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 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.
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.
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)
Phosphoric or pyrophosphoric acid esters of polyisoprenoids.
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.
An enzyme involved in the MEVALONATE pathway, it catalyses the synthesis of farnesyl diphosphate from isopentenyl diphosphate and dimethylallyl diphosphate.
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.
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.
Twenty-carbon compounds derived from MEVALONIC ACID or deoxyxylulose phosphate.
A class of compounds composed of repeating 5-carbon units of HEMITERPENES.
Compounds that inhibit HMG-CoA reductases. They have been shown to directly lower cholesterol synthesis.
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 characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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.
An X chromosome-linked abnormality characterized by atrophy of the choroid and degeneration of the retinal pigment epithelium causing night blindness.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.

Cell growth inhibition by farnesyltransferase inhibitors is mediated by gain of geranylgeranylated RhoB. (1/756)

Recent results have shown that the ability of farnesyltransferase inhibitors (FTIs) to inhibit malignant cell transformation and Ras prenylation can be separated. We proposed previously that farnesylated Rho proteins are important targets for alternation by FTIs, based on studies of RhoB (the FTI-Rho hypothesis). Cells treated with FTIs exhibit a loss of farnesylated RhoB but a gain of geranylgeranylated RhoB (RhoB-GG), which is associated with loss of growth-promoting activity. In this study, we tested whether the gain of RhoB-GG elicited by FTI treatment was sufficient to mediate FTI-induced cell growth inhibition. In support of this hypothesis, when expressed in Ras-transformed cells RhoB-GG induced phenotypic reversion, cell growth inhibition, and activation of the cell cycle kinase inhibitor p21WAF1. RhoB-GG did not affect the phenotype or growth of normal cells. These effects were similar to FTI treatment insofar as they were all induced in transformed cells but not in normal cells. RhoB-GG did not promote anoikis of Ras-transformed cells, implying that this response to FTIs involves loss-of-function effects. Our findings corroborate the FTI-Rho hypothesis and demonstrate that gain-of-function effects on Rho are part of the drug mechanism. Gain of RhoB-GG may explain how FTIs inhibit the growth of human tumor cells that lack Ras mutations.  (+info)

Cloning and characterization of a mammalian prenyl protein-specific protease. (2/756)

Proteins containing C-terminal "CAAX" sequence motifs undergo three sequential post-translational processing steps: modification of the cysteine with either a 15-carbon farnesyl or 20-carbon geranylgeranyl isoprenyl lipid, proteolysis of the C-terminal -AAX tripeptide, and methylation of the carboxyl group of the now C-terminal prenylcysteine. A putative prenyl protein protease in yeast, designated Rce1p, was recently identified. In this study, a portion of a putative human homologue of RCE1 (hRCE1) was identified in a human expressed sequence tag data base, and the corresponding cDNA was cloned. Expression of hRCE1 was detected in all tissues examined. Both yeast and human RCE1 proteins were produced in Sf9 insect cells by infection with a recombinant baculovirus; membrane preparations derived from the infected Sf9 cells exhibited a high level of prenyl protease activity. Recombinant hRCE1 so produced recognized both farnesylated and geranylgeranylated proteins as substrates, including farnesyl-Ki-Ras, farnesyl-N-Ras, farnesyl-Ha-Ras, and the farnesylated heterotrimeric G protein Ggamma1 subunit, as well as geranylgeranyl-Ki-Ras and geranylgeranyl-Rap1b. The protease activity of hRCE1 activity was specific for prenylated proteins, because unprenylated peptides did not compete for enzyme activity. hRCE1 activity was also exquisitely sensitive to a prenyl peptide analogue that had been previously described as a potent inhibitor of the prenyl protease activity in mammalian tissues. These data indicate that both the yeast and the human RCE1 gene products are bona fide prenyl protein proteases and suggest that they play a major role in the processing of CAAX-type prenylated proteins.  (+info)

Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells. (3/756)

Little is known about the enzyme(s) required for the endoproteolytic processing of mammalian Ras proteins. We identified a mouse gene (designated Rce1) that shares sequence homology with a yeast gene (RCE1) implicated in the proteolytic processing of Ras2p. To define the role of Rce1 in mammalian Ras processing, we generated and analyzed Rce1-deficient mice. Rce1 deficiency was lethal late in embryonic development (after embryonic day 15.5). Multiple lines of evidence revealed that Rce1-deficient embryos and cells lacked the ability to endoproteolytically process Ras proteins. First, Ras proteins from Rce1-deficient cells migrated more slowly on SDS-polyacrylamide gels than Ras proteins from wild-type embryos and fibroblasts. Second, metabolic labeling of Rce1-deficient cells revealed that the Ras proteins were not carboxymethylated. Finally, membranes from Rce1-deficient fibroblasts lacked the capacity to proteolytically process farnesylated Ha-Ras, N-Ras, and Ki-Ras or geranylgeranylated Ki-Ras. The processing of two other prenylated proteins, the farnesylated Ggamma1 subunit of transducin and geranylgeranylated Rap1B, was also blocked. The absence of endoproteolytic processing and carboxymethylation caused Ras proteins to be mislocalized within cells. These studies indicate that Rce1 is responsible for the endoproteolytic processing of the Ras proteins in mammals and suggest a broad role for this gene in processing other prenylated CAAX proteins.  (+info)

The prenylation status of a novel plant calmodulin directs plasma membrane or nuclear localization of the protein. (4/756)

Post-translational attachment of isoprenyl groups to conserved cysteine residues at the C-terminus of a number of regulatory proteins is important for their function and subcellular localization. We have identified a novel calmodulin, CaM53, with an extended C-terminal basic domain and a CTIL CaaX-box motif which are required for efficient prenylation of the protein in vitro and in vivo. Ectopic expression of wild-type CaM53 or a non-prenylated mutant protein in plants causes distinct morphological changes. Prenylated CaM53 associates with the plasma membrane, but the non-prenylated mutant protein localizes to the nucleus, indicating a dual role for the C-terminal domain. The subcellular localization of CaM53 can be altered by a block in isoprenoid biosynthesis or sugar depletion, suggesting that CaM53 activates different targets in response to metabolic changes. Thus, prenylation of CaM53 appears to be a novel mechanism by which plant cells can coordinate Ca2+ signaling with changes in metabolic activities.  (+info)

Elevation of alpha2(I) collagen, a suppressor of Ras transformation, is required for stable phenotypic reversion by farnesyltransferase inhibitors. (5/756)

Farnesyltransferase inhibitors (FTIs) are a novel class of anticancer drugs that can reverse Ras transformation. One of the intriguing aspects of FTI biology is that continuous drug exposure is not necessary to maintain phenotypic reversion. For example, after a single exposure to FTIs, Ha-Ras-transformed fibroblasts revert to a flat and anchorage-dependent phenotype that persists for many days after processed Ras has returned to pretreatment levels. In this study, we show that persistence of the reverted state is mediated by elevated expression of the collagen isoform alpha2(I), a suppressor of Ras transformation the transcription of which is repressed by activated Ras and derepressed by FTI treatment. To our knowledge, this is the first report identifying an FTI-regulated gene which is linked to phenotypic reversion. The finding that extracellular matrix alterations can influence the kinetics of reversion supports our assertion that Rho-regulated cell adhesion parameters are a crucial determinant of the cellular response to FTIs.  (+info)

Activation of C3G guanine nucleotide exchange factor for Rap1 by phosphorylation of tyrosine 504. (6/756)

C3G is a guanine nucleotide exchange factor for Rap1 and is activated by the expression of Crk adaptor proteins. We found that expression of CrkI in COS cells induced significant tyrosine phosphorylation of C3G. To understand the mechanism by which C3G is phosphorylated and activated by Crk, we constructed a series of deletion mutants. Deletion of the amino terminus of C3G to amino acid 61 did not remarkably affect either tyrosine phosphorylation or Crk-dependent activation of C3G. When C3G was truncated to amino acid 390, C3G was still phosphorylated on tyrosine but was not effectively activated by CrkI. Deletion of the amino terminus of C3G to amino acid 579 significantly reduced the Crk-dependent tyrosine phosphorylation of C3G and increased GTP-bound Rap1 irrespective of the presence of CrkI. We substituted all seven tyrosine residues in this region, amino acids 391-579, for phenylalanine for identification of the phosphorylation site. Among the substitution mutants, the C3G-Y504F mutant, in which tyrosine 504 was substituted by phenylalanine, was remarkably less activated and phosphorylated than the wild type. All the other substitution mutants were activated and tyrosyl-phosphorylated by the expression of CrkI. Thus, CrkI activates C3G by the phosphorylation of tyrosine 504, which represses the cis-acting negative regulatory domain outside the catalytic region.  (+info)

A mutant form of the rho protein can restore stress fibers and adhesion plaques in v-src transformed fibroblasts. (7/756)

The organization of polymerized actin in the mammalian cell is regulated by several members of the rho family. Three rho proteins, cdc42, rac and rho act in a cascade to organize the intracellular actin cytoskeleton. Rho proteins are involved in the formation of actin stress fibers and adhesion plaques in fibroblasts. During transformation of mammalian cells by oncogenes the cytoskeleton is rearranged and stress fibers and adhesion plaques are disintegrated. In this paper we investigate the function of the rho protein in RR1022 rat fibroblasts transformed by the Rous sarcoma virus. Two activated mutants of the rho protein, rho G14V and rho Q63L, and a dominant negative mutant, rho N1171, were stably transfected into RR1022 cells. The resulting cell lines were analysed for the organization of polymerized actin and adhesion plaques. Cells expressing rho Q63L, but not rho wt, rho G14V or rho N1171, showed an altered morphology. These cells displayed a flat, fibroblast like shape when compared with the RR1022 ancestor cells. Immunofluorescence analyses revealed that actin stress fibers and adhesion plaques were rearranged in these cells. We conclude from these data that an active rho protein can restore elements of the actin cytoskeleton in transformed cells by overriding the tyrosine kinase phosphorylation induced by the pp60(v-src).  (+info)

Carcinogen and dietary lipid regulate ras expression and localization in rat colon without affecting farnesylation kinetics. (8/756)

Epidemiological and experimental data suggest that dietary fiber and fat are major determinants of colorectal cancer. However, the mechanisms by which these dietary constituents alter the incidence of colon cancer have not been elucidated. Evidence indicates that dominant gain-of-function mutations short-circuit protooncogenes and contribute to the pathogenesis of cancer. Therefore, we began to dissect the mechanisms whereby dietary fat and fiber, fed during the initiation, promotion and progression stages of colon tumorigenesis, regulate ras p21 localization, expression and mutation frequency. Male Sprague-Dawley rats (140) were provided with corn oil or fish oil and pectin or cellulose plus or minus the carcinogen azoxymethane (AOM) in a 2 x 2 x 2 factorial design and killed after 34 weeks. We have previously shown adenocarcinoma incidence in these animals to be 70.3% (52/74) for corn oil + AOM and 56.1% (37/66) for fish oil + AOM (P < 0.05). Total ras expression as well as ras membrane:cytosol ratio was 4- to 6-fold higher in colon tumors than in mucosa from AOM- or saline-injected rats. Expression of ras in the mucosal membrane fraction was 13% higher for animals fed corn oil compared with fish oil feeding (P < 0.05), which is noteworthy since ras must be localized at the plasma membrane to function. The elevated ras membrane:cytosol ratio in tumors was not due to increased farnesyl protein transferase activity or prenylation state, as nearly all detectable ras was in the prenylated form. Phosphorylated p42 and p44 mitogen activated protein kinase (ERK) expression was two-fold higher in tumor extracts compared with uninvolved mucosa from AOM- and saline-injected rats (P < 0.05). The frequency of K-ras mutations was not significantly different between the various groups, but there was a trend toward a greater incidence of mutations in tumors from corn oil fed rats (85%) compared with fish oil fed rats (58%). Our results indicate that the carcinogen-induced changes in ras expression and membrane localization are associated with the in vivo activation of the ERK pathway. In addition, suppression of tumor development by dietary n-3 polyunsaturated fatty acids may be partly due to a combined effect on colonic ras expression, membrane localization, and mutation frequency.  (+info)

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.

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.

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.

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.

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.

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.

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.

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."

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.

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.

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.

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.

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.

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.

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.

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.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

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.

In this kind of glycosylation a protein is attached to a lipid anchor, via a glycan chain. (See also prenylation.) ... For instance, some proteins do not fold correctly unless they are glycosylated. In other cases, proteins are not stable unless ... In addition to their function in protein folding and cellular attachment, the N-linked glycans of a protein can modulate a ... Thrombospondins are one of the proteins most commonly modified in this way. However, there is another group of proteins that ...
Leys D (December 2018). "Flavin metamorphosis: cofactor transformation through prenylation". Current Opinion in Chemical ... Portal: Biology (EC 2.5.1, Bacterial proteins). ...
In 2011 Hrycyna wrote the book Protein Prenylation. Hrycyna is the first female department head of the Purdue chemistry ... Hrycyna studies the post-translational modification of eukaryotic proteins, including the small G proteins. Eukaryotic proteins ... She worked in Steven Clarke's laboratory on protein modifications. Hrycyna was a postdoctoral fellow at The Jane Coffin Childs ... "Clarke stands out with seminal discoveries in protein methylation and inspired teaching". www.asbmb.org. Retrieved 2019-04-04. ...
Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus. While the N-terminus of a protein ... One form of C-terminal modification is prenylation. During prenylation, a farnesyl- or geranylgeranyl-isoprenoid membrane ... protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is ... This allows other proteins to bind to the C-terminal domain of RNA polymerase in order to activate polymerase activity. These ...
... 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/ ... Protein tyrosine phosphatase type IVA 2 is an enzyme that in humans is encoded by the PTP4A2 gene. The protein encoded by this ... PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif. ... 2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi: ...
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/ ... Protein tyrosine phosphatase type IVA 1 is an enzyme that in humans is encoded by the PTP4A1 gene. The protein encoded by this ... The surface membrane association of this protein depends on its C-terminal prenylation. Overexpression of this gene in ...
However, another role for prenylation appears to be its importance in protein-protein interactions. The only nuclear proteins ... Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends. Prenylation was initially ... "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. Bibcode:2005Natur. ... The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina. It shares limited ...
No signal peptide or transmembrane domains are predicted within human or any ortholog protein. No prenylation sites are ... indicates the possible interaction of the protein with a SUMO protein, enabling or inhibiting interaction with other proteins. ... DEP Domain Containing Protein 1B also known as XTP1, XTP8, HBV XAg-Transactivated Protein 8, [formerly referred to as BRCC3] is ... The DEP domain is primarily found in proteins involved in G-protein signalling pathways and regulation of GTPase. As well, ...
Rab GGTase is "responsible for the largest number of individual protein prenylation events in the cell," probably due to this ... Instead Rab proteins are bound by the Rab escort protein (REP) over a more conserved region of the Rab protein and then ... it is in the protein prenyltransferase family along with two other enzymes (protein farnesyltransferase and protein ... geranylgeranyl diphosphate + protein-cysteine ⇌ {\displaystyle \rightleftharpoons } S-geranylgeranyl-Cys-protein + diphosphate ...
The prenylation motif "CaaX box" is the most common prenylation site in proteins, that is, the site where farnesyl or ... the site where the lipids bind to the protein depends both on the lipid group and protein. Prenylated proteins are proteins ... Lipid-anchored proteins (also known as lipid-linked proteins) are proteins located on the surface of the cell membrane[of what ... Overall, there are three main types of lipid-anchored proteins which include prenylated proteins, fatty acylated proteins and ...
This process, called prenylation, causes prenylated proteins to become membrane-associated due to the hydrophobic nature of the ... Most prenylated proteins are involved in cellular signaling, wherein membrane association is critical for function. ... Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I". J. Lipid Res. 47 (4): 681-99. doi: ... El Oualid F, Cohen LH, van der Marel GA, Overhand M (2006). "Inhibitors of protein: geranylgeranyl transferases". Curr. Med. ...
Wang, M. & Casey, P.J. (2016) Protein prenylation: unique fats make their mark on biology. Nat. Rev. Mol. Cell Biol. 17:110-122 ... Zhang, F.L. & Casey, P.J. (1996) Protein prenylation: Molecular mechanisms and biological consequences. Annu. Rev. Biochem. 65: ... His primary areas of research are in the fields of lipid modifications of proteins and in G protein signaling in cancer. Casey ... Park, H.W., Boduluri, S.R., Moomaw, J.F., Casey, P.J. & Beese, L.S. (1997) Crystal structure of protein farnesyltransferase at ...
2006). "MUBs, a family of ubiquitin-fold proteins that are plasma membrane-anchored by prenylation". J. Biol. Chem. 281 (37): ... Ubiquitin-like protein 3 is a protein that in humans is encoded by the UBL3 gene. In melanocytic cells UBL3 gene expression may ... 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs ... 2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287- ...
... residues play a valuable role by crosslinking proteins, which increases the rigidity of proteins and also functions to ... The nucleophilic sulfhydryl group allows cysteine to conjugate to other groups, e.g., in prenylation. Ubiquitin ligases ... which play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular ... Disulfide bonds in proteins are formed by oxidation of the sulfhydryl group of cysteine residues. The other sulfur-containing ...
Biochemist at Duke University, known for structural biochemistry of DNA replication and protein prenylation enzymes. Member ... American protein chemist at the University of Washington, known for molecular dynamics simulations of proteins and other ... Emil L. Smith (1911-2009). American protein chemist at UCLA, known in particular for studies of protein evolution. Member Natl ... Mortimer Louis Anson (1901-1968). American biochemist and protein chemist, the first to propose that protein folding was ...
2000). "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the ... Protein tyrosine phosphatase type IVA 3 is an enzyme that in humans is encoded by the PTP4A3 gene. The protein encoded by this ... 2006). "Identification of integrin alpha1 as an interacting protein of protein tyrosine phosphatase PRL-3". Biochem. Biophys. ... "Entrez Gene: PTP4A3 protein tyrosine phosphatase type IVA, member 3". Zeng Q, Hong W, Tan YH (1998). "Mouse PRL-2 and PRL-3, ...
Some of them are probably inactive, and only mediate protein-protein interactions. Dual-Specificity+Phosphatases at the U.S. ... They share a high sequence identity and possess an N-terminal prenylation sequence (CAAX box). Despite their up-regulation in ... Mitogen-activated protein Kinase Phosphatases (MKPs) MKPs form a rather large family, with some 11 well-characterized members. ... The human genome encodes at least 61 different DUSP proteins. The following major groups or families of DUSPs were identified: ...
1996). "Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1". J. Leukoc ... 2000). "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the ... 2000). "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins". Nature. 403 (6769 ... 2002). "Evaluation of farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical ...
1996). "Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1". J. Leukoc ... 2000). "Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the ... 2000). "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins". Nature. 403 (6769 ... Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha is an enzyme that in humans is encoded by the FNTA ...
1996). "Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1". J. Leukoc ... Interferon-induced guanylate-binding protein 1 is a protein that in humans is encoded by the GBP1 gene. It belongs to the ... Guanylate binding protein expression is induced by interferon. Guanylate binding proteins are characterized by their ability to ... 2000). "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins". Nature. 403 (6769 ...
Prenylation (including geranylgeranylation) is thought to function, at least in part, as a membrane anchor for proteins. The ... Geranylgeranylation is a form of prenylation, which is a post-translational modification of proteins that involves the ... seen in the lipid anchoring of the Rho GTPase family of signaling molecules and the gamma subunit of heterotrimeric G proteins ... at the C-terminus of specific proteins. ...
... most likely mediated by defective protein prenylation. Prenylation refers to addition of hydrophobic isoprenoids to proteins, ... When isoprenoids such as these are coupled to a target protein, this affects the protein's cellular location and function. In a ... Immunoglobulin D (IgD) is a protein produced by a certain type of white blood cells. There are five classes of Immunoglobulin: ... C-reactive protein (CRP) also increases. CRP is released by liver which causes inflammation. Hyperimmunoglobulinemia D with ...
... rather than myristoylation or prenylation). These coat proteins are necessary but insufficient to direct or dock the vesicle to ... The Coat Protein Complex II, or COPII, is a group of proteins that facilitate the formation of vesicles to transport proteins ... Both Sec23 proteins can interact with any of the four Sec24 proteins: Sec24A, Sec24B, Sec24C, and Sec24D. Lethal or pathogenic ... Sec24 proteins recognize various cargo proteins, packaging them into the budding vesicles. The COPII coat consists of an inner ...
REP1 assists the prenylation of Rab G-proteins by binding and presenting them to the Rab geranylgeranyltransferase subunit. ... Choroideremia is caused by a loss-of-function mutation in the CHM gene which encodes Rab escort protein 1 (REP1), a protein ... "Multiple factors contribute to inefficient prenylation of Rab27a in Rab prenylation diseases". The Journal of Biological ... While the complete mechanism of disease is not fully understood, the lack of a functional protein in the retina results in cell ...
PDE6Îē is the only protein that undergoes the two types of post-translational modification, prenylation and carboxymethylation. ... PDE6 is a protein complex located on the photoreceptor's outer segment, and plays an important role in the phototransduction ... Anant JS, Ong OC, Xie HY, Clarke S, O'Brien PJ, Fung BK (Jan 1992). "In vivo differential prenylation of retinal cyclic GMP ... PDE6 is a highly concentrated protein in retinal photoreceptors. With the presence of the GAF domain, PDE6 can actively bind to ...
"Proteolipids - proteins modified by covalent attachment to lipids - N-myristoylated, S-palmitoylated, prenylated proteins, ... and prenylation (also to cysteine). Despite the seemingly specific names, N-myristoylation and S-palmitoylation can also ... ghrelin, hedgehog proteins". The LipidWeb. Retrieved 18 July 2019. Li Y, Qi B (2017). "Progress toward Understanding Protein S- ... protein and RNA, leading to apoptosis. Myelin proteolipid protein This article incorporates text by Jessica Hutchinson ...
... a REP-1 like protein) both help with the prenylation and transport of Rab proteins. Rab27 has been found to preferentially ... Surface protein recycling returns proteins to the surface whose function involves carrying another protein or substance inside ... Rab proteins are peripheral membrane proteins, anchored to a membrane via a lipid group covalently linked to an amino acid. ... The Rab family of proteins is a member of the Ras superfamily of small G proteins. Approximately 70 types of Rabs have now been ...
... prenylation is thought to be involved in directing the interaction of the subunit both with membrane lipids and other proteins ... Portal: Biology (Protein pages needing a picture, G proteins, Protein complexes). ... "Evidence that a protein-protein interaction 'hot spot' on heterotrimeric G protein betagamma subunits is used for recognition ... "Mechanism of assembly of G protein betagamma subunits by protein kinase CK2-phosphorylated phosducin-like protein and the ...
Significance: Deciphering FTase peptide recognition allows creation of bioengineered prenylation pathways and provides a model ... T1 - Expansion of protein farnesyltransferase specificity using "tunable" active site interactions. T2 - Development of ... Background: FTase recognizes and modifies many proteins with C-terminal CA1A2X sequences. Results: Mutating active site ... Expansion of protein farnesyltransferase specificity using "tunable" active site interactions: Development of bioengineered ...
... and protein geranylgeranyltransferase type I (PGGTase-I) confirmed that ajoene inhibits protein prenylation. High performance ... and protein geranylgeranyltransferase type I (PGGTase-I) confirmed that ajoene inhibits protein prenylation. High performance ... Ajoene, a garlic compound, inhibits protein prenylation and arterial smooth muscle cell proliferation. FERRI, NICOLA;K. ... We investigated the effect of ajoene on rat aortic smooth muscle cell proliferation as related to protein prenylation. (3) Cell ...
In this kind of glycosylation a protein is attached to a lipid anchor, via a glycan chain. (See also prenylation.) ... For instance, some proteins do not fold correctly unless they are glycosylated. In other cases, proteins are not stable unless ... In addition to their function in protein folding and cellular attachment, the N-linked glycans of a protein can modulate a ... Thrombospondins are one of the proteins most commonly modified in this way. However, there is another group of proteins that ...
Gao J, Liao J, Yang GY . CAAX-box protein, prenylation process and carcinogenesis. Am J Transl Res 2009; 1: 312-325. ... TIPE2 protein serves as a negative regulator of phagocytosis and oxidative burst during infection. Proc Natl Acad Sci USA 2012 ... Human tumor necrosis factor (TNF)-alpha-induced protein 8-like 2 suppresses hepatocellular carcinoma metastasis through ... The Rac1 C-terminal polybasic region regulates the nuclear localization and protein degradation of Rac1. J Biol Chem 2004; 279 ...
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 ...
... tumor protein 53 (TP53), DPYD, ERBB2 interacting protein (ERBB2IP), FBXW7, KMT2D, PPP2R1A, TSC2, whereas amplification of MYC ... extensive non-specific protein-protein/DNA/RNA interactions and haphazard oligomerization. To date, expression hosts for ... protein binding - retinal dehydrogenase activity - steroid metabolic process Data from Gene Ontology via CGAP [Hide] ... What pathways are this gene/protein implicaed in?. Show (12). AKR1B10 is involved in:. - Ascorbate and aldarate metabolism KEGG ...
... by a single bifunctional protein, CoaBC. Depletion of CoaBC was found to be bactericidal in M. tuberculosis. Here we report the ... Wang, M. & Casey, P. J. Protein prenylation: unique fats make their mark on biology. Nat. Rev. Mol. Cell Biol. 17, 110-122 ( ... For CoaBC 300 nL of pure protein at 30 mg mL−1, pre-incubated with 3 mM CTP and 10 mM MgCl2, was mixed in 1:1 and 1:2 (protein ... As the HFCD protein family of flavin-binding proteins are known to form homo-oligomers16, we performed native electrospray- ...
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 ... The membrane protein extractions from the aortic media (VSMCs were the only cell type in this layer) or cultured VSMCs were ... Total proteins were also extracted, and western blot was performed as described in our previous reports [12, 13]. The ...
Protein Glycosylation (includes transferases involved in synthesis of glycolipids). GPI Anchoring. Prenylation and Related ... LIM Domain Proteins. PDZ Domain. WD Repeat Proteins. Ring Finger Proteins. Tripartite Motif Family. Zinc Finger Proteins. ... G-Protein-coupled Receptors. Peptide and Protein G-coupled Signals. G Proteins. Inositol Pathways (includes protein kinase C). ... 8. Structural Proteins. Origins of Structural Proteins. Actin and Related Proteins. Myosin. Tubulin and Microtubules. Kinesins ...
Such prenylation has important roles in the generation of lipidated protein domains that enable protein-protein interactions ... The prevention of protein prenylation by either statins or bisphosphonates also leads to endoplasmic reticulum stress as a ... Protein Sci. 2004, 13, 155-165. [Google Scholar] [CrossRef]. *Zhu, Z.; Jiang, W.; Thompson, M.D.; McGinley, J.N.; Thompson, H.J ... both of which are required for protein prenylation. ... Seol, W.; Choi, H.S.; Moore, D.D. Isolation of proteins that ...
... and prenylation of proteins involved in cell proliferation and differentiation. Mutations associated with HIDS lead to markedly ... PAPA is caused by mutations in the proline serine threonine phosphatase-interacting protein (PSTPIP1, or CD2 binding protein 1 ... also known as CD2-binding protein 1 (CD2BP1), which is a tyrosine-phosphorylated protein involved in cytoskeletal organization ... 80, 81] The mutated protein expressed in vitro had no affinity with the IL-1 receptor, and stimulation of the patients cells ...
... and protein prenylation. The most notable oxysterol activities center around the regulation of cholesterol homeostasis, which ... Wnt proteins control diverse biological processes through Îē-catenin-dependent canonical signalling and Îē-catenin-independent ...
Protein prenylation restrains innate immunity by inhibiting Rac1 effector interactions. Nature Communications. 2019. ISSN 2041- ... The Rhotekin-RBD protein supplied in this kit contains Rhotekin residues 7-89 and is in the form of a GST fusion protein, which ... The fact that many Rho family effector proteins will specifically recognize the GTP bound form of the protein has been ... Positive Cellular Protein Control:. Total cell lysate (300 - 800 Ξg) should be loaded with GTPÎģS as a positive control for the ...
Protein Prenylation in the moss Physcomitrium patens. Zayna Qaissi, Anam F. Ahmed, Mark P. Running, and Katherine Vo. Brown ...
Protein Carbonylation. Miranda CL, Reed RL, Kuiper HC, Alber S, Stevens JF. 2009. Ascorbic acid promotes detoxification and ... Prenylation. Peluso MR, Miranda CL, Hobbs DJ, Proteau RR, Stevens JFrederik. 2010. Xanthohumol and related prenylated ... structure-activity relationships and in silico binding to myeloid differentiation protein-2 (MD-2).. Planta Med. 76(14):1536-43 ... structure-activity relationships and in silico binding to myeloid differentiation protein-2 (MD-2).. Planta Med. 76(14):1536-43 ...
New insights into the link between protein prenylation and inflammation using models of mevalonate kinase deficiency (MKD) ...
Our work now shows that prenylation, in the context of an adjacent polybasic region, can reversibly transfer proteins from the ... Both protein kinase A and mitogen-activated protein kinase are required in the amygdala for the macromolecular synthesis- ... Both protein kinase A and mitogen-activated protein kinase are required in the amygdala for the macromolecular synthesis- ... Direct involvement of protein myristoylation in calmodulin-target protein interaction. J. Biol. Chem. ...
Lonafarnib works by blocking farnesyl transferase, an enzyme involved in prenylation, the modification of proteins that is ... The first of these is called Lonafarnib, which is being evaluated for how well it works to target the protein assembly process ... Pegylated interferon (Peg IFN) is a protein-based medication that prompts the body to activate its natural immune system ( ... which keeps new viruses from being created (it is known as a prenylation inhibitor). Lonafarnib, in combination with another ...
2019Delayed death in the malaria parasite Plasmodium falciparum is caused by disruption of prenylation-dependent intracellular ... Conditional protein mislocalization combined with high-resolution imaging provides convincing evidence that K13 is involved in ... Moreover, specific proteins important for this process and the cellular structures involved have not been unambiguously ... The Plasmodium falciparum artemisinin resistance-associated protein Kelch 13 is required for formation of normal cytostomes. * ...
The chemical toolbox for monitoring protein fatty acylation and prenylation. RN Hannoush, JL Sun ... Phosphorylation of Dishevelled by protein kinase RIPK4 regulates Wnt signaling. XD Huang, JC McGann, BY Liu, RN Hannoush, JR ... Imaging the lipidome: ω-alkynyl fatty acids for detection and cellular visualization of lipid-modified proteins. RN Hannoush, N ... Systematic mapping of WNT-FZD protein interactions reveals functional selectivity by distinct WNT-FZD pairs. JP Dijksterhuis, B ...
Example of prenylation Prenylation is known to occur on proteins of the RAB family of RAS-related G-proteins, oncogenic GTP- ... Many of ER and Golgi membrane proteins, also proteins secreted from the cell like serum and mucus proteins, Glycosylation is ... O-linked proteins O-linked found in mucous fluids, but can also be present in membrane and secretory proteins, 3 or more sugars ... N-linked protein in hormones GlcNAc is linked to serine residue that become phosphorylated by protein kinases in hormonal ...
Key Words : ras p21, small G proteins, Prenylation, GDP/GTP exchange protein, GTPase activating protein, Tumor markers. Less ... ras p21 / small GTP-binding proteins / prenylation / GDP / GTP exchange protein / GTPase activating protein / Tumor markers / , ... and GTPase activating Proteins (GAP) for small G proteins. Among these regulatory proteins, we have cloned the cDNAs of smg p21 ... purified the regulatory proteins for small G proteins, and made monoclonal antibodies against small G proteins and their ...
A: Yes, we found a way to change some cancer cells into benign cells through a process known as protein prenylation. By ...
... an enzyme involved in modification of proteins through a process called prenylation. HDV uses this host cell process inside ... Lonafarnib inhibits the prenylation step of HDV replication inside liver cells and blocks the virus life cycle at the stage of ...
One of the examples of prenylation dependent protein-protein interactions is the interaction with chaperone proteins such as ... protein-protein interactions, and signaling [46, 47]. There are various protein-protein interactions that involve the ... Our results show that PCAIs deplete the protein levels of some significant G-proteins which are known to be involved in the ... reduction in NRAS protein levels at 5 ΞM treatment with NSL-YHJ-2-27 (Figure 3D). Of all the proteins tested, the non- ...
The genes encoding CaaX protein prenyltransferases are considerably longer than those encoding non-CaaX subunits, as a result ... Farnesyltransferase and geranylgeranyltransferase I both recognize a Ca1a2X motif on their protein substrates; ... the attachment of prenyl lipid anchors 15 or 20 carbons long to the carboxyl termini of a variety of eukaryotic proteins. ... Three different protein prenyltransferases (farnesyltransferase and geranylgeranyltransferases I and II) catalyze ...
  • We have used specific inhibitors for farnesyltransferase (FTase) and geranylgeranyltransferase (GGTase) I as well as combinations of lovastatin with geranylgeraniol (GGOH) or farnesol (FOH) to investigate the role of protein prenylation in platelet-derived growth factor (PDGF)-induced PDGF receptor tyrosine phosphorylation. (nyu.edu)
  • 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)
  • Resistance of Plasmodium falciparum to artemisinin, which has become a threat to malaria control, has been linked to mutations in the parasite protein K13. (elifesciences.org)
  • Protein prenylation catalyzed by protein farnesyltransferase (FTase) and protein geranylgeranyltransferase (GGTase) is essential to the survival of Cryptococcus neoformans, Candida albicans, and Plasmodium falciparum. (duke.edu)
  • In vitro and in vivo antiplasmodial activities of risedronate and its interference with protein prenylation in Plasmodium falciparum. (lktlabs.com)
  • That is followed by a detailed description for how such analyses are performed for one example where the prenylated proteins from Plasmodium falciparum, the causative agent for malaria, were identified. (umn.edu)
  • 2010. Xanthohumol and related prenylated flavonoids inhibit inflammatory cytokine production in LPS-activated THP-1 monocytes: structure-activity relationships and in silico binding to myeloid differentiation protein-2 (MD-2). . (oregonstate.edu)
  • Changes in the level of prenylated proteins may serve a critical function in a variety of diseases. (umn.edu)
  • 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)
  • Metabolic labeling using modified isoprenoid probes followed by enrichment and proteomic analysis allows the identities and levels of prenylated proteins to be investigated. (umn.edu)
  • We show that metabolically incorporating an alkyne isoprenoid into mammalian cells, followed by a Cu(I)-catalyzed alkyne azide cycloaddition reaction to a fluorophore, allows for detection of prenylated proteins in several cell lines and that different cell types vary significantly in their levels of prenylated proteins. (bvsalud.org)
  • The majority of proteins synthesized in the rough endoplasmic reticulum undergo glycosylation. (wikipedia.org)
  • Glycosylation is the process by which a carbohydrate is covalently attached to a target macromolecule, typically proteins and lipids. (wikipedia.org)
  • Glycosylation also plays a role in cell-to-cell adhesion (a mechanism employed by cells of the immune system) via sugar-binding proteins called lectins, which recognize specific carbohydrate moieties. (wikipedia.org)
  • In addition, glycosylation is often used by viruses to shield the underlying viral protein from immune recognition. (wikipedia.org)
  • Glycosylation can also module the thermodynamic and kinetic stability of the proteins. (wikipedia.org)
  • Fti inhibitors for Progeria try to block prenylation. (freezingblue.com)
  • Polyisoprenylated cysteinyl amide inhibitors (PCAIs) are agents that mimic the essential posttranslational modifications of G-proteins. (oncotarget.com)
  • 1994) Protein farnesyltransferase inhibitors block the growth of ras-dependent tumors in nude mice. (guidetopharmacology.org)
  • In this short presentation, I will describe our work in developing chemical probes to study this process in order to learn about the biology of prenylation, develop new inhibitors with therapeutic potential and use lipid modification for biotechnology applications. (umn.edu)
  • Significance: Deciphering FTase peptide recognition allows creation of bioengineered prenylation pathways and provides a model for other multispecific enzymes. (syr.edu)
  • This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. (cancerindex.org)
  • Geranylgeranyl transferase-I (GGTase-I) is one of the key enzymes mediating protein isoprenylation during the posttranslational modification, especially the geranylgeranylation of small GTPase, Rac1 [ 6 ]. (hindawi.com)
  • Glycans serve a variety of structural and functional roles in membrane and secreted proteins. (wikipedia.org)
  • Such a membrane-anchoring strategy has been adopted by a wide range of signaling proteins ( Fivaz and Meyer, 2003 ) with significant variations in the structure of these motifs (see Table S1). (rupress.org)
  • O-linked found in mucous fluids, but can also be present in membrane and secretory proteins, 3 or more sugars linked by N-acetylglalactosamine (GalNAc)--connected to serine, theronine. (freezingblue.com)
  • Prenylation creates a hydrophobic domain on protein tails which acts as a membrane anchor. (guidetopharmacology.org)
  • Prenylation facilitates protein localization mainly to the plasma membrane where the prenylated proteins, including small GTPases, mediate signal transduction pathways. (umn.edu)
  • the prenyl group serves to anchor these proteins in the membrane so that they are positioned to interact with cell surface receptors either directly or via adaptor proteins. (umn.edu)
  • Protein prenylation is a post-translational modification that is responsible for membrane association and protein-protein interactions. (bvsalud.org)
  • 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)
  • Lonafarnib inhibits the prenylation step of HDV replication inside liver cells and blocks the virus life cycle at the stage of assembly. (researchandmarkets.com)
  • Main conclusion: Despite AtJ3 and AtJ2 sharing a high protein-sequence identity and both being substrates of protein farnesyltransferase (PFT), AtJ3 but not AtJ2 mediates in Arabidopsis the heat-dependent phenotypes derived from farnesylation modification. (ncu.edu.tw)
  • Abstract: Arabidopsis HEAT-INTOERANT 5 (HIT5)/ENHANCED RESPONSE TO ABA 1 (ERA1) encodes the Îē-subunit of the protein farnesyltransferase (PFT), and the hit5/era1 mutant is better able to tolerate heat-shock stress than the wild type. (ncu.edu.tw)
  • 5) In vitro assays for protein farnesyltransferase (PFTase) and protein geranylgeranyltransferase type I (PGGTase-I) confirmed that ajoene inhibits protein prenylation. (unipd.it)
  • Furthermore, although lovastatin, which inhibits both protein geranylgeranylation and protein farnesylation, blocked PDGF receptor tyrosine phosphorylation, co-treatment with GGOH, but not FOH, reversed the lovastatin block. (nyu.edu)
  • Protein prenylation is the posttranslational attachment of either a farnesyl group or a geranylgeranyl group via a thioether linkage (-C-S-C-) to a cysteine at or near the carboxyl terminus of the protein. (biomedcentral.com)
  • Protein prenylation, found in eukaryotes, is a posttranslational modification in which one or two isoprenoid groups are added to the C terminus of selected proteins using either a farnesyl group or a geranylgeranyl group. (umn.edu)
  • In relation to the causative association between oncogenic Ras proteins and cancer, farnesyltransferase has become an important mechanistic drug discovery target. (guidetopharmacology.org)
  • The oncogenic protein Ras, which is prenylated, has been the subject of intense study in the past 20 years as a therapeutic target. (bvsalud.org)
  • Covalent attachment of these MVA-derived isoprenoid groups (prenylation) is a required function of several proteins that regulate cell proliferation. (unipd.it)
  • Here we describe the preparation of isoprenoid diphosphate analogues incorporating diazirine groups that can be used to probe interactions between prenylated proteins and other proteins that interact with them. (bvsalud.org)
  • These new isoprenoid analogues should be broadly useful in the studies of protein prenylation. (bvsalud.org)
  • The addition of a prenyltransferase inhibitor or the precursors to the native isoprenoid substrates lowers the levels of labeled prenylated proteins. (bvsalud.org)
  • The genes encoding CaaX protein prenyltransferases are considerably longer than those encoding non-CaaX subunits, as a result of longer introns. (biomedcentral.com)
  • The Îą subunits of protein prenyltransferases consist of tetratricopeptide repeats and are part of the tetratricopeptide repeat superfamily [ 5 ], which also includes functionally diverse proteins involved in transcription, co-chaperoning, protein transport, cell-cycle control and phosphorylation. (biomedcentral.com)
  • Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, G-protein Îģ-subunits, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. (guidetopharmacology.org)
  • Twenty alpha-amino acids are the subunits which are polymerized to form proteins. (lookformedical.com)
  • Prenylation attaches the cysteine residue and prenyl (15 residue farnesyl) group via a thioester. (freezingblue.com)
  • Most of small G proteins have the unique consensus C-terminal motifs containing at least one cysteine residue. (nii.ac.jp)
  • There is a superfamily of ras p21/ras p21-like small GTP-binding proteins (small G proteins) with GTPase activity. (nii.ac.jp)
  • Evidence is accumulating that small G proteins are involved in the regulation of cell growth and differentiation. (nii.ac.jp)
  • In this research project, we have investigated the C-terminal structures of small G proteins, purified the regulatory proteins for small G proteins, and made monoclonal antibodies against small G proteins and their regulatory proteins. (nii.ac.jp)
  • Small G proteins have two interconvertible forms, GDP-bound inactive and GTP-bound active forms. (nii.ac.jp)
  • We have purified and characterized several GDP/GTP exchange proteins (GDP dissociation stimulator (GDS) and GDP dissociation inhibitor (GDI)) and GTPase activating Proteins (GAP) for small G proteins. (nii.ac.jp)
  • Small G-proteins, monomeric GTPases, or the RAS (Rat sarcoma) superfamily are a large family of small guanine nucleotide-binding proteins with molecular weights ranging from 20 to 30 kDa [ 1 , 2 ]. (oncotarget.com)
  • Further points of attack seams to be other farnesylated proteins like small G-proteins, RHEB and centromer-binding-proteins. (uni-marburg.de)
  • 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)
  • These analogs alter prenylation specificity and reactivity suggesting that in vivo results obtained using these FPP analogs should be interpreted cautiously. (bvsalud.org)
  • In particular, protein lipid modification is essential for both stable anchoring of proteins to membranes and protein trafficking. (umn.edu)
  • Protein prenylation is a post-translational modification that consists of the attachment of 15 or 20 carbon isoprenoids near the C-termini of proteins. (umn.edu)
  • 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)
  • The fact that many Rho family effector proteins will specifically recognize the GTP bound form of the protein has been exploited experimentally to develop a powerful affinity purification assay that monitors RhoA protein activation. (cytoskeleton.com)
  • His-tagged RhoA protein (Cat. (cytoskeleton.com)
  • The RhoA activation assay was tested by loading the RhoA protein in cell lysates with either GTPÎģS or GDP. (cytoskeleton.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)
  • Furthermore, pyrin interacts with proline-serine-threonine phosphatase-interacting protein (PSTPIP1), also known as CD2-binding protein 1 (CD2BP1), which is a tyrosine-phosphorylated protein involved in cytoskeletal organization and thereby involved in immunologic cellular interactions. (medscape.com)
  • Labelling of smooth muscle cell cellular proteins with [3H]-FOH and [3H]-GGOH was significantly inhibited by ajoene. (unipd.it)
  • There are three different protein prenyltransferases in humans: farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) share the same motif (the CaaX box) around the cysteine in their substrates, and are thus called CaaX prenyltransferases, whereas geranylgeranyltransferase 2 (GGT2, also called Rab geranylgeranyltransferase) recognizes a different motif and is thus called a non-CaaX prenyltransferase [ 1 ]. (biomedcentral.com)
  • Gene structures and chromosomal locations of human protein prenyltransferase subunit genes. (biomedcentral.com)
  • Automatic comparisons of data from expressed sequence tags (ESTs) with genes (for example using the program Acembly, for which the results are available from the NCBI AceView server [ 2 ]) shows that all the human protein prenyltransferase genes have multiple alternative splice variants. (biomedcentral.com)
  • The chromosomal locations and number of exons from protein prenyltransferase genes in the major eukaryotic model organisms are shown in Table 2 . (biomedcentral.com)
  • Post-translational modifications are key players in the regulation of biological function of proteins, as well as modulators of activity and cellular localization. (umn.edu)
  • Studies using synthetic peptides and whole proteins demonstrate that these diazirine analogues are efficient substrates for prenyltransferases. (bvsalud.org)
  • 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)
  • 2001) Characterization of the antitumor effects of the selective farnesyl protein transferase inhibitor R115777 in vivo and in vitro. (guidetopharmacology.org)
  • We characterized the reactivity of four alkyne-containing analogs of FPP with purified protein farnesyltransferase and a small library of dansylated peptides using an in vitro continuous spectrofluorimetric assay. (bvsalud.org)
  • Gao S, Yu R, Zhou X. (2016) The Role of Geranylgeranyltransferase I-Mediated Protein Prenylation in the Brain. (guidetopharmacology.org)
  • Background: FTase recognizes and modifies many proteins with C-terminal CA 1 A 2 X sequences. (syr.edu)
  • abstract = "Background: FTase recognizes and modifies many proteins with C-terminal CA1A2X sequences. (syr.edu)
  • NIH-3T3 cells treated with the highly specific FTase inhibitor FTI-277 had no effect on PDGF receptor tyrosine phosphorylation or PDGF activation of mitogen-activated protein kinase (MAPK) at doses that completely inhibit FTase-dependent processing. (nyu.edu)
  • Glypiation, which is the addition of a GPI anchor that links proteins to lipids through glycan linkages. (wikipedia.org)
  • In biological systems, proteins, nucleic acids and lipids are precisely organized to form higher ordered structures across multiple length scales. (umn.edu)
  • Among these regulatory proteins, we have cloned the cDNAs of smg p21 GDS, smg p25A GDI, and rho GDI, and made monoclonal antibodies against them. (nii.ac.jp)
  • 1995) Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. (guidetopharmacology.org)
  • Mevalonate pathway produces farnesyl pyrophosphate and geranylgeranyl pyrophosphate essential in protein prenylation. (tocotrienolresearch.org)
  • What does this gene/protein do? (cancerindex.org)
  • Artemisinin-resistant parasites contain mutations in the gene encoding the Kelch 13 protein (K13). (elifesciences.org)
  • It is hypothesized that PCAIs work as anticancer agents by disrupting polyisoprenylation-dependent functional interactions of the G-Proteins. (oncotarget.com)
  • Thus, these results demonstrate that PDGF receptor tyrosine phosphorylation requires protein geranylgeranylation but not protein farnesylation and that the tyrosine phosphorylation levels of the receptor are modulated by a protein that is a substrate for GGTase I. (nyu.edu)
  • 2020) The balance of protein farnesylation and geranylgeranylation during the progression of nonalcoholic fatty liver disease. (guidetopharmacology.org)
  • Three different protein prenyltransferases (farnesyltransferase and geranylgeranyltransferases I and II) catalyze the attachment of prenyl lipid anchors 15 or 20 carbons long to the carboxyl termini of a variety of eukaryotic proteins. (biomedcentral.com)
  • It causes the production of abnormal proteins with impaired biological activity. (lookformedical.com)
  • (b) genes encoding non-CaaX protein prenyltransferases are much shorter. (biomedcentral.com)
  • In the online version, these sections contain links to more information about proteins encoded by over 17,000 known or predicted human genes. (cshlpress.com)
  • The genomic organization of the human genes that encode protein prenyltransferases is shown in Figure 1 . (biomedcentral.com)
  • Publications] Araki,S.: 'Role of the Cマterminal region of smg p25A in its interaction with membranes and the GDP/GTP exchange protein. (nii.ac.jp)
  • In other cases, proteins are not stable unless they contain oligosaccharides linked at the amide nitrogen of certain asparagine residues. (wikipedia.org)
  • This study tested this hypothesis by determining the effect of the PCAIs on the levels of RAS and related monomeric G-proteins. (oncotarget.com)