.

In a medical context, mevalonic acid may be mentioned in relation to certain rare genetic disorders, such as mevalonate kinase deficiency (MKD) or hyperimmunoglobulinemia D and periodic fever syndrome (HIDS), which are caused by mutations in the gene encoding mevalonate kinase, an enzyme involved in the metabolism of mevalonic acid. These conditions can cause recurrent fevers, rashes, joint pain, and other symptoms.

Polyisoprenyl phosphates are a type of organic compound that play a crucial role in the biosynthesis of various essential biomolecules in cells. They are formed by the addition of isoprene units, which are five-carbon molecules with a branched structure, to a phosphate group.

In medical terms, polyisoprenyl phosphates are primarily known for their role as intermediates in the biosynthesis of dolichols and farnesylated proteins. Dolichols are long-chain isoprenoids that function as lipid carriers in the synthesis of glycoproteins, which are proteins that contain carbohydrate groups attached to them. Farnesylated proteins, on the other hand, are proteins that have been modified with a farnesyl group, which is a 15-carbon isoprenoid. This modification plays a role in the localization and function of certain proteins within the cell.

Abnormalities in the biosynthesis of polyisoprenyl phosphates and their downstream products have been implicated in various diseases, including cancer, neurological disorders, and genetic syndromes. Therefore, understanding the biology and regulation of these compounds is an active area of research with potential therapeutic implications.

Farnesol is a chemical compound classified as a sesquiterpene alcohol. It is produced by various plants and insects, including certain types of roses and citrus fruits, and plays a role in their natural defense mechanisms. Farnesol has a variety of uses in the perfume industry due to its pleasant, floral scent.

In addition to its natural occurrence, farnesol is also synthetically produced for use in various applications, including as a fragrance ingredient and as an antimicrobial agent in cosmetics and personal care products. It has been shown to have antibacterial and antifungal properties, making it useful for preventing the growth of microorganisms in these products.

Farnesol is not typically used as a medication or therapeutic agent in humans, but it may have potential uses in the treatment of certain medical conditions due to its antimicrobial and anti-inflammatory properties. However, more research is needed to fully understand its effects and safety profile in these contexts.

Transferases are a class of enzymes that facilitate the transfer of specific functional groups (like methyl, acetyl, or phosphate groups) from one molecule (the donor) to another (the acceptor). This transfer of a chemical group can alter the physical or chemical properties of the acceptor molecule and is a crucial process in various metabolic pathways. Transferases play essential roles in numerous biological processes, such as biosynthesis, detoxification, and catabolism.

The classification of transferases is based on the type of functional group they transfer:

1. Methyltransferases - transfer a methyl group (-CH3)
2. Acetyltransferases - transfer an acetyl group (-COCH3)
3. Aminotransferases or Transaminases - transfer an amino group (-NH2 or -NHR, where R is a hydrogen atom or a carbon-containing group)
4. Glycosyltransferases - transfer a sugar moiety (a glycosyl group)
5. Phosphotransferases - transfer a phosphate group (-PO3H2)
6. Sulfotransferases - transfer a sulfo group (-SO3H)
7. Acyltransferases - transfer an acyl group (a fatty acid or similar molecule)

These enzymes are identified and named according to the systematic nomenclature of enzymes developed by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB). The naming convention includes the class of enzyme, the specific group being transferred, and the molecules involved in the transfer reaction. For example, the enzyme that transfers a phosphate group from ATP to glucose is named "glucokinase."

Choroideremia is a rare inherited eye disorder that causes progressive loss of vision. It primarily affects the choroid, which is the layer of blood vessels that provides oxygen and nutrients to the outer layers of the retina. The disease also damages the retina and the optic nerve over time.

The condition is caused by mutations in the CHM gene, which provides instructions for making a protein called REP-1 that is essential for maintaining the health of the light-sensitive cells in the retina (rods and cones). Without this protein, these cells gradually deteriorate and die, leading to vision loss.

Choroideremia typically affects males more severely than females, and it usually begins in childhood with night blindness (nyctalopia) and decreased visual acuity. Over time, the field of vision becomes narrower (tunnel vision), and eventually, complete blindness can occur. Currently, there is no cure for choroideremia, but research is ongoing to develop potential treatments such as gene therapy.

Lovastatin is a medication that belongs to a class of drugs called statins, which are used to lower cholesterol levels in the blood. It works by inhibiting HMG-CoA reductase, an enzyme that plays a crucial role in the production of cholesterol in the body. By reducing the amount of cholesterol produced in the liver, lovastatin helps to decrease the levels of low-density lipoprotein (LDL) or "bad" cholesterol and triglycerides in the blood, while increasing the levels of high-density lipoprotein (HDL) or "good" cholesterol.

Lovastatin is available in both immediate-release and extended-release forms, and it is typically taken orally once or twice a day, depending on the dosage prescribed by a healthcare provider. Common side effects of lovastatin include headache, nausea, diarrhea, and muscle pain, although more serious side effects such as liver damage and muscle weakness are possible, particularly at higher doses.

It is important to note that lovastatin should not be taken by individuals with active liver disease or by those who are pregnant or breastfeeding. Additionally, it may interact with certain other medications, so it is essential to inform a healthcare provider of all medications being taken before starting lovastatin therapy.

Rab GTP-binding proteins, also known as Rab GTPases or simply Rabs, are a large family of small GTP-binding proteins that play a crucial role in regulating intracellular vesicle trafficking. They function as molecular switches that cycle between an active GTP-bound state and an inactive GDP-bound state.

In the active state, Rab proteins interact with various effector molecules to mediate specific membrane trafficking events such as vesicle budding, transport, tethering, and fusion. Each Rab protein is thought to have a unique function and localize to specific intracellular compartments or membranes, where they regulate the transport of vesicles and organelles within the cell.

Rab proteins are involved in several important cellular processes, including endocytosis, exocytosis, Golgi apparatus function, autophagy, and intracellular signaling. Dysregulation of Rab GTP-binding proteins has been implicated in various human diseases, such as cancer, neurodegenerative disorders, and infectious diseases.

Diterpenes are a class of naturally occurring compounds that are composed of four isoprene units, which is a type of hydrocarbon. They are synthesized by a wide variety of plants and animals, and are found in many different types of organisms, including fungi, insects, and marine organisms.

Diterpenes have a variety of biological activities and are used in medicine for their therapeutic effects. Some diterpenes have anti-inflammatory, antimicrobial, and antiviral properties, and are used to treat a range of conditions, including respiratory infections, skin disorders, and cancer.

Diterpenes can be further classified into different subgroups based on their chemical structure and biological activity. Some examples of diterpenes include the phytocannabinoids found in cannabis plants, such as THC and CBD, and the paclitaxel, a diterpene found in the bark of the Pacific yew tree that is used to treat cancer.

It's important to note that while some diterpenes have therapeutic potential, others may be toxic or have adverse effects, so it is essential to use them under the guidance and supervision of a healthcare professional.

RhoB GTP-binding protein is a member of the Rho family of small GTPases, which are involved in regulating various cellular processes such as actin cytoskeleton organization, gene expression, and cell cycle progression. Specifically, RhoB functions as a molecular switch that cycles between an inactive GDP-bound state and an active GTP-bound state.

When RhoB is activated by GTP binding, it interacts with various downstream effectors to regulate the dynamics of the actin cytoskeleton, which is important for cell motility, adhesion, and membrane trafficking. RhoB has been implicated in several physiological processes, including angiogenesis, wound healing, and immune response.

RhoB is unique among the Rho GTPases because it can be localized to both the plasma membrane and endosomal compartments, allowing it to regulate various cellular processes in different subcellular locations. Dysregulation of RhoB has been associated with various pathological conditions, including cancer, inflammation, and neurodegenerative diseases.

Alkadienes are organic compounds that contain two carbon-carbon double bonds in their molecular structure. The term "alka" refers to the presence of hydrocarbons, while "diene" indicates the presence of two double bonds. These compounds can be classified as either conjugated or non-conjugated dienes based on the arrangement of the double bonds.

Conjugated dienes have their double bonds adjacent to each other, separated by a single bond, while non-conjugated dienes have at least one methylene group (-CH2-) separating the double bonds. The presence and positioning of these double bonds can significantly affect the chemical and physical properties of alkadienes, including their reactivity, stability, and spectral characteristics.

Alkadienes are important intermediates in various chemical reactions and have applications in the production of polymers, pharmaceuticals, and other industrial products. However, they can also be produced naturally by some plants and microorganisms as part of their metabolic processes.

Geranyltranstransferase is not a commonly used medical term, but it is a type of enzyme involved in the biosynthesis of various compounds in the body. According to biochemistry and molecular biology resources, Geranyltranstransferase (GTT) is an enzyme that catalyzes the head-to-tail condensation of geranyl diphosphate with isopentenyl diphosphate to form farnesyl diphosphate.

Farnesyl diphosphate is a key intermediate in the biosynthesis of steroids, sesquiterpenes, and other isoprenoid compounds. These compounds have diverse functions in the body, including serving as components of cell membranes, hormones, and signaling molecules.

In summary, Geranyltranstransferase is a biochemical term that refers to an enzyme involved in the biosynthesis of various isoprenoid compounds through the condensation of geranyl diphosphate with isopentenyl diphosphate.

'Claviceps' is a genus of filamentous fungi that are commonly known as ergots. These fungi infect the grasses and grains in the family Poaceae, which includes important crop plants such as wheat, rye, barley, and corn. The most well-known species in this genus is Claviceps purpurea, which causes a disease called ergotism in humans and animals that consume contaminated grains.

Ergotism is a serious condition that can cause a range of symptoms, including convulsions, hallucinations, gangrene, and death. The fungus produces alkaloids that can affect the nervous system and blood vessels, leading to these symptoms. Historically, ergotism was a significant public health problem in Europe, where it was known as "St. Anthony's Fire" because of the burning sensations it caused in the limbs.

Today, ergotism is rare thanks to improved grain storage and monitoring practices. However, Claviceps species continue to be important in agriculture and medicine. Some of the alkaloids produced by these fungi have been used in pharmaceuticals to treat conditions such as migraines and Parkinson's disease.

Guanine Nucleotide Dissociation Inhibitors (GDI) are a group of proteins that bind to and inhibit the dissociation of guanine nucleotides from small GTPases, which are important regulatory molecules involved in various cellular processes such as signal transduction, vesicle trafficking, and cytoskeleton organization.

GDI's function is to maintain these small GTPases in their inactive state by keeping them bound to guanine nucleotides, specifically GDP (guanosine diphosphate). By doing so, GDIs help regulate the activity of small GTPases and control their subcellular localization.

GDIs have been identified in various organisms, including bacteria, yeast, and mammals. In humans, there are two major types of GDIs: RhoGDI (also known as D4-GDI) and RacGDI (also known as GDI-α). These GDIs play crucial roles in regulating the activity of Rho family GTPases, which are involved in various cellular functions such as cell motility, membrane trafficking, and gene expression.

Overall, Guanine Nucleotide Dissociation Inhibitors are essential regulators of small GTPases, controlling their activity and localization to ensure proper cellular function.

Iridium is not a medical term, but rather a chemical element with the symbol Ir and atomic number 77. It's a transition metal that is part of the platinum group. Iridium has no known biological role in humans or other organisms, and it is not used in medical treatments or diagnoses.

However, iridium is sometimes mentioned in the context of geological time scales because iridium-rich layers in rock formations are associated with major extinction events, such as the one that marked the end of the Cretaceous period 65 million years ago. The leading hypothesis for this association is that large asteroid impacts can create iridium-rich vapor plumes that settle onto the Earth's surface and leave a distinct layer in the rock record.

RAB1 GTP-binding proteins are a subfamily of the RAS superfamily of small GTPases, which function as molecular switches in intracellular vesicle trafficking. RAB1 proteins exist in two forms, RAB1A and RAB1B, that bind to guanosine triphosphate (GTP) and guanosine diphosphate (GDP).

In their GTP-bound form, RAB1 proteins interact with effector molecules to regulate the formation of transport vesicles at the endoplasmic reticulum (ER) and their subsequent fusion with the cis-Golgi apparatus. This process is critical for the proper sorting and transport of proteins and lipids between the ER, Golgi, and other cellular membranes.

RAB1 proteins play a crucial role in maintaining the integrity of the early secretory pathway and have been implicated in various cellular processes, including autophagy, mitochondrial dynamics, and cytokinesis. Dysregulation of RAB1 GTP-binding proteins has been linked to several human diseases, such as cancer, neurodegenerative disorders, and infectious diseases.

Ras proteins are a group of small GTPases that play crucial roles as regulators of intracellular signaling pathways in cells. They are involved in various cellular processes, such as cell growth, differentiation, and survival. Ras proteins cycle between an inactive GDP-bound state and an active GTP-bound state to transmit signals from membrane receptors to downstream effectors. Mutations in Ras genes can lead to constitutive activation of Ras proteins, which has been implicated in various human cancers and developmental disorders.

GTP-binding proteins, also known as G proteins, are a family of molecular switches present in many organisms, including humans. They play a crucial role in signal transduction pathways, particularly those involved in cellular responses to external stimuli such as hormones, neurotransmitters, and sensory signals like light and odorants.

G proteins are composed of three subunits: α, β, and γ. The α-subunit binds GTP (guanosine triphosphate) and acts as the active component of the complex. When a G protein-coupled receptor (GPCR) is activated by an external signal, it triggers a conformational change in the associated G protein, allowing the α-subunit to exchange GDP (guanosine diphosphate) for GTP. This activation leads to dissociation of the G protein complex into the GTP-bound α-subunit and the βγ-subunit pair. Both the α-GTP and βγ subunits can then interact with downstream effectors, such as enzymes or ion channels, to propagate and amplify the signal within the cell.

The intrinsic GTPase activity of the α-subunit eventually hydrolyzes the bound GTP to GDP, which leads to re-association of the α and βγ subunits and termination of the signal. This cycle of activation and inactivation makes G proteins versatile signaling elements that can respond quickly and precisely to changing environmental conditions.

Defects in G protein-mediated signaling pathways have been implicated in various diseases, including cancer, neurological disorders, and cardiovascular diseases. Therefore, understanding the function and regulation of GTP-binding proteins is essential for developing targeted therapeutic strategies.

Monomeric GTP-binding proteins, also known as small GTPases, are a family of proteins that bind and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). These proteins function as molecular switches, cycling between an inactive GDP-bound state and an active GTP-bound state. They play crucial roles in regulating various cellular processes such as signal transduction, vesicle trafficking, cytoskeleton organization, and cell cycle progression. Examples of monomeric GTP-binding proteins include Ras, Rho, Rab, and Ran families.

Rab5 GTP-binding proteins are a subfamily of Rab (Ras-related in brain) proteins that function as molecular switches in the regulation of intracellular membrane trafficking. They play a crucial role in the early stages of endocytosis, including the formation and movement of early endosomes.

Rab5 GTP-binding proteins cycle between an active GTP-bound state and an inactive GDP-bound state. In their active form, they interact with various effector proteins to regulate vesicle transport, tethering, and fusion. Specifically, Rab5 GTP-binding proteins are involved in the homotypic fusion of early endosomes, promoting the maturation of early endosomes into late endosomes.

There are multiple isoforms of Rab5 GTP-binding proteins (Rab5A, Rab5B, and Rab5C) that share a high degree of sequence similarity but may have distinct functions in different cellular contexts. Dysregulation of Rab5 GTP-binding proteins has been implicated in various human diseases, including cancer and neurodegenerative disorders.

Naphthols are chemical compounds that consist of a naphthalene ring (a polycyclic aromatic hydrocarbon made up of two benzene rings) substituted with a hydroxyl group (-OH). They can be classified as primary or secondary naphthols, depending on whether the hydroxyl group is directly attached to the naphthalene ring (primary) or attached through a carbon atom (secondary). Naphthols are important intermediates in the synthesis of various chemical and pharmaceutical products. They have been used in the production of azo dyes, antioxidants, and pharmaceuticals such as analgesics and anti-inflammatory agents.

Diphosphonates are a class of medications that are used to treat bone diseases, such as osteoporosis and Paget's disease. They work by binding to the surface of bones and inhibiting the activity of bone-resorbing cells called osteoclasts. This helps to slow down the breakdown and loss of bone tissue, which can help to reduce the risk of fractures.

Diphosphonates are typically taken orally in the form of tablets, but some forms may be given by injection. Commonly prescribed diphosphonates include alendronate (Fosamax), risedronate (Actonel), and ibandronate (Boniva). Side effects of diphosphonates can include gastrointestinal symptoms such as nausea, heartburn, and abdominal pain. In rare cases, they may also cause esophageal ulcers or osteonecrosis of the jaw.

It is important to follow the instructions for taking diphosphonates carefully, as they must be taken on an empty stomach with a full glass of water and the patient must remain upright for at least 30 minutes after taking the medication to reduce the risk of esophageal irritation. Regular monitoring of bone density and kidney function is also recommended while taking these medications.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Hydroxymethylglutaryl-CoA (HMG-CoA) reductase inhibitors, also known as statins, are a class of cholesterol-lowering medications. They work by inhibiting the enzyme HMG-CoA reductase, which plays a central role in the production of cholesterol in the liver. By blocking this enzyme, the liver is stimulated to take up more low-density lipoprotein (LDL) cholesterol from the bloodstream, leading to a decrease in LDL cholesterol levels and a reduced risk of cardiovascular disease.

Examples of HMG-CoA reductase inhibitors include atorvastatin, simvastatin, pravastatin, rosuvastatin, and fluvastatin. These medications are commonly prescribed to individuals with high cholesterol levels, particularly those who are at risk for or have established cardiovascular disease.

It's important to note that while HMG-CoA reductase inhibitors can be effective in reducing LDL cholesterol levels and the risk of cardiovascular events, they should be used as part of a comprehensive approach to managing high cholesterol, which may also include lifestyle modifications such as dietary changes, exercise, and weight management.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

Rho GTP-binding proteins are a subfamily of the Ras superfamily of small GTPases, which function as molecular switches in various cellular signaling pathways. These proteins play crucial roles in regulating diverse cellular processes such as actin cytoskeleton dynamics, gene expression, cell cycle progression, and cell migration.

Rho GTP-binding proteins cycle between an active GTP-bound state and an inactive GDP-bound state. In the active state, they interact with various downstream effectors to regulate their respective cellular functions. Guanine nucleotide exchange factors (GEFs) activate Rho GTP-binding proteins by promoting the exchange of GDP for GTP, while GTPase-activating proteins (GAPs) inactivate them by enhancing their intrinsic GTP hydrolysis activity.

There are several members of the Rho GTP-binding protein family, including RhoA, RhoB, RhoC, Rac1, Rac2, Rac3, Cdc42, and Rnd proteins, each with distinct functions and downstream effectors. Dysregulation of Rho GTP-binding proteins has been implicated in various human diseases, including cancer, cardiovascular disease, neurological disorders, and inflammatory diseases.

"Sophora" does not have a specific medical definition, but it is a term that refers to various species of the Sophora plant genus, which belongs to the Fabaceae (legume) family. Some of these plants have been used in traditional medicine in different cultures.

For instance, Sophora flavescens (Ku Shen) has been used in Traditional Chinese Medicine for its anti-inflammatory, antiviral, and antipyretic properties. It contains several alkaloids, such as matrine and oxymatrine, which have demonstrated pharmacological activities.

Another example is Sophora japonica (Japanese pagoda tree), whose seeds, leaves, and bark have been used in traditional Chinese medicine for treating various conditions like diarrhea, insomnia, and skin diseases. Its active compounds include flavonoids, saponins, and alkaloids, which contribute to its medicinal properties.

It is essential to note that the use of Sophora species or their extracts in a medical context should be based on scientific research and under professional medical supervision due to potential side effects and interactions with other medications.

RhoA (Ras Homolog Family Member A) is a small GTPase protein that acts as a molecular switch, cycling between an inactive GDP-bound state and an active GTP-bound state. It plays a crucial role in regulating various cellular processes such as actin cytoskeleton organization, gene expression, cell cycle progression, and cell migration.

RhoA GTP-binding protein becomes activated when it binds to GTP, and this activation leads to the recruitment of downstream effectors that mediate its functions. The activity of RhoA is tightly regulated by several proteins, including guanine nucleotide exchange factors (GEFs) that promote the exchange of GDP for GTP, GTPase-activating proteins (GAPs) that stimulate the intrinsic GTPase activity of RhoA to hydrolyze GTP to GDP and return it to an inactive state, and guanine nucleotide dissociation inhibitors (GDIs) that sequester RhoA in the cytoplasm and prevent its association with the membrane.

Mutations or dysregulation of RhoA GTP-binding protein have been implicated in various human diseases, including cancer, neurological disorders, and cardiovascular diseases.

I'm sorry for any confusion, but "Hemiterpenes" is not a recognized term in medical or biochemistry terminology. The term "terpene" does refer to a large class of naturally occurring organic hydrocarbons, which are synthesized in various plants and animals. They are built from repeating units of isoprene (a five-carbon molecule), and can be further classified into monoterpenes (two isoprene units), sesquiterpenes (three isoprene units), diterpenes (four isoprene units), and so on.

However, the prefix "hemi-" means "half," which doesn't have a clear application in this context. It's possible there may be a misunderstanding or a typo in your question. If you meant to ask about a specific type of compound or a concept related to terpenes, please provide more context so I can give a more accurate answer.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Sesquiterpenes are a class of terpenes that consist of three isoprene units, hence the name "sesqui-" meaning "one and a half" in Latin. They are composed of 15 carbon atoms and have a wide range of chemical structures and biological activities. Sesquiterpenes can be found in various plants, fungi, and insects, and they play important roles in the defense mechanisms of these organisms. Some sesquiterpenes are also used in traditional medicine and have been studied for their potential therapeutic benefits.

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

Terpenes are a large and diverse class of organic compounds produced by a variety of plants, including cannabis. They are responsible for the distinctive aromas and flavors found in different strains of cannabis. Terpenes have been found to have various therapeutic benefits, such as anti-inflammatory, analgesic, and antimicrobial properties. Some terpenes may also enhance the psychoactive effects of THC, the main psychoactive compound in cannabis. It's important to note that more research is needed to fully understand the potential medical benefits and risks associated with terpenes.

Hepatitis Delta Virus (HDV) is not a traditional virus but rather a defective RNA particle that requires the assistance of the hepatitis B virus (HBV) to replicate. It's also known as delta agent or hepatitis D. HDV is a unique pathogen that only infects individuals who are already infected with HBV.

The virus causes a more severe form of viral hepatitis than HBV alone, leading to a higher risk of fulminant hepatitis (acute liver failure) and chronic hepatitis, which can progress to cirrhosis and hepatocellular carcinoma. HDV is primarily transmitted through percutaneous or sexual contact with infected blood or body fluids.

Prevention strategies include vaccination against HBV, which also prevents HDV infection, and avoiding high-risk behaviors such as intravenous drug use and unprotected sex with multiple partners. There is no specific treatment for HDV; however, antiviral therapy for HBV can help manage the infection.

Cyclic nucleotide phosphodiesterases (PDEs) are a family of enzymes that regulate intracellular levels of cyclic adenosine monophosphate (cAMP) and cyclic guanosine monophosphate (cGMP), which are important second messengers involved in various cellular processes.

Type 2 phosphodiesterases (PDE2) are a subtype of this family that specifically hydrolyze both cAMP and cGMP to their respective 5'-monophosphates, thereby reducing their intracellular concentrations. PDE2 enzymes are widely expressed in various tissues, including the brain, heart, and vasculature, where they play important roles in regulating signal transduction pathways.

PDE2 enzymes are composed of two regulatory subunits and one catalytic subunit, which contains the active site for phosphodiesterase activity. The regulatory subunits can bind to cGMP, leading to an increase in PDE2 activity towards both cAMP and cGMP. This unique property of PDE2 enzymes allows them to act as coincidence detectors that integrate signals from multiple second messenger pathways.

Inhibition of PDE2 has been shown to have therapeutic potential in various diseases, including cardiovascular disease, neurodegenerative disorders, and cancer. For example, PDE2 inhibitors have been shown to improve cardiac function, protect against ischemic injury, and enhance cognitive function in animal models. However, further research is needed to fully understand the therapeutic potential of PDE2 inhibition and its potential side effects.

Simvastatin is a medication that belongs to a class of drugs called statins, which are used to lower cholesterol levels in the blood. It works by inhibiting HMG-CoA reductase, an enzyme that plays a key role in the production of cholesterol in the body. By reducing the amount of cholesterol produced by the liver, simvastatin helps to lower the levels of LDL (low-density lipoprotein) or "bad" cholesterol and triglycerides in the blood, while increasing HDL (high-density lipoprotein) or "good" cholesterol.

Simvastatin is used to prevent cardiovascular diseases such as heart attacks and strokes in individuals with high cholesterol levels, particularly those who have other risk factors such as diabetes, hypertension, or a history of smoking. It is available in various strengths and forms, and is typically taken orally once a day, usually in the evening.

Like all medications, simvastatin can cause side effects, ranging from mild to severe. Common side effects include headache, muscle pain, and gastrointestinal symptoms such as nausea, constipation, or diarrhea. Rare but serious side effects may include liver damage, muscle breakdown (rhabdomyolysis), and increased risk of diabetes. It is important to follow the dosage instructions carefully and inform your healthcare provider of any pre-existing medical conditions or medications you are taking, as these may affect the safety and efficacy of simvastatin.

Hydrogenation, in the context of food science and biochemistry, refers to the process of adding hydrogen atoms to certain unsaturated fats or oils, converting them into saturated fats. This is typically done through a chemical reaction using hydrogen gas in the presence of a catalyst, often a metal such as nickel or palladium.

The process of hydrogenation increases the stability and shelf life of fats and oils, but it can also lead to the formation of trans fats, which have been linked to various health issues, including heart disease. Therefore, the use of partially hydrogenated oils has been largely phased out in many countries.

Biocatalysis is the use of living organisms or their components, such as enzymes, to accelerate chemical reactions. In other words, it is the process by which biological systems, including cells, tissues, and organs, catalyze chemical transformations. Biocatalysts, such as enzymes, can increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They are highly specific and efficient, making them valuable tools in various industries, including pharmaceuticals, food and beverage, and biofuels.

In medicine, biocatalysis is used in the production of drugs, such as antibiotics and hormones, as well as in diagnostic tests. Enzymes are also used in medical treatments, such as enzyme replacement therapy for genetic disorders that affect enzyme function. Overall, biocatalysis plays a critical role in many areas of medicine and healthcare.

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Hydroxymethylglutaryl CoA (HMG-CoA) reductase is an enzyme that plays a crucial role in the synthesis of cholesterol in the body. It is found in the endoplasmic reticulum of cells and catalyzes the conversion of HMG-CoA to mevalonic acid, which is a key rate-limiting step in the cholesterol biosynthetic pathway.

The reaction catalyzed by HMG-CoA reductase is as follows:

HMG-CoA + 2 NADPH + 2 H+ → mevalonic acid + CoA + 2 NADP+

This enzyme is the target of statin drugs, which are commonly prescribed to lower cholesterol levels in the treatment of cardiovascular diseases. Statins work by inhibiting HMG-CoA reductase, thereby reducing the production of cholesterol in the body.

GTP (Guanosine Triphosphate) Phosphohydrolases are a group of enzymes that catalyze the hydrolysis of GTP to GDP (Guanosine Diphosphate) and inorganic phosphate. This reaction plays a crucial role in regulating various cellular processes, including signal transduction pathways, protein synthesis, and vesicle trafficking.

The human genome encodes several different types of GTP Phosphohydrolases, such as GTPase-activating proteins (GAPs), GTPase effectors, and G protein-coupled receptors (GPCRs). These enzymes share a common mechanism of action, in which they utilize the energy released from GTP hydrolysis to drive conformational changes that enable them to interact with downstream effector molecules and modulate their activity.

Dysregulation of GTP Phosphohydrolases has been implicated in various human diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the structure, function, and regulation of these enzymes is essential for developing novel therapeutic strategies to target these conditions.

Methionine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. It plays a crucial role in various biological processes, including:

1. Protein synthesis: Methionine is one of the building blocks of proteins, helping to create new proteins and maintain the structure and function of cells.
2. Methylation: Methionine serves as a methyl group donor in various biochemical reactions, which are essential for DNA synthesis, gene regulation, and neurotransmitter production.
3. Antioxidant defense: Methionine can be converted to cysteine, which is involved in the formation of glutathione, a potent antioxidant that helps protect cells from oxidative damage.
4. Homocysteine metabolism: Methionine is involved in the conversion of homocysteine back to methionine through a process called remethylation, which is essential for maintaining normal homocysteine levels and preventing cardiovascular disease.
5. Fat metabolism: Methionine helps facilitate the breakdown and metabolism of fats in the body.

Foods rich in methionine include meat, fish, dairy products, eggs, and some nuts and seeds.

Amino acid motifs are recurring patterns or sequences of amino acids in a protein molecule. These motifs can be identified through various sequence analysis techniques and often have functional or structural significance. They can be as short as two amino acids in length, but typically contain at least three to five residues.

Some common examples of amino acid motifs include:

1. Active site motifs: These are specific sequences of amino acids that form the active site of an enzyme and participate in catalyzing chemical reactions. For example, the catalytic triad in serine proteases consists of three residues (serine, histidine, and aspartate) that work together to hydrolyze peptide bonds.
2. Signal peptide motifs: These are sequences of amino acids that target proteins for secretion or localization to specific organelles within the cell. For example, a typical signal peptide consists of a positively charged n-region, a hydrophobic h-region, and a polar c-region that directs the protein to the endoplasmic reticulum membrane for translocation.
3. Zinc finger motifs: These are structural domains that contain conserved sequences of amino acids that bind zinc ions and play important roles in DNA recognition and regulation of gene expression.
4. Transmembrane motifs: These are sequences of hydrophobic amino acids that span the lipid bilayer of cell membranes and anchor transmembrane proteins in place.
5. Phosphorylation sites: These are specific serine, threonine, or tyrosine residues that can be phosphorylated by protein kinases to regulate protein function.

Understanding amino acid motifs is important for predicting protein structure and function, as well as for identifying potential drug targets in disease-associated proteins.

Rap1 GTP-binding proteins are a subfamily of the Ras superfamily of small GTPases, which function as molecular switches that regulate various cellular processes, including cell growth, differentiation, and motility. Rap1 proteins cycle between an inactive GDP-bound state and an active GTP-bound state, and this cycling is regulated by guanine nucleotide exchange factors (GEFs) that promote the exchange of GDP for GTP, and GTPase-activating proteins (GAPs) that stimulate the intrinsic GTPase activity of Rap1, promoting its return to the inactive state.

Rap1 has been implicated in a variety of cellular processes, including cell adhesion, migration, and polarity, as well as cell cycle progression and transcriptional regulation. In particular, Rap1 has been shown to play important roles in the regulation of integrin-mediated adhesion and signaling, and in the control of endothelial cell barrier function. Dysregulation of Rap1 activity has been implicated in a number of human diseases, including cancer and inflammatory disorders.

Hepatitis D, also known as Delta hepatitis, is a viral infection of the liver that can only occur in people who have a current infection with the hepatitis B virus (HBV). It's caused by the hepatitis delta virus (HDV), which is a small, enveloped, single-stranded RNA virus.

HDV requires the presence of HBV for its replication and survival, so it can't infect someone who doesn't already have HBV. When both viruses are present, they can interact in ways that lead to more severe liver disease than either virus would cause alone.

Hepatitis D can be an acute or chronic infection, and it can range from mild to severe, with symptoms similar to those of other types of viral hepatitis, such as jaundice, fatigue, loss of appetite, nausea, vomiting, abdominal pain, and joint pain. In some cases, hepatitis D can lead to serious complications, including liver failure and death.

Hepatitis D is primarily spread through contact with infected blood or other bodily fluids, such as during sexual contact, sharing needles, or mother-to-child transmission during childbirth. It's preventable through vaccination against hepatitis B, which provides immunity to both viruses. There is no specific treatment for hepatitis D, but antiviral therapy for hepatitis B can help manage the infection and prevent complications.

Diphosphates, also known as pyrophosphates, are chemical compounds that contain two phosphate groups joined together by an oxygen atom. The general formula for a diphosphate is P~PO3~2-, where ~ represents a bond. Diphosphates play important roles in various biological processes, such as energy metabolism and cell signaling. In the context of nutrition, diphosphates can be found in some foods, including milk and certain vegetables.

Progeria, also known as Hutchinson-Gilford Progeria Syndrome (HGPS), is a rare and fatal genetic condition characterized by the rapid aging of children. The term "progeria" comes from the Greek words "pro," meaning prematurely, and "gereas," meaning old age.

Individuals with progeria typically appear normal at birth but begin to display signs of accelerated aging within the first two years of life. These symptoms can include growth failure, loss of body fat and hair, aged-looking skin, joint stiffness, hip dislocation, and cardiovascular disease. The most common cause of death in progeria patients is heart attack or stroke due to widespread atherosclerosis (the hardening and narrowing of the arteries).

Progeria is caused by a mutation in the LMNA gene, which provides instructions for making a protein called lamin A. This protein is essential for the structure and function of the nuclear envelope, the membrane that surrounds the cell's nucleus. The mutation leads to the production of an abnormal form of lamin A called progerin, which accumulates in cells throughout the body, causing premature aging.

There is currently no cure for progeria, and treatment is focused on managing symptoms and complications. Researchers are actively studying potential treatments that could slow or reverse the effects of the disease.

I'm sorry for any confusion, but "Ruthenium" is not a medical term. It is a chemical element with the symbol "Ru" and atomic number 44. Ruthenium is a transition metal that belongs to the platinum group. It is typically found in ores alongside other platinum group metals and is used in various industrial applications, such as electrical contacts and wear-resistant surfaces. It does not have direct relevance to medical terminology or healthcare.

Protein methyltransferases (PMTs) are a family of enzymes that transfer methyl groups from a donor, such as S-adenosylmethionine (SAM), to specific residues on protein substrates. This post-translational modification plays a crucial role in various cellular processes, including epigenetic regulation, signal transduction, and protein stability.

PMTs can methylate different amino acid residues, such as lysine, arginine, and histidine, on proteins. The methylation of these residues can lead to changes in the charge, hydrophobicity, or interaction properties of the target protein, thereby modulating its function.

For example, lysine methyltransferases (KMTs) are a subclass of PMTs that specifically methylate lysine residues on histone proteins, which are the core components of nucleosomes in chromatin. Histone methylation can either activate or repress gene transcription, depending on the specific residue and degree of methylation.

Protein arginine methyltransferases (PRMTs) are another subclass of PMTs that methylate arginine residues on various protein substrates, including histones, transcription factors, and RNA-binding proteins. Arginine methylation can also affect protein function by altering its interaction with other molecules or modulating its stability.

Overall, protein methyltransferases are essential regulators of cellular processes and have been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Therefore, understanding the mechanisms and functions of PMTs is crucial for developing novel therapeutic strategies to target these diseases.

Rho-specific guanine nucleotide dissociation inhibitors (RhoGDI) are a group of proteins that regulate the function of Rho GTPases, which are important signaling molecules involved in various cellular processes such as actin cytoskeleton regulation, gene expression, and cell cycle progression.

RhoGDIs bind to Rho GTPases in their inactive state, preventing them from interacting with guanine nucleotide exchange factors (GEFs) that would activate them. By doing so, RhoGDIs help regulate the spatial and temporal activation of Rho GTPases, ensuring that they are activated only when and where needed in the cell.

RhoGDI proteins have been identified as potential targets for therapeutic intervention in various diseases, including cancer, inflammation, and neurological disorders. Inhibitors of RhoGDI function have been shown to disrupt Rho GTPase signaling and may have therapeutic benefits in these conditions.

Benzamides are a class of organic compounds that consist of a benzene ring (a aromatic hydrocarbon) attached to an amide functional group. The amide group can be bound to various substituents, leading to a variety of benzamide derivatives with different biological activities.

In a medical context, some benzamides have been developed as drugs for the treatment of various conditions. For example, danzol (a benzamide derivative) is used as a hormonal therapy for endometriosis and breast cancer. Additionally, other benzamides such as sulpiride and amisulpride are used as antipsychotic medications for the treatment of schizophrenia and related disorders.

It's important to note that while some benzamides have therapeutic uses, others may be toxic or have adverse effects, so they should only be used under the supervision of a medical professional.

Palmitic acid is a type of saturated fatty acid, which is a common component in many foods and also produced naturally by the human body. Its chemical formula is C16H32O2. It's named after palm trees because it was first isolated from palm oil, although it can also be found in other vegetable oils, animal fats, and dairy products.

In the human body, palmitic acid plays a role in energy production and storage. However, consuming large amounts of this fatty acid has been linked to an increased risk of heart disease due to its association with elevated levels of bad cholesterol (LDL). The World Health Organization recommends limiting the consumption of saturated fats, including palmitic acid, to less than 10% of total energy intake.

Guanosine diphosphate (GDP) is a nucleotide that consists of a guanine base, a sugar molecule called ribose, and two phosphate groups. It is an ester of pyrophosphoric acid with the hydroxy group of the ribose sugar at the 5' position. GDP plays a crucial role as a secondary messenger in intracellular signaling pathways and also serves as an important intermediate in the synthesis of various biomolecules, such as proteins and polysaccharides.

In cells, GDP is formed from the hydrolysis of guanosine triphosphate (GTP) by enzymes called GTPases, which convert GTP to GDP and release energy that can be used to power various cellular processes. The conversion of GDP back to GTP can be facilitated by nucleotide diphosphate kinases, allowing for the recycling of these nucleotides within the cell.

It is important to note that while guanosine diphosphate has a significant role in biochemical processes, it is not typically associated with medical conditions or diseases directly. However, understanding its function and regulation can provide valuable insights into various physiological and pathophysiological mechanisms.

Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.

Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.

Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.

Molecular structure, in the context of biochemistry and molecular biology, refers to the arrangement and organization of atoms and chemical bonds within a molecule. It describes the three-dimensional layout of the constituent elements, including their spatial relationships, bond lengths, and angles. Understanding molecular structure is crucial for elucidating the functions and reactivities of biological macromolecules such as proteins, nucleic acids, lipids, and carbohydrates. Various experimental techniques, like X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cryo-electron microscopy (cryo-EM), are employed to determine molecular structures at atomic resolution, providing valuable insights into their biological roles and potential therapeutic targets.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Dansyl compounds are fluorescent compounds that contain a dansyl group, which is a chemical group made up of a sulfonated derivative of dimethylaminonaphthalene. These compounds are often used as tracers in biochemical and medical research because they emit bright fluorescence when excited by ultraviolet or visible light. This property makes them useful for detecting and quantifying various biological molecules, such as amino acids, peptides, and proteins, in a variety of assays and techniques, including high-performance liquid chromatography (HPLC), thin-layer chromatography (TLC), and fluorescence microscopy.

The dansyl group can be attached to biological molecules through chemical reactions that involve the formation of covalent bonds between the sulfonate group in the dansyl compound and amino, thiol, or hydroxyl groups in the target molecule. The resulting dansylated molecules can then be detected and analyzed using various techniques.

Dansyl compounds are known for their high sensitivity, stability, and versatility, making them valuable tools in a wide range of research applications. However, it is important to note that the use of dansyl compounds requires careful handling and appropriate safety precautions, as they can be hazardous if mishandled or ingested.

GTP-binding protein (G protein) gamma subunits are a type of regulatory protein that bind to and hydrolyze guanosine triphosphate (GTP). They are a component of heterotrimeric G proteins, which are composed of alpha, beta, and gamma subunits. The gamma subunit is tightly associated with the beta subunit and together they form a stable complex called the beta-gamma dimer.

When a G protein-coupled receptor (GPCR) is activated by an agonist, it causes a conformational change in the associated G protein, allowing the alpha subunit to exchange GDP for GTP. This leads to the dissociation of the alpha subunit from the beta-gamma dimer. Both the alpha and beta-gamma subunits can then go on to activate downstream effectors, leading to a variety of cellular responses.

The gamma subunit plays a role in regulating the activity of various signaling pathways, including those involved in vision, neurotransmission, and immune function. Mutations in genes encoding gamma subunits have been associated with several human diseases, including forms of retinal degeneration and neurological disorders.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

Guanosine triphosphate (GTP) is a nucleotide that plays a crucial role in various cellular processes, such as protein synthesis, signal transduction, and regulation of enzymatic activities. It serves as an energy currency, similar to adenosine triphosphate (ATP), and undergoes hydrolysis to guanosine diphosphate (GDP) or guanosine monophosphate (GMP) to release energy required for these processes. GTP is also a precursor for the synthesis of other essential molecules, including RNA and certain signaling proteins. Additionally, it acts as a molecular switch in many intracellular signaling pathways by binding and activating specific GTPase proteins.

Ras genes are a group of genes that encode for proteins involved in cell signaling pathways that regulate cell growth, differentiation, and survival. Mutations in Ras genes have been associated with various types of cancer, as well as other diseases such as developmental disorders and autoimmune diseases. The Ras protein family includes H-Ras, K-Ras, and N-Ras, which are activated by growth factor receptors and other signals to activate downstream effectors involved in cell proliferation and survival. Abnormal activation of Ras signaling due to mutations or dysregulation can contribute to tumor development and progression.

Acylation is a medical and biological term that refers to the process of introducing an acyl group (-CO-) into a molecule. This process can occur naturally or it can be induced through chemical reactions. In the context of medicine and biology, acylation often occurs during post-translational modifications of proteins, where an acyl group is added to specific amino acid residues, altering the protein's function, stability, or localization.

An example of acylation in medicine is the administration of neuraminidase inhibitors, such as oseltamivir (Tamiflu), for the treatment and prevention of influenza. These drugs work by inhibiting the activity of the viral neuraminidase enzyme, which is essential for the release of newly formed virus particles from infected cells. Oseltamivir is administered orally as an ethyl ester prodrug, which is then hydrolyzed in the body to form the active acylated metabolite that inhibits the viral neuraminidase.

In summary, acylation is a vital process in medicine and biology, with implications for drug design, protein function, and post-translational modifications.

Imidazoles are a class of heterocyclic organic compounds that contain a double-bonded nitrogen atom and two additional nitrogen atoms in the ring. They have the chemical formula C3H4N2. In a medical context, imidazoles are commonly used as antifungal agents. Some examples of imidazole-derived antifungals include clotrimazole, miconazole, and ketoconazole. These medications work by inhibiting the synthesis of ergosterol, a key component of fungal cell membranes, leading to increased permeability and death of the fungal cells. Imidazoles may also have anti-inflammatory, antibacterial, and anticancer properties.

Rac1 (Ras-related C3 botulinum toxin substrate 1) is a GTP-binding protein, which belongs to the Rho family of small GTPases. These proteins function as molecular switches that regulate various cellular processes such as actin cytoskeleton organization, gene expression, cell proliferation, and differentiation.

Rac1 cycles between an inactive GDP-bound state and an active GTP-bound state. When Rac1 is in its active form (GTP-bound), it interacts with various downstream effectors to modulate the actin cytoskeleton dynamics, cell adhesion, and motility. Activation of Rac1 has been implicated in several cellular responses, including cell migration, membrane ruffling, and filopodia formation.

Rac1 GTP-binding protein plays a crucial role in many physiological processes, such as embryonic development, angiogenesis, and wound healing. However, dysregulation of Rac1 activity has been associated with various pathological conditions, including cancer, inflammation, and neurological disorders.

Small molecules can also undergo prenylation, such as in the case of prenylflavonoids. Prenylation of a vitamin B2 derivative ( ... Wikimedia Commons has media related to Prenylation. Prenylation at the U.S. National Library of Medicine Medical Subject ... Protein prenylation involves the transfer of either a farnesyl or a geranylgeranyl moiety to C-terminal cysteine(s) of the ... Proteins that undergo prenylation include Ras, which plays a central role in the development of cancer. This suggests that ...
See also prenylation.) Glycosylation can also be effected using the tools of synthetic organic chemistry. Unlike the ...
Leys D (December 2018). "Flavin metamorphosis: cofactor transformation through prenylation". Current Opinion in Chemical ...
Leys D (December 2018). "Flavin metamorphosis: cofactor transformation through prenylation". Current Opinion in Chemical ...
Leys, David (December 2018). "Flavin metamorphosis: cofactor transformation through prenylation". Current Opinion in Chemical ... with the modifications branched nature and the position of the covalent linkages with flavin suggesting prenylation. UbiD ...
Farnesol Nerolidol Prenylation Terpene HUELIN, F.E.; Murray, K.E. (18 June 1966). "α-Farnesene in the Natural Coating of Apples ...
In 2011 Hrycyna wrote the book Protein Prenylation. Hrycyna is the first female department head of the Purdue chemistry ...
One form of C-terminal modification is prenylation. During prenylation, a farnesyl- or geranylgeranyl-isoprenoid membrane ...
Trost, BM; Stiles, DT (2007). "Total Synthesis of Spirotryprostatin B via Diastereoselective Prenylation". Org. Lett. 9 (15): ...
Trost, BM; Stiles, DT (2007). "Total Synthesis of Spirotryprostatin B via Diastereoselective Prenylation". Org. Lett. 9 (15): ... the stereochemistry at the spirocyclic ring juncture is established by a decarboxylation-prenylation sequence, reminiscent of ...
No prenylation sites are predicted in any DEPDC1B orthologs. Expression of DEPDC1B is reported to be largely ubiquitous ...
There are no N-myristoylation pattern or prenylation patterns. Kinase finder at Cuckoo determined kinase binding sites for ...
"Novel prenyltransferase enzymes as a tool for flavonoid prenylation". Trends Pharmacol. Sci. 26 (12): 606-8. doi:10.1016/j.tips ... "Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products". Nature. 435 (7044): 983-7. Bibcode ...
... from protein prenylation to immunomodulation". Nat. Rev. Immunol. 6 (5): 358-70. doi:10.1038/nri1839. PMC 3842637. PMID ... including protein prenylation). On March 28, 2008, Takeda halted further development of lapaquistat. While effective at ...
1997). "Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases". Cancer Lett. 110 (1-2): 49-55. doi:10.1016/ ... This PTP has been shown to primarily associate with plasmic and endosomal membrane through its C-terminal prenylation. This PTP ... PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif. ...
Prenylation may increase the potential activity of its original flavonoid. Monoprenyl isoflavone epoxidase is a key enzyme in ...
Magee T, Seabra MC (April 2005). "Fatty acylation and prenylation of proteins: what's hot in fat". Current Opinion in Cell ...
... s A and B are biosynthesized by prenylation of chrysoeriol. Barrett, M. L.; Scutt, A. M.; Evans, F. J. (1986). " ...
Inhibition of protein prenylation for proteins such as RhoA (and subsequent inhibition of Rho-associated protein kinase) may be ... In addition, the inhibitory effect on protein prenylation may also be involved in a number of unwanted side effects associated ... Kowluru A (January 2008). "Protein prenylation in glucose-induced insulin secretion from the pancreatic islet beta cell: a ... Greenwood J, Steinman L, Zamvil SS (May 2006). "Statin therapy and autoimmune disease: from protein prenylation to ...
2000). "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the ... 1997). "Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases". Cancer Lett. 110 (1-2): 49-55. doi:10.1016/ ... The surface membrane association of this protein depends on its C-terminal prenylation. Overexpression of this gene in ... which contains a PTP domain and a characteristic C-terminal prenylation motif. PTPs are cell signaling molecules that play ...
Prenylation was initially believed to be important only for membrane attachment. However, another role for prenylation appears ...
Kuzuyama T, Noel JP, Richard SB (June 2005). "Structural basis for the promiscuous biosynthetic prenylation of aromatic natural ...
Anant JS, Ong OC, Xie HY, Clarke S, O'Brien PJ, Fung BK (Jan 1992). "In vivo differential prenylation of retinal cyclic GMP ... PDE6β is the only protein that undergoes the two types of post-translational modification, prenylation and carboxymethylation. ...
The prenylation of these adenines is carried out by tRNA-isopentenyltransferase. Auxin is known to regulate the biosynthesis of ...
"Multiple factors contribute to inefficient prenylation of Rab27a in Rab prenylation diseases". The Journal of Biological ... REP1 assists the prenylation of Rab G-proteins by binding and presenting them to the Rab geranylgeranyltransferase subunit. ...
Rab GGTase is "responsible for the largest number of individual protein prenylation events in the cell," probably due to this ... Wilson AL, Erdman RA, Castellano F, Maltese WA (1998). "Prenylation of Rab8 GTPase by type I and type II geranylgeranyl ... Thoma NH, Niculae A, Goody RS, Alexandrov K (2001). "Double prenylation by RabGGTase can proceed without dissociation of the ... Phosphonocarboxylate inhibitors of Rabnext term geranylgeranyl transferase disrupt the prenylation and membrane localization of ...
Wilson AL, Erdman RA, Castellano F, Maltese WA (Aug 1998). "Prenylation of Rab8 GTPase by type I and type II geranylgeranyl ...
In addition, in signal transduction via G protein, palmitoylation of the α subunit, prenylation of the γ subunit, and ... Acylation Prenylation Palmitoylation Palmitoleoylation Glycophosphatidylinositol Cox, David L. Nelson, Michael M. (2005). ...
"Germ cell migration in zebrafish is dependent on HMGCoA reductase activity and prenylation". Developmental Cell. 6 (2): 295-302 ... pathway regulates developmental cerebral-vascular stability via prenylation-dependent signalling pathway". Developmental ...
Additionally, there are 5 N-myristoylation sites, and there is 1 prenylation site. FAM63A contains no glycosylation sites, ...
Small molecules can also undergo prenylation, such as in the case of prenylflavonoids. Prenylation of a vitamin B2 derivative ( ... Wikimedia Commons has media related to Prenylation. Prenylation at the U.S. National Library of Medicine Medical Subject ... Protein prenylation involves the transfer of either a farnesyl or a geranylgeranyl moiety to C-terminal cysteine(s) of the ... Proteins that undergo prenylation include Ras, which plays a central role in the development of cancer. This suggests that ...
Prenylation inhibitors and methods of their synthesis and use. Brown, BB., & Rehder, K. (2005). Prenylation inhibitors and ... The present invention is directed to compounds useful in the treatment of diseases associated with prenylation of proteins and ... and to methods for inhibiting protein prenylation in an organism using the same. ...
The Role of Prenylation in Vascular Calcification. File: application/pdf, -1 bytes ... The Role of Prenylation in Vascular Calcification. Ponnusamy, A. (Author). 1 Aug 2014 ... depleting cells of farnesyl pyrophosphate and geranylgeranyl pyrophosphate which are essential for the prenylation and ...
Significance: Deciphering FTase peptide recognition allows creation of bioengineered prenylation pathways and provides a model ... Significance: Deciphering FTase peptide recognition allows creation of bioengineered prenylation pathways and provides a model ... Significance: Deciphering FTase peptide recognition allows creation of bioengineered prenylation pathways and provides a model ... Significance: Deciphering FTase peptide recognition allows creation of bioengineered prenylation pathways and provides a model ...
... FERRI, NICOLA;K. ... We investigated the effect of ajoene on rat aortic smooth muscle cell proliferation as related to protein prenylation. (3) Cell ... We investigated the effect of ajoene on rat aortic smooth muscle cell proliferation as related to protein prenylation. (3) Cell ... Covalent attachment of these MVA-derived isoprenoid groups (prenylation) is a required function of several proteins that ...
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Functional characterization of the first aromatic prenyltransferase which catalyzes the prenylation of umbelliferone to produce ... Chapter III: Functional characterization of the first aromatic prenyltransferase which catalyzes the prenylation of ... Functional characterization of the first aromatic prenyltransferase which catalyzes the prenylation of umbelliferone to produce ...
Both fluvastatin and zoledronic acid inhibited Rap and Ras prenylation as well as the phosphorylation of ERK1/2 and AKT. The ... 2.4 Fluvastatin and Zoledronic Acidity Inhibit Proteins Prenylation of RAS and RAP To be able to investigate the molecular ... Background Bisphosphonates hinder the mevalonate pathway and inhibit the prenylation of. Background Bisphosphonates hinder the ... Inhibition of Rap and Ras prenylation by fluvastatin and zoledronic acidity about T24 cells. T24 cells had been grown in ...
Gao J, Liao J, Yang GY . CAAX-box protein, prenylation process and carcinogenesis. Am J Transl Res 2009; 1: 312-325. ...
The bisphosphonate zoledronic acid has antimyeloma activity in vivo by inhibition of protein prenylation. ... The bisphosphonate zoledronic acid has antimyeloma activity in vivo by inhibition of protein prenylation. Together they form a ...
... but have differential effects on the cell cycle and protein prenylation in human myeloma cells. ... but have differential effects on the cell cycle and protein prenylation in human myeloma cells. ...
Apomine, an inhibitor of HMG-COA-reductase, does not act by inhibiting protein prenylation in human myeloma cells in vitro ... Apomine, an inhibitor of HMG-COA-reductase, does not act by inhibiting protein prenylation in human myeloma cells in vitro ...
The bisphosphonate-ester apornine does not act by inhibiting protein prenylation, but enhances the effects of lovastatin on ... The bisphosphonate-ester apornine does not act by inhibiting protein prenylation, but enhances the effects of lovastatin on ...
The microbiome research is going through an evolutionary transition from focusing on the characterization of reference microbiomes associated with different environments/hosts to the translational applications, including using microbiome for disease diagnosis, improving the effcacy of cancer treatments, and prevention of diseases (e.g., using probiotics). Microbial markers have been identified from microbiome data derived from cohorts of patients with different diseases, treatment responsiveness, etc, and often predictors based on these markers were built for predicting host phenotype given a microbiome dataset (e.g., to predict if a person has type 2 diabetes given his or her microbiome data). Unfortunately, these microbial markers and predictors are often not published so are not reusable by others. In this paper, we report the curation of a repository of microbial marker genes and predictors built from these markers for microbiome-based prediction of host phenotype, and a computational ...
Prenylation. Peluso MR, Miranda CL, Hobbs DJ, Proteau RR, Stevens JFrederik. 2010. Xanthohumol and related prenylated ...
Subsequently, olivetolic acid undergoes prenylation by geranyl-diphosphate (Figure 1). The product of this synthesis, ...
Wang, M. & Casey, P. J. Protein prenylation: unique fats make their mark on biology. Nat. Rev. Mol. Cell Biol. 17, 110-122 ( ...
Prenylation of Rab GTPases: molecular mechanisms and involvement in genetic disease. FEBS Lett 2001. 498:197-200. View this ... Rab geranylgeranyl transferase alpha mutation in the gunmetal mouse reduces Rab prenylation and platelet synthesis. Proc Natl ...
Prenylation and Related Modifications. Transglutaminases. Peptidylprolyl Isomerases. polyADP-Ribose Polymerase Family. ...
One such example is the use of oral prenylation inhibitor lonafarnib (LNF). Prenylation inhibitors have been shown to abolish ... Identification of a prenylation site in delta virus large antigen. Science. 1992;256:1331-1333. [PubMed] [DOI] [Cited in This ...
Fellermeier, M., and Zenk, M. H. (1998). Prenylation of olivetolate by a hemp transferase yields cannabigerolic acid, the ... prior to aromatic prenylation by geranyl-pyrophosphate:olivetolate geranyltransferase (GOT) (Fellermeier and Zenk, 1998) ...
Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem.. 65. , 241 ...
M. Wang and P. J. Casey, "Protein prenylation: unique fats make their mark on biology," Nature Reviews. Molecular Cell Biology ... C. C. Palsuledesai and M. D. Distefano, "Protein prenylation: enzymes, therapeutics, and biotechnology applications," ACS ... and prenylation," Journal of Molecular and Cellular Cardiology, vol. 138, pp. 49-58, 2020. ...
Formin, nucleates the formation of linear actin filaments, involved in cell processes such as budding and mitotic spindle orientation which require the formation of polarized actin cables, functionally redundant with ...
2016) Rho-A prenylation and signaling link epithelial homeostasis to intestinal inflammation. J Clin Invest 126(2): 611-26. ...
Stanjek, V.; Piel, J.; Boland, W.: Biosynthesis of furanocoumarins: mevalonate-independent prenylation of umbelliferone in ...
Ultrahigh Throughput Microscale Mass Spectrometry for Pharmaceutical Prenylation Enzyme Engineering. $0. 2021. UNIVERSITY OF ... Ultrahigh Throughput Microscale Mass Spectrometry for Pharmaceutical Prenylation Enzyme Engineering. $0. 2021. UNIVERSITY OF ...
... both of which are required for protein prenylation. Such prenylation has important roles in the generation of lipidated protein ... The prevention of protein prenylation by either statins or bisphosphonates also leads to endoplasmic reticulum stress as a ...
In addition, Rab localization requires carboxy-terminal prenylation and specific structural determinants. Here we describe the ... despite its efficient prenylation and capacity to bind and hydrolyze GTP. These results strongly suggest that rab9 functions in ...
Structural Basis for the Prenylation Reaction of Carbazole-Containing Natural Products Catalyzed by Squalene Synthase-like ...
  • Prenylation (also known as isoprenylation or lipidation) is the addition of hydrophobic molecules to a protein or a biomolecule. (wikipedia.org)
  • Protein prenylation involves the transfer of either a farnesyl or a geranylgeranyl moiety to C-terminal cysteine(s) of the target protein. (wikipedia.org)
  • The second motif for prenylation is CXC, which, in the Ras-related protein Rab3A, leads to geranylgeranylation on both cysteine residues and methyl esterification. (wikipedia.org)
  • The present invention is directed to compounds useful in the treatment of diseases associated with prenylation of proteins and pharmaceutically acceptable salts thereof, to pharmaceutical compositions comprising same, and to methods for inhibiting protein prenylation in an organism using the same. (rti.org)
  • Hougland, JL , Gangopadhyay, SA & Fierke, CA 2012, ' Expansion of protein farnesyltransferase specificity using "tunable" active site interactions: Development of bioengineered prenylation pathways ', Journal of Biological Chemistry , vol. 287, no. 45, pp. 38090-38100. (syr.edu)
  • We investigated the effect of ajoene on rat aortic smooth muscle cell proliferation as related to protein prenylation. (unipd.it)
  • 5) In vitro assays for protein farnesyltransferase (PFTase) and protein geranylgeranyltransferase type I (PGGTase-I) confirmed that ajoene inhibits protein prenylation. (unipd.it)
  • Risedronate, and its phosphonocarboxylate analogue NE10790, both induce apoptosis, but have differential effects on the cell cycle and protein prenylation in human myeloma cells. (ox.ac.uk)
  • This is known as 'prenylation' -- a process involving the addition of hydrophobic molecules onto a protein to facilitate cell attachment -- which is not cost-effective or sustainable. (sciencedaily.com)
  • We have found that the C-terminal systeine residues of smg p21B, rhoA p21, and smg p25A are geranylgeranylated, and that these prenylation are essential for each small G protein to bind to membranes. (nii.ac.jp)
  • A: Yes, we found a way to change some cancer cells into benign cells through a process known as protein prenylation. (a-star.edu.sg)
  • These new isoprenoid analogues should be broadly useful in the studies of protein prenylation. (bvsalud.org)
  • Protein prenylation is a post-translational modification that is responsible for membrane association and protein-protein interactions. (bvsalud.org)
  • Several studies have shown a correlation between neurodegenerative diseases including Alzheimer's disease and Parkinson's disease and protein prenylation. (bvsalud.org)
  • Finally, we demonstrate that there is a significantly higher (22%) level of prenylated proteins in a cellular model of compromised autophagy as compared to normal cells, supporting the hypothesis of a potential involvement of protein prenylation in abrogated autophagy. (bvsalud.org)
  • These results highlight the utility of total prenylome labeling for studies on the role of protein prenylation in various diseases including aging-related disorders. (bvsalud.org)
  • There are three enzymes that carry out prenylation in the cell, farnesyl transferase, Caax protease and geranylgeranyl transferase I. Farnesylation is a type of prenylation, a post-translational modification of proteins by which an isoprenyl group is added to a cysteine residue. (wikipedia.org)
  • Proteins that undergo prenylation include Ras, which plays a central role in the development of cancer. (wikipedia.org)
  • Covalent attachment of these MVA-derived isoprenoid groups (prenylation) is a required function of several proteins that regulate cell proliferation. (unipd.it)
  • Background Bisphosphonates hinder the mevalonate pathway and inhibit the prenylation of little GTP-binding Bay 60-7550 proteins such as for example ras and rap. (researchhunt.com)
  • 2.4 Fluvastatin and Zoledronic Acidity Inhibit Proteins Prenylation of RAS and RAP To be able to investigate the molecular systems of fluvastatin and zoledronic acidity induced cell development inhibition the consequences of the two medicines on proteins prenylation of Ras and Rap1 had been analyzed by European blot. (researchhunt.com)
  • Lonafarnib is a well-characterized, late-stage, orally active inhibitor of farnesyl transferase, an enzyme involved in modification of proteins through a process called prenylation. (researchandmarkets.com)
  • Both fluvastatin and zoledronic acid inhibited Rap and Ras prenylation as well as the phosphorylation of ERK1/2 and AKT. (researchhunt.com)
  • This suggests that inhibitors of prenylation enzymes (e.g., farnesyltransferase) may influence tumor growth. (wikipedia.org)
  • Fti inhibitors for Progeria try to block prenylation. (freezingblue.com)
  • Inhibition of Rap and Ras prenylation by fluvastatin and zoledronic acidity about T24 cells. (researchhunt.com)
  • Biosynthesis of furanocoumarins: mevalonate-independent prenylation of umbelliferone in Apium graveolens (Apiaceae). (mpg.de)
  • Previous work from the host laboratory has shown that nitrogen-containing bisphosphonates attenuate vascular calcification by inhibiting farnesyl pyrophosphate synthase, depleting cells of farnesyl pyrophosphate and geranylgeranyl pyrophosphate which are essential for the prenylation and activation of small GTPases such as Ras and Rho. (manchester.ac.uk)
  • Prenylation attaches the cysteine residue and prenyl (15 residue farnesyl) group via a thioester. (freezingblue.com)
  • Attempts to identify the prenyl-proteome of cells or changes in prenylation following drug treatment have used 'clickable' alkyne-modified analogs of the lipid substrates farnesyl- and geranylgeranyl-diphosphate (FPP and GGPP). (bvsalud.org)
  • There is no known enzyme activity that can carry out the prenylation reaction with the isoprenoid alcohol. (wikipedia.org)
  • In accordance with this, farnesol and geranylgeraniol have been shown to be able to rescue effects caused by statins or nitrogenous bisphosphonates, further supporting that alcohols can be involved in prenylation, likely via phosphorylation to the corresponding isoprenoid pyrophosphate. (wikipedia.org)
  • Lonafarnib inhibits the prenylation step of HDV replication inside liver cells and blocks the virus life cycle at the stage of assembly. (researchandmarkets.com)
  • These analogs alter prenylation specificity and reactivity suggesting that in vivo results obtained using these FPP analogs should be interpreted cautiously. (bvsalud.org)
  • In the case of the K- and N-Ras forms of Ras, when cells are treated with FTIs, these forms of Ras can undergo alternate prenylation in the form of geranylgeranylation. (wikipedia.org)
  • There are at least 3 types of sites that are recognized by prenylation enzymes. (wikipedia.org)
  • Significance: Deciphering FTase peptide recognition allows creation of bioengineered prenylation pathways and provides a model for other multispecific enzymes. (syr.edu)
  • Farnesylation is a subspecies of prenylation in which a 15-carbon isoprenoid lipid is attached to a cysteine residue by farnesyltransferase. (protpi.ch)
  • Generic CAAX box prenylation motif. (eu.org)
  • This class of PTPs contain a PTP domain and a characteristic C-terminal prenylation motif. (prosci-inc.com)
  • After prenylation the three C -terminal amino acids (AAX) are then cleaved off by RAS-converting CAAX endopeptidase 1. (protpi.ch)
  • Farnesyltransferase-Mediated Delivery of a Covalent Inhibitor Overcomes Alternative Prenylation to Mislocalize K-Ras. (standuptocancer.org)
  • The United States Food and Drug Administration has granted fast-track designation to lonafarnib, a hepatitis D virus prenylation inhibitor, in combination with ritonavir for treatment of hepatitis D virus infection after a phase IIa study showed a decrease in hepatitis D virus RNA during 4 weeks of treatment (8). (who.int)
  • Here we demonstrate that cancer cell death triggered by statins can be uncoupled from prenylation of the RAS superfamily of oncoproteins. (athena-innovation.gr)
  • Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. (calixar.com)
  • In the case of the K- and N-Ras forms of Ras, when cells are treated with FTIs, these forms of Ras can undergo alternate prenylation in the form of geranylgeranylation. (wikipedia.org)
  • Prenylation is thought to be necessary for membrane anchoring and thereby proper function of the respective signaling pathways. (medscape.com)
  • These findings suggest that prenylchalcones and prenylflavanones found in hops and beer protect human LDL from oxidation and that prenylation antagonizes the prooxidant effects of the chalcone, CN, and the flavanone, NG. (oregonstate.edu)
  • It is usually assumed that prenyl groups (3-methylbut-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence of this has not been observed. (wikipedia.org)
  • Here we report that lipophilic statin treatment of mouse and human T cells increased expression of KLF2 through a HMG-CoA/prenylation-dependent pathway. (jci.org)