A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-
An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.
A 17-KDa cytoplasmic PEPTIDYLPROLYL ISOMERASE involved in immunoregulation. It is a member of the cyclophilin family of proteins that binds to CYCLOSPORINE.
Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
A cyclic undecapeptide from an extract of soil fungi. It is a powerful immunosupressant with a specific action on T-lymphocytes. It is used for the prophylaxis of graft rejection in organ and tissue transplantation. (From Martindale, The Extra Pharmacopoeia, 30th ed).
Members of a family of highly conserved proteins which are all cis-trans peptidyl-prolyl isomerases (PEPTIDYLPROLYL ISOMERASE). They bind the immunosuppressant drugs CYCLOSPORINE; TACROLIMUS and SIROLIMUS. They possess rotamase activity, which is inhibited by the immunosuppressant drugs that bind to them.
A widely distributed cell surface transmembrane glycoprotein that stimulates the synthesis of MATRIX METALLOPROTEINASES. It is found at high levels on the surface of malignant NEOPLASMS and may play a role as a mediator of malignant cell behavior.
A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-
A group of closely related cyclic undecapeptides from the fungi Trichoderma polysporum and Cylindocarpon lucidum. They have some antineoplastic and antifungal action and significant immunosuppressive effects. Cyclosporins have been proposed as adjuvants in tissue and organ transplantation to suppress graft rejection.
An actinomycete from which the antibiotic OLEANDOMYCIN is obtained.
Biological properties, processes, and activities of VIRUSES.
Transport proteins that carry specific substances in the blood or across cell membranes.
A CALCIUM and CALMODULIN-dependent serine/threonine protein phosphatase that is composed of the calcineurin A catalytic subunit and the calcineurin B regulatory subunit. Calcineurin has been shown to dephosphorylate a number of phosphoproteins including HISTONES; MYOSIN LIGHT CHAIN; and the regulatory subunits of CAMP-DEPENDENT PROTEIN KINASES. It is involved in the regulation of signal transduction and is the target of an important class of immunophilin-immunosuppressive drug complexes.
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.
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.
A macrolide isolated from the culture broth of a strain of Streptomyces tsukubaensis that has strong immunosuppressive activity in vivo and prevents the activation of T-lymphocytes in response to antigenic or mitogenic stimulation in vitro.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Proteins prepared by recombinant DNA technology.
The interactions between a host and a pathogen, usually resulting in disease.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
A constellation of responses that occur when an organism is exposed to excessive heat. Responses include synthesis of new proteins and regulation of others.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Agents that suppress immune function by one of several mechanisms of action. Classical cytotoxic immunosuppressants act by inhibiting DNA synthesis. Others may act through activation of T-CELLS or by inhibiting the activation of HELPER CELLS. While immunosuppression has been brought about in the past primarily to prevent rejection of transplanted organs, new applications involving mediation of the effects of INTERLEUKINS and other CYTOKINES are emerging.

Two distinct regions of cyclophilin B are involved in the recognition of a functional receptor and of glycosaminoglycans on T lymphocytes. (1/501)

Cyclophilin B is a cyclosporin A-binding protein exhibiting peptidyl-prolyl cis/trans isomerase activity. We have previously shown that it interacts with two types of binding sites on T lymphocytes. The type I sites correspond to specific functional receptors and the type II sites to sulfated glycosaminoglycans. The interactions of cyclophilin B with type I and type II sites are reduced in the presence of cyclosporin A and of a synthetic peptide mimicking the N-terminal part of cyclophilin B, respectively, suggesting that the protein possesses two distinct binding regions. In this study, we intended to characterize the areas of cyclophilin B involved in the interactions with binding sites present on Jurkat cells. The use of cyclophilin B mutants modified in the N-terminal region demonstrated that the 3Lys-Lys-Lys5 and 14Tyr-Phe-Asp16 clusters are probably solely required for the interactions with the type II sites. We further engineered mutants of the conserved central core of cyclophilin B, which bears the catalytic and the cyclosporin A binding sites as an approach to localize the binding regions for the type I sites. The enzymatic activity of cyclophilin B was dramatically reduced after substitution of the Arg62 and Phe67 residues, whereas the cyclosporin A binding activity was destroyed by mutation of the Trp128 residue and strongly decreased after modification of the Phe67 residue. Only the substitution of the Trp128 residue reduced the binding of the resulting cyclophilin B mutant to type I binding sites. The catalytic site of cyclophilin B therefore did not seem to be essential for cellular binding and the cyclosporin A binding site appeared to be partially involved in the binding to type I sites.  (+info)

Evidence that cyclophilin-A protects cells against oxidative stress. (2/501)

Cyclophilin-A is the cytosolic isoform of a family of peptidylproline cis-trans-isomerases that bind cyclosporin A. This study investigates the role of cyclophilin-A in necrotic cell death, induced by 'chemical ischaemia' and by t-butylhydroperoxide. An 18-mer antisense phosphorothioate oligodeoxynucleotide was used to target a translated region of cyclophilin-A mRNA in rat neonatal cardiomyocytes. After a 24 h exposure to the oligonucleotide, the amount of cyclophilin-A in the cells was decreased by at least 93% as judged by immunological and enzymic criteria. For the enzyme assays, peptidyl proline cis-trans-isomerase activity was measured fluorimetrically in small (10 microl) volumes of cell extract. Immunoblots were developed with a polyclonal anti-cyclophilin-A antibody after sample isoelectric focusing and SDS/PAGE. Cyclophilin-A suppression had no effect on cyanide-plus-2-deoxyglucose-induced cell death. However, cyclophilin-A-suppressed cells were markedly more sensitive to t-butylhydroperoxide. Cyclosporin A conferred some resistance to the peroxide in both types of cell, but protection was greater in cyclophilin-A-suppressed cells, where cyclosporin A increased the survival time 2-fold. It is concluded that two cyclophilin isoforms are involved, in quite different ways, in peroxide-induced cell death. Cyclophilin-A has a protective role. Another isoform, possibly mitochondrial cyclophilin-D, has a deleterious role, such that blockade by cyclosporin A leads to protection.  (+info)

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. (3/501)

A role for DnaK, the major E. coli Hsp70, in chaperoning de novo protein folding has remained elusive. Here we show that under nonstress conditions DnaK transiently associates with a wide variety of nascent and newly synthesized polypeptides, with a preference for chains larger than 30 kDa. Deletion of the nonessential gene encoding trigger factor, a ribosome-associated chaperone, results in a doubling of the fraction of nascent polypeptides interacting with DnaK. Combined deletion of the trigger factor and DnaK genes is lethal under normal growth conditions. These findings indicate important, partially overlapping functions of DnaK and trigger factor in de novo protein folding and explain why the loss of either chaperone can be tolerated by E. coli.  (+info)

The mitochondrial permeability transition pore and its role in cell death. (4/501)

This article reviews the involvement of the mitochondrial permeability transition pore in necrotic and apoptotic cell death. The pore is formed from a complex of the voltage-dependent anion channel (VDAC), the adenine nucleotide translocase and cyclophilin-D (CyP-D) at contact sites between the mitochondrial outer and inner membranes. In vitro, under pseudopathological conditions of oxidative stress, relatively high Ca2+ and low ATP, the complex flickers into an open-pore state allowing free diffusion of low-Mr solutes across the inner membrane. These conditions correspond to those that unfold during tissue ischaemia and reperfusion, suggesting that pore opening may be an important factor in the pathogenesis of necrotic cell death following ischaemia/reperfusion. Evidence that the pore does open during ischaemia/reperfusion is discussed. There are also strong indications that the VDAC-adenine nucleotide translocase-CyP-D complex can recruit a number of other proteins, including Bax, and that the complex is utilized in some capacity during apoptosis. The apoptotic pathway is amplified by the release of apoptogenic proteins from the mitochondrial intermembrane space, including cytochrome c, apoptosis-inducing factor and some procaspases. Current evidence that the pore complex is involved in outer-membrane rupture and release of these proteins during programmed cell death is reviewed, along with indications that transient pore opening may provoke 'accidental' apoptosis.  (+info)

Import and processing of heart mitochondrial cyclophilin D. (5/501)

Cyclophilins are a family of cyclosporin-A-binding proteins which catalyse rotation about prolyl peptide bonds. A mitochondrial isoform in mammalian cells, cyclophilin D, is a component of the permeability transition pore that is formed by the adenine nucleotide translocase and the voltage-dependent anion channel at contact sites between the inner and outer membrane. This study investigated the submitochondrial location of cyclophilin D by following the fate of radiolabelled protein following import. Precursor [(35)S]cyclophilin D was expressed in vitro from a PCR-generated cDNA. The precursor was imported by rat heart mitochondria and processed in a single step to a 21-kDa protein that was identical (SDS/PAGE) to an in vitro expressed mature protein and a cyclophilin D purified from rat heart mitochondria. No further modification of the mature protein could be demonstrated. Fractionation of mitochondria following import established that cyclophilin D locates only to the matrix. It is concluded that cyclophilin D binding to the permeability transition pore must occur at the inner face of the mitochondrial inner membrane.  (+info)

Cyclophilin B binding to platelets supports calcium-dependent adhesion to collagen. (6/501)

We have recently reported that cyclophilin B (CyPB), a secreted cyclosporine-binding protein, could bind to T lymphocytes through interactions with two types of binding sites. The first ones, referred to as type I, involve interactions with the conserved domain of CyPB and promote the endocytosis of surface-bound ligand, while the second type of binding sites, termed type II, are represented by glycosaminoglycans (GAG). Here, we further investigated the interactions of CyPB with blood cell populations. In addition to lymphocytes, CyPB was found to interact mainly with platelets. The binding is specific, with a dissociation constant (kd) of 9 +/- 3 nmol/L and the number of sites estimated at 960 +/- 60 per cell. Platelet glycosaminoglycans are not required for the interactions, but the binding is dramatically reduced by active cyclosporine derivatives. We then analyzed the biologic effects of CyPB and found a significant increase in platelet adhesion to collagen. Concurrently, CyPB initiates a transmembranous influx of Ca(2+) and induces the phosphorylation of the P-20 light chains of myosin. Taken together, the present results demonstrate for the first time that extracellular CyPB specifically interacts with platelets through a functional receptor related to the lymphocyte type I binding sites and might act by regulating the activity of a receptor-operated membrane Ca(2+) channel.  (+info)

A cyclophilin B gene encodes antigenic epitopes recognized by HLA-A24-restricted and tumor-specific CTLs. (7/501)

We have studied Ags recognized by HLA class I-restricted CTLs established from tumor site to better understand the molecular basis of tumor immunology. HLA-A24-restricted and tumor-specific CTLs established from T cells infiltrating into lung adenocarcinoma recognized the two antigenic peptides encoded by a cyclophilin B gene, a family of genes for cyclophilins involved in T cell activation. These two cyclophilin B peptides at positions 84-92 and 91-99 induced HLA-A24-restricted CTL activity against tumor cells in PBMCs of leukemia patients, but not in epithelial cancer patients or in healthy donors. In contrast, the modified peptides at position 2 from phenylalanine to tyrosine, which had more than 10 times higher binding affinities to HLA-A24 molecules, could induce HLA-A24-restricted CTL activity against tumor cells in PBMCs from leukemia patients, epithelial cancer patients, or healthy donors. PHA-activated normal T cells were resistant to lysis by the CTL line or by these peptide-induced CTLs. These results indicate that a cyclophilin B gene encodes antigenic epitopes recognized by CTLs at the tumor site, although T cells in peripheral blood (except for those from leukemia patients) are immunologically tolerant to the cyclophilin B. These peptides might be applicable for use in specific immunotherapy of leukemia patients or that of epithelial cancer patients.  (+info)

Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis. (8/501)

Here, we describe the isolation of adenine nucleotide translocase-1 (ANT-1) in a screen for dominant, apoptosis-inducing genes. ANT-1 is a component of the mitochondrial permeability transition complex, a protein aggregate connecting the inner with the outer mitochondrial membrane that has recently been implicated in apoptosis. ANT-1 expression led to all features of apoptosis, such as phenotypic alterations, collapse of the mitochondrial membrane potential, cytochrome c release, caspase activation, and DNA degradation. Both point mutations that impair ANT-1 in its known activity to transport ADP and ATP as well as the NH(2)-terminal half of the protein could still induce apoptosis. Interestingly, ANT-2, a highly homologous protein could not lead to cell death, demonstrating the specificity of the signal for apoptosis induction. In contrast to Bax, a proapoptotic Bcl-2 gene, ANT-1 was unable to elicit a form of cell death in yeast. This and the observed repression of apoptosis by the ANT-1-interacting protein cyclophilin D suggest that the suicidal effect of ANT-1 is mediated by specific protein-protein interactions within the permeability transition pore.  (+info)

Cyclophilins are a family of proteins that have peptidyl-prolyl isomerase activity, which means they help with the folding and functioning of other proteins in cells. They were first identified as binding proteins for the immunosuppressive drug cyclosporine A, hence their name.

Cyclophilins are found in various organisms, including humans, and play important roles in many cellular processes such as signal transduction, protein trafficking, and gene expression. In addition to their role in normal cell function, cyclophilins have also been implicated in several diseases, including viral infections, cancer, and neurodegenerative disorders.

In medicine, the most well-known use of cyclophilins is as a target for immunosuppressive drugs used in organ transplantation. Cyclosporine A and its derivatives work by binding to cyclophilins, which inhibits their activity and subsequently suppresses the immune response.

Peptidylprolyl Isomerase (PPIase) is an enzyme that catalyzes the cis-trans isomerization of peptidyl-prolyl bonds in proteins. This isomerization process, which involves the rotation around a proline bond, is a rate-limiting step in protein folding and can be a significant factor in the development of various diseases, including neurodegenerative disorders and cancer.

PPIases are classified into three families: cyclophilins, FK506-binding proteins (FKBPs), and parvulins. These enzymes play important roles in protein folding, trafficking, and degradation, as well as in signal transduction pathways and the regulation of gene expression.

Inhibitors of PPIases have been developed as potential therapeutic agents for various diseases, including transplant rejection, autoimmune disorders, and cancer. For example, cyclosporine A and FK506 are immunosuppressive drugs that inhibit cyclophilins and FKBPs, respectively, and are used to prevent transplant rejection.

Cyclophilin A is a type of intracellular protein that belongs to the immunophilin family. It has peptidyl-prolyl cis-trans isomerase activity, which means it helps in folding and assembling other proteins by catalyzing the cis-trans isomerization of proline residues.

Cyclophilin A is widely distributed in various tissues and cells, including immune cells such as T lymphocytes. It plays a crucial role in the immune system by binding to and activating the immunosuppressive drug cyclosporine A, which is used to prevent rejection of transplanted organs.

In addition to its role in protein folding and immunosuppression, Cyclophilin A has been implicated in various cellular processes such as signal transduction, gene expression, and apoptosis (programmed cell death). It also plays a role in viral replication, particularly of HIV-1, the virus that causes AIDS.

Amino acid isomerases are a class of enzymes that catalyze the conversion of one amino acid stereoisomer to another. These enzymes play a crucial role in the metabolism and biosynthesis of amino acids, which are the building blocks of proteins.

Amino acids can exist in two forms, called L- and D-stereoisomers, based on the spatial arrangement of their constituent atoms around a central carbon atom. While most naturally occurring amino acids are of the L-configuration, some D-amino acids are also found in certain proteins and peptides, particularly in bacteria and lower organisms.

Amino acid isomerases can convert one stereoisomer to another by breaking and reforming chemical bonds in a process that requires energy. This conversion can be important for the proper functioning of various biological processes, such as protein synthesis, neurotransmitter metabolism, and immune response.

Examples of amino acid isomerases include proline racemase, which catalyzes the interconversion of L-proline and D-proline, and serine hydroxymethyltransferase, which converts L-serine to D-serine. These enzymes are essential for maintaining the balance of amino acids in living organisms and have potential therapeutic applications in various diseases, including neurodegenerative disorders and cancer.

Cyclosporine is a medication that belongs to a class of drugs called immunosuppressants. It is primarily used to prevent the rejection of transplanted organs, such as kidneys, livers, and hearts. Cyclosporine works by suppressing the activity of the immune system, which helps to reduce the risk of the body attacking the transplanted organ.

In addition to its use in organ transplantation, cyclosporine may also be used to treat certain autoimmune diseases, such as rheumatoid arthritis and psoriasis. It does this by suppressing the overactive immune response that contributes to these conditions.

Cyclosporine is available in capsule, oral solution, and injectable forms. Common side effects of the medication include kidney problems, high blood pressure, tremors, headache, and nausea. Long-term use of cyclosporine can also increase the risk of certain types of cancer and infections.

It is important to note that cyclosporine should only be used under the close supervision of a healthcare provider, as it requires regular monitoring of blood levels and kidney function.

Immunophilins are a group of intracellular proteins that have peptidyl-prolyl isomerase (PPIase) activity, which enables them to catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. They play crucial roles in protein folding, trafficking, and assembly, as well as in immunoregulation and signal transduction processes.

Two major classes of immunophilins are FK506-binding proteins (FKBPs) and cyclophilins. These proteins can bind to immunosuppressive drugs like FK506 (tacrolimus) and cyclosporin A, respectively, forming complexes that inhibit the activity of calcineurin, a phosphatase involved in T-cell activation. This interaction leads to an inhibition of immune responses and is exploited in transplantation medicine to prevent graft rejection.

Immunophilins also participate in various cellular processes, such as protein trafficking, neuroprotection, and regulation of gene expression, by interacting with other proteins or acting as chaperones during protein folding. Dysregulation of immunophilin function has been implicated in several diseases, including cancer, neurological disorders, and viral infections.

CD147 (also known as basigin or EMMPRIN) is a transmembrane protein that belongs to the immunoglobulin superfamily. It is widely expressed on various cell types including immune cells, epithelial cells, and endothelial cells. CD147 plays important roles in several biological processes such as cell adhesion, migration, and activation of matrix metalloproteinases (MMPs), which are enzymes involved in extracellular matrix remodeling.

CD147 can also function as an antigen, a molecule that is recognized by the immune system and can stimulate an immune response. CD147 has been identified as a receptor for the cyclophilin A protein of several enveloped viruses, including HIV-1, dengue virus, and hepatitis C virus. The interaction between CD147 and these viral proteins is important for viral entry into host cells and can also modulate the immune response to infection.

In addition, CD147 has been implicated in various pathological conditions such as cancer, inflammation, and autoimmune diseases. It has been shown to promote tumor growth, invasion, and metastasis, and its expression is often upregulated in various types of cancer. CD147 has also been found to contribute to the pathogenesis of several inflammatory and autoimmune diseases, including rheumatoid arthritis, multiple sclerosis, and lupus erythematosus.

Overall, CD147 is a multifunctional protein that can act as an antigen and play important roles in various biological processes, pathological conditions, and infectious diseases.

Tacrolimus binding proteins, also known as FK506 binding proteins (FKBPs), are a group of intracellular proteins that bind to the immunosuppressive drug tacrolimus (also known as FK506) and play a crucial role in its mechanism of action. Tacrolimus is primarily used in organ transplantation to prevent rejection of the transplanted organ.

FKBPs are a family of peptidyl-prolyl cis-trans isomerases (PPIases) that catalyze the conversion of proline residues from their cis to trans conformations in proteins, thereby regulating protein folding and function. FKBP12, a member of this family, has a high affinity for tacrolimus and forms a complex with it upon entry into the cell.

The formation of the tacrolimus-FKBP12 complex inhibits calcineurin, a serine/threonine phosphatase that plays a critical role in T-cell activation. Calcineurin inhibition prevents the dephosphorylation and nuclear translocation of the transcription factor NFAT (nuclear factor of activated T-cells), thereby blocking the expression of genes involved in T-cell activation, proliferation, and cytokine production.

In summary, tacrolimus binding proteins are intracellular proteins that bind to tacrolimus and inhibit calcineurin, leading to the suppression of T-cell activation and immune response, which is essential in organ transplantation and other immunological disorders.

Cyclosporins are a group of cyclic undecapeptides that have immunosuppressive properties. The most well-known and widely used cyclosporin is cyclosporine A, which is commonly used in organ transplantation to prevent rejection. It works by inhibiting the activation of T-cells, a type of white blood cell that plays a central role in the immune response. By suppressing the activity of T-cells, cyclosporine A reduces the risk of an immune response against the transplanted organ.

Cyclosporins are also used in the treatment of autoimmune diseases, such as rheumatoid arthritis and psoriasis, where they help to reduce inflammation and prevent damage to tissues. Like all immunosuppressive drugs, cyclosporins can increase the risk of infection and cancer, so they must be used with caution and under close medical supervision.

"Streptomyces antibioticus" is not a medical term per se, but rather a scientific name used in microbiology and biochemistry. It refers to a specific species of bacteria belonging to the genus "Streptomyces," which are known for their ability to produce various antibiotics. The species "S. antibioticus" has been particularly important in the discovery and production of several clinically relevant antibiotics, such as neomycin and ribostamycin. These antibiotics have been used in medical treatments to target various bacterial infections. However, it is essential to note that the bacteria itself is not a medical condition or disease; instead, its products (antibiotics) are significant in medical contexts.

I'm sorry for any confusion, but "Virus Physiological Phenomena" is not a widely recognized or established medical term or concept. It seems to be a combination of two concepts: "virus" and "physiological phenomena."

1. A virus is a small infectious agent that replicates inside the living cells of an organism. Viruses can cause many different types of illnesses, from the common cold to more serious diseases like HIV/AIDS or hepatitis.

2. Physiological phenomena refer to the functions and activities of living organisms and their parts, including cells, tissues, and organs.

If you're looking for information about how viruses affect physiological processes in the body, I would be happy to help provide some general information on that topic! However, it would be best to consult a specific medical text or expert for more detailed or specialized knowledge.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Calcineurin is a calcium-calmodulin-activated serine/threonine protein phosphatase that plays a crucial role in signal transduction pathways involved in immune response and neuronal development. It consists of two subunits: the catalytic A subunit (calcineurin A) and the regulatory B subunit (calcineurin B). Calcineurin is responsible for dephosphorylating various substrates, including transcription factors, which leads to changes in their activity and ultimately affects gene expression. In the immune system, calcineurin plays a critical role in T-cell activation by dephosphorylating the nuclear factor of activated T-cells (NFAT), allowing it to translocate into the nucleus and induce the expression of cytokines and other genes involved in the immune response. Inhibitors of calcineurin, such as cyclosporine A and tacrolimus, are commonly used as immunosuppressive drugs to prevent organ rejection after transplantation.

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.

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.

Tacrolimus is an immunosuppressant drug that is primarily used to prevent the rejection of transplanted organs. It works by inhibiting the activity of T-cells, which are a type of white blood cell that plays a central role in the body's immune response. By suppressing the activity of these cells, tacrolimus helps to reduce the risk of an immune response being mounted against the transplanted organ.

Tacrolimus is often used in combination with other immunosuppressive drugs, such as corticosteroids and mycophenolate mofetil, to provide a comprehensive approach to preventing organ rejection. It is available in various forms, including capsules, oral solution, and intravenous injection.

The drug was first approved for use in the United States in 1994 and has since become a widely used immunosuppressant in transplant medicine. Tacrolimus is also being studied as a potential treatment for a variety of other conditions, including autoimmune diseases and cancer.

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.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Host-pathogen interactions refer to the complex and dynamic relationship between a living organism (the host) and a disease-causing agent (the pathogen). This interaction can involve various molecular, cellular, and physiological processes that occur between the two entities. The outcome of this interaction can determine whether the host will develop an infection or not, as well as the severity and duration of the illness.

During host-pathogen interactions, the pathogen may release virulence factors that allow it to evade the host's immune system, colonize tissues, and obtain nutrients for its survival and replication. The host, in turn, may mount an immune response to recognize and eliminate the pathogen, which can involve various mechanisms such as inflammation, phagocytosis, and the production of antimicrobial agents.

Understanding the intricacies of host-pathogen interactions is crucial for developing effective strategies to prevent and treat infectious diseases. This knowledge can help identify new targets for therapeutic interventions, inform vaccine design, and guide public health policies to control the spread of infectious agents.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Molecular chaperones are a group of proteins that assist in the proper folding and assembly of other protein molecules, helping them achieve their native conformation. They play a crucial role in preventing protein misfolding and aggregation, which can lead to the formation of toxic species associated with various neurodegenerative diseases. Molecular chaperones are also involved in protein transport across membranes, degradation of misfolded proteins, and protection of cells under stress conditions. Their function is generally non-catalytic and ATP-dependent, and they often interact with their client proteins in a transient manner.

The Heat-Shock Response is a complex and highly conserved stress response mechanism present in virtually all living organisms. It is activated when the cell encounters elevated temperatures or other forms of proteotoxic stress, such as exposure to toxins, radiation, or infectious agents. This response is primarily mediated by a group of proteins known as heat-shock proteins (HSPs) or chaperones, which play crucial roles in protein folding, assembly, transport, and degradation.

The primary function of the Heat-Shock Response is to protect the cell from damage caused by misfolded or aggregated proteins that can accumulate under stress conditions. The activation of this response leads to the rapid transcription and translation of HSP genes, resulting in a significant increase in the intracellular levels of these chaperone proteins. These chaperones then assist in the refolding of denatured proteins or target damaged proteins for degradation via the proteasome or autophagy pathways.

The Heat-Shock Response is critical for maintaining cellular homeostasis and ensuring proper protein function under stress conditions. Dysregulation of this response has been implicated in various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Immunosuppressive agents are medications that decrease the activity of the immune system. They are often used to prevent the rejection of transplanted organs and to treat autoimmune diseases, where the immune system mistakenly attacks the body's own tissues. These drugs work by interfering with the immune system's normal responses, which helps to reduce inflammation and damage to tissues. However, because they suppress the immune system, people who take immunosuppressive agents are at increased risk for infections and other complications. Examples of immunosuppressive agents include corticosteroids, azathioprine, cyclophosphamide, mycophenolate mofetil, tacrolimus, and sirolimus.

Other cyclophilins have similar structures to cyclophilin A. The cyclosporin-cyclophilin A complex inhibits a calcium/ ... Cyclophilin A is a cytosolic and highly abundant protein. The protein belongs to a family of isozymes, including cyclophilins B ... Cyclophilin D (PPIF, note that literature is confusing, the mitochondrial cyclophilin is encoded by the PPIF gene), which is ... Cyclophilin inhibitors, such as cyclosporin, are being developed to treat neurodegenerative diseases. Cyclophilin inhibition ...
As a cyclophilin, PPIB binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin ... Price ER, Zydowsky LD, Jin MJ, Baker CH, McKeon FD, Walsh CT (Apr 1991). "Human cyclophilin B: a second cyclophilin gene ... Mikol V, Kallen J, Walkinshaw MD (1994). "X-ray structure of a cyclophilin B/cyclosporin complex: comparison with cyclophilin A ... As a cyclophilin, PPIB binds cyclosporin A (CsA) and can be found within the cell or secreted by the cell. PPIB is the second ...
As a cyclophilin, PPIC binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin ... Depletion of these two cyclophilins lead to hyperoxidation of the ER. In the brain, PPIC complexes with cyclophilin C- ... Like other cyclophilins, PPIC forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti- ... Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C (Mar 2005). "Roles of cyclophilins in cancers and other organ systems". World ...
As a cyclophilin, PPIF binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin ... Thus, cyclophilins may function in cardioprotection during ischemia-reperfusion injury. Currently, cyclophilin expression is ... Like other cyclophilins, PPIF forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti- ... It has also been referred to as, but should not be confused with, cyclophilin D (CypD), which is encoded by the PPID gene. As a ...
As a cyclophilin, PPID binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets calcineurin ... Thus, cyclophilins may function in cardioprotection during ischemia-reperfusion injury. Currently, cyclophilin expression is ... Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the PPID gene on ... Like other cyclophilins, PPID forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti- ...
As a cyclophilin, PPIE also binds the immunosuppressive drug CsA to form a CsA-cyclophilin complex, which then targets ... Thus, cyclophilins may function in cardioprotection during ischemia-reperfusion injury. Currently, cyclophilin expression is ... Peptidylprolyl isomerase E (cyclophilin E), also known as PPIE, is an enzyme which in humans is encoded by the PPIE gene on ... Wang Z, Liu X, Zhao Z, Xu C, Zhang K, Chen C, Sun L, Gao GF, Ye X, Liu W (2011). "Cyclophilin E functions as a negative ...
Like other cyclophilins, PPIA forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti- ... Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C (Mar 2005). "Roles of cyclophilins in cancers and other organ systems". World ... Peptidylprolyl isomerase A (PPIA), also known as cyclophilin A (CypA) or rotamase A is an enzyme that in humans is encoded by ... Wei Y, Jinchuan Y, Yi L, Jun W, Zhongqun W, Cuiping W (Jun 2013). "Antiapoptotic and proapoptotic signaling of cyclophilin A in ...
... is a type I integral membrane receptor that has many ligands, including the cyclophilin (CyP) proteins Cyp-A and CyP-B ... June 2002). "Active site residues of cyclophilin A are crucial for its signaling activity via CD147". The Journal of Biological ... June 2002). "Active site residues of cyclophilin A are crucial for its signaling activity via CD147". The Journal of Biological ... Yurchenko V, Constant S, Bukrinsky M (March 2006). "Dealing with the family: CD147 interactions with cyclophilins". Immunology ...
Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK (1997). "RS cyclophilins: identification of an NK-TR1-related cyclophilin ...
Lin CL, Leu S, Lu MC, Ouyang P (2004). "Over-expression of SR-cyclophilin, an interaction partner of nuclear pinin, releases SR ... Nestel FP, Colwill K, Harper S, Pawson T, Anderson SK (Jan 1997). "RS cyclophilins: identification of an NK-TR1-related ... "Entrez Gene: PPIG peptidylprolyl isomerase G (cyclophilin G)". Lin, Chun Lun; Leu Steve; Lu Ming Chu; Ouyang Pin (Aug 2004). " ... 2004). "The human nuclear SRcyp is a cell cycle-regulated cyclophilin". J. Biol. Chem. 279 (21): 22322-30. doi:10.1074/jbc. ...
Horowitz DS, Kobayashi R, Krainer AR (Dec 1997). "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a ... Horowitz DS, Lee EJ, Mabon SA, Misteli T (Feb 2002). "A cyclophilin functions in pre-mRNA splicing". The EMBO Journal. 21 (3): ... a nuclear cyclophilin" (PDF). The Journal of Biological Chemistry. 275 (11): 7439-42. doi:10.1074/jbc.275.11.7439. PMID ... "Crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide". Journal of Molecular ...
FKBP-12 and cyclophilins both share common peptide-prolyl isomerase activity. While the majority of the Peptide bonds within ... These two families are: "cyclosporin-binding cyclophilins (CyPs)" and "FK506-binding proteins (FKBPs)". In 2005, a group of ...
Ferreira PA, Nakayama TA, Pak WL, Travis GH (Oct 1996). "Cyclophilin-related protein RanBP2 acts as chaperone for red/green ... Ferreira PA, Yunfei C, Schick D, Roepman R (Sep 1998). "The cyclophilin-like domain mediates the association of Ran-binding ... Yi H, Friedman JL, Ferreira PA (Nov 2007). "The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the ... Ferreira PA, Hom JT, Pak WL (Sep 1995). "Retina-specifically expressed novel subtypes of bovine cyclophilin". The Journal of ...
This gene is a member of the cyclophilin family of peptidylprolyl isomerases. The cyclophilins are a highly conserved ... 2005). "Cell surface expression of CD147/EMMPRIN is regulated by cyclophilin 60". J. Biol. Chem. 280 (30): 27866-71. doi: ... "Entrez Gene: PPIL2 peptidylprolyl isomerase (cyclophilin)-like 2". Wang BB, Hayenga KJ, Payan DG, Fisher JM (1996). " ... 2010). "Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases". PLOS Biol. ...
This gene encodes a member of the cyclophilin family. Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl imide ... Huang LL, Zhao XM, Huang CQ, Yu L, Xia ZX (Mar 2005). "Structure of recombinant human cyclophilin J, a novel member of the ... "Entrez Gene: PPIL3 peptidylprolyl isomerase (cyclophilin)-like 3". Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high ... cyclophilin)-like gene (PPIL3) from human fetal brain". Cytogenetics and Cell Genetics. 92 (3-4): 231-6. doi:10.1159/000056909 ...
This gene is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved ... "Entrez Gene: PPIL1 peptidylprolyl isomerase (cyclophilin)-like 1". Tripodis N, Mason R, Humphray SJ, et al. (1999). "Physical ... expression and chromosomal mapping of a novel cyclophilin-related gene (PPIL1) from human fetal brain". Cytogenet Cell Genet. ...
Examples include photoisomerase and immunophilins such as cyclophilin. cis-trans-Isomerases at the U.S. National Library of ...
This gene is a member of the cyclophilin family of peptidylprolyl isomerases. The cyclophilins are a highly conserved family, ... "Entrez Gene: PPIL4 peptidylprolyl isomerase (cyclophilin)-like 4". Zeng L, Zhou Z, Xu J, et al. (2002). "Molecular cloning, ... structure and expression of a novel nuclear RNA-binding cyclophilin-like gene (PPIL4) from human fetal brain". Cytogenet. Cell ...
... which binds cyclophilin. Both the FKBP-tacrolimus complex and the cyclosporin-cyclophilin complex inhibit a phosphatase called ... Along with cyclophilin, FKBPs belong to the immunophilin family. FKBP1A (also known as FKBP12) is notable in humans for binding ... Liu J, Farmer JD, Lane WS, Friedman J, Weissman I, Schreiber SL (August 1991). "Calcineurin is a common target of cyclophilin- ... constitute a family of proteins that have prolyl isomerase activity and are related to the cyclophilins in function, though not ...
When bound to cyclophilin B, cyclosporin A binds and inactivates the key signaling intermediate calcineurin. The protein ... Bram RJ, Crabtree GR (1994). "Calcium signalling in T cells stimulated by a cyclophilin B-binding protein". Nature. 371 (6495 ... Tovey SC, Bootman MD, Lipp P, Berridge MJ, Bram RJ (2000). "Calcium-modulating cyclophilin ligand desensitizes hormone-evoked ... Guo S, Lopez-Ilasaca M, Dzau VJ (2005). "Identification of calcium-modulating cyclophilin ligand (CAML) as transducer of ...
The Role of Cyclophilin D in learning and memory. Brush, F. Robert (2003). "Selection for Differences in avoidance Learning: ...
Cyp33 is a cyclophilin that has the ability to isomerize H3 proline residues at P16 and P30 positions. Histones H2A and H2B ... Cyclophilin A uses an "electrostatic handle" to pull proline into cis and trans formations. Most of these biological functions ... PPIases are present in three types: cyclophilins, FK507-binding proteins, and the parvulins. PPIase enzymes catalyze the ...
To the end of this, necrosis occurs by physical interaction with the PTP regulator cyclophilin D (CypD). The mitochondrial p53- ... Alam, M.R.; D. Baetz; M. Ovize (2015). "Cyclophilin D and myocardial ischemia-reperfusion injury: a fresh perspective". J Mol ...
Cyclosporin A binds to cyclophilin D to block the opening of MPTP, and thus decreases the release of protein cytochrome C, ... October 2010). "Cyclophilin D controls mitochondrial pore-dependent Ca(2+) exchange, metabolic flexibility, and propensity for ... It does this by forming a complex with cyclophilin to block the phosphatase activity of calcineurin, which in turn decreases ... This cyclosporin-cyclophilin complex inhibits calcineurin, which is normally responsible for activating the transcription of ...
... (INN), or Debio 025, DEB025, (or UNIL-025) is a cyclophilin inhibitor. Its structure is reminiscent of, and ... April 2008). "Inhibition of human immunodeficiency virus type 1 replication in human cells by Debio-025, a novel cyclophilin ... December 2008). "Debio 025, a cyclophilin binding molecule, is highly efficient in clearing HCV replicon containing cells, ... a cyclophilin inhibitor, in the dystrophic mdx mouse, a model for Duchenne muscular dystrophy". British Journal of Pharmacology ...
October 2011). "The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors ...
Identification of Cyclophilins as Target for Pan-Coronavirus Inhibitors". PLOS Pathogens. 7 (10): e1002331. doi:10.1371/journal ...
October 2011). "The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors ...
October 2011). "The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors ...
Sanglifehrin is a mixed polyketide / non-ribosomal peptide natural product found to be a potent cyclophilin inhibitor and ... "Biotica nominates drug candidate, BC556, a cyclophilin inhibitor to treat Hepatitis C". www.businesswire.com. 31 October 2011. ... "NeuroVive: NeuroVive acquires highly potent, novel cyclophilin inhibitors from Biotica - Abliva". abliva.com. 11 March 2013. ...
Other cyclophilins have similar structures to cyclophilin A. The cyclosporin-cyclophilin A complex inhibits a calcium/ ... Cyclophilin A is a cytosolic and highly abundant protein. The protein belongs to a family of isozymes, including cyclophilins B ... Cyclophilin D (PPIF, note that literature is confusing, the mitochondrial cyclophilin is encoded by the PPIF gene), which is ... Cyclophilin inhibitors, such as cyclosporin, are being developed to treat neurodegenerative diseases. Cyclophilin inhibition ...
Timeline for Protein Cyclophilin 40 from a.118.8.1: Tetratricopeptide repeat (TPR): *Protein Cyclophilin 40 from a.118.8.1: ... Protein Cyclophilin 40 from a.118.8.1: Tetratricopeptide repeat (TPR) appears in SCOP 1.59. *Protein Cyclophilin 40 from a. ... Lineage for Protein: Cyclophilin 40. *Root: SCOP 1.57 *. Class a: All alpha proteins [46456] (144 folds). ... More info for Protein Cyclophilin 40 from a.118.8.1: Tetratricopeptide repeat (TPR). ...
... Inflammation. 2017 Oct;40(5 ... This study is designed to explore the effects of cyclophilin A (CypA) on macrophage polarization and describe the underlying ...
Crystal structure of cyclophilin D in complex with CsA analogue, JW47. ... The peptidylprolyl isomerase, cyclophilin D (CypD, PPIF), is a positive regulator of the pore, and genetic down-regulation or ... The peptidylprolyl isomerase, cyclophilin D (CypD, PPIF), is a positive regulator of the pore, and genetic down-regulation or ... Current inhibitors of peptidylprolyl isomerases show no selectivity between the tightly conserved cyclophilin paralogs and ...
The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and ... The cyclophilin-like domain (CLD) of Ran-binding protein-2 (RanBP2/Nup358) associates specifically with at least one subunit, ... "The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and ... The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and ...
Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury. Free Radic Res. 2011 Feb; 45(2 ... "Cyclophilins" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Cyclophilins" by people in this website by year, and whether " ... Cyclophilin D as a drug target. Curr Med Chem. 2003 Aug; 10(16):1485-506. ...
Recombinant Protein Cyclophilin H, his,,Cyclophilin H, his Protein ... U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, ... Cyclophilin H, his Recombinant Protein. Product code: 32-2250. *specify in mg or ml ...
Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro. Additionally, CyP40 ameliorated silver- ... Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro. Additionally, CyP40 ameliorated silver- ... "Human Cyclophilin 40 Unravels Neurotoxic Amyloids" (2017). Molecular Medicine Faculty Publications. 259. https://digitalcommons ...
Cyclophilin inhibitors on the market or in clinical trials are cyclosporin (a natural product) or cyclosporin derivatives; the ... Mike Peel, CSO of Cypralis, said: The discovery of completely synthetic and very potent cyclophilin inhibitors that fully ... Selcias collaboration with Cypralis and Gilead delivered a set of synthetic macrocyclic cyclophilin inhibitors inspired by the ... The paper describes how novel macrocyclic non-immunosuppressive cyclophilin inhibitors, with high potency in both biochemical ...
Ermittlung der räumlichen Struktur von an Cyclophilin gebundenem Cyclosporin A mittels isotopengefilterter ... PROTONEN-KERNRESONANZSPEKTROSKOPIE; CYCLOSPORIN-A (ANTIBIOTIKA); PEPTIDYLPROLYL-ISOMERASE, CYCLOPHILIN (ENZYME); PROTON NUCLEAR ...
Cyclophilin A - A Mediator of Cardiovascular Disease Bradford C. Berk, MD, PhD. Distinguished University Professor in Medicine, ...
Peptidyl-prolyl cis-trans isomerase, cyclophilin type (NCBI) PpiB protein (EC 5.2.1.8) 1119717 1119106 - 15466049 ... MMP1128 MMP1128 Peptidyl-prolyl cis-trans isomerase, cyclophilin type (NCBI). × Error message. *Unable to create CTools CSS ... O) COG652 , Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family (5.2.1.8) Peptidylprolyl isomerase. ...
Abstract: Peptidylprolyl isomerases (PPIase) cyclophilin A (CypA, encoded by PPIA) is a typical member of the Cyclophilin ... 摘要: Cyclophilin A (简称CypA)由PPIA(Peptidylprolyl isomerase A)基因编码,是典型的Cyclophilin家族蛋白,具有肽基脯氨酰顺反异构酶活性,在蛋白质的折叠和转运、信号转导、炎症、免疫调节、细胞凋亡 ... 脊椎动物Cyclophilin A肽基脯氨酰顺反异构酶活性及遗传变异分析 任丽倩1, 2, 刘薇
Emerging picture of host chaperone and cyclophilin roles in RNA virus replication. / Nagy, P. D.; Wang, R. Y.; Pogany, J. et al ... Nagy PD, Wang RY, Pogany J, Hafren A, Makinen K. Emerging picture of host chaperone and cyclophilin roles in RNA virus ... Nagy, PD, Wang, RY, Pogany, J, Hafren, A & Makinen, K 2011, Emerging picture of host chaperone and cyclophilin roles in RNA ... Nagy, P. D., Wang, R. Y., Pogany, J., Hafren, A., & Makinen, K. (2011). Emerging picture of host chaperone and cyclophilin ...
Structure/epitope analysis and IgE binding activities of three cyclophilin family proteins from Dermatophagoides pteronyssinus ... Structure/epitope analysis and IgE binding activities of three cyclophilin family proteins from Dermatophagoides pteronyssinus ...
Ontario, QC, Canada). Although normalization to Cyclophilin A was performed, RPL13 and Ubiquitin C showed similar trends and ... all values were normalized to Cyclophilin A (Table 7). The 2−ΔΔCT method was used for relative quantification of RT-qPCR ... Cyclophilin A. 5′-ACAGCTCAAAGGAGACGCGGCCCA-3′. F 5′-CCCACCGTGTTCTTCGACAT-3′. R 5′-TTTCTGCTGTCTTTGGGACCTT-3′. ...
The standard curves, multiplexed with cyclophilin, showed the following reaction efficiencies: Gimap8: , Gimap7: , Gimap4: , ... after normalization to cyclophilin. Black columns represent and grey hatched columns represent . Data is expressed as a ... To compare Gimap and Lr8 gene expression across multiple tissues, data was first normalized to cyclophilin then scaled and ... Figure 4). We observed the same expression pattern whether the data were normalized to cyclophilin or to total RNA (data not ...
CYCLOPHILIN APEPTIDE FROM THE HIV-1 CAPSID PROTEIN ...
Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site ... Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site ...
Launch Cyclophilins and FK506 binding protein (FKBPs) are mobile goals TKI-258 for the immunosuppressive medications ... Within steroid receptor heterocomplexes the large tetratricopeptide repeat-containing immunophilins cyclophilin 40. Within ... Individual cyclophilin 40 (CyP40; Kieffer et al 1993) and its own bovine homolog (Ratajczak et al 1993) had been cloned from ... steroid receptor heterocomplexes the large tetratricopeptide repeat-containing immunophilins cyclophilin 40 (CyP40) FKBP51 and ...
HUMAN CYCLOPHILIN D IN COMPLEX WITH N-CYCLOPENTYL-N-PYRIDIN-2- YLMETHYL-OXALAMIDE - 6R9X , canSARS ... HUMAN CYCLOPHILIN D IN COMPLEX WITH N-CYCLOPENTYL-N-PYRIDIN-2- YLMETHYL-OXALAMIDE ... HUMAN CYCLOPHILIN D IN COMPLEX WITH N-CYCLOPENTYL-N-PYRIDIN-2- YLMETHYL-OXALAMIDE ...
Another human protein, cyclophilin A (CypA), can shield HIV capsid from premature binding to CPSF6, which can differ in CD4+ T ... and cyclophilin A (CypA). We observe that HIV-1 infection induces higher-order CPSF6 formation, and capsid-CPSF6 complexes ... Another human protein, cyclophilin A (CypA), can shield HIV capsid from premature binding to CPSF6, which can differ in CD4+ T ... Cytoplasmic CPSF6 Regulates HIV-1 Capsid Trafficking and Infection in a Cyclophilin A-Dependent Manner. ...
Beim Quarter Horse ist HERDA mit einer Mutation im Cyclophilin B Gen (PPIB) assoziiert. Cyclophilin B ist ein Enzym, welches ... Schweizer Warmblutfohlen mit Symptomen von hereditärer dermaler Asthenie (HERDA) ohne Mutation im Cyclophilin B-Gen (PPIB). ... Schweizer Warmblutfohlen mit Symptomen von hereditärer dermaler Asthenie (HERDA) ohne Mutation im Cyclophilin B-Gen (PPIB). S. ... In the Quarter Horse, HERDA is associated with a mutation in cyclophilin B (PPIB), an enzyme involved in triple helix formation ...
... we have determined cryo-EM structures of apo-CA hexamers and in complex with cyclophilin A (CypA) at near-atomic resolutions. ... Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A. ... Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A. ... we have determined cryo-EM structures of apo-CA hexamers and in complex with cyclophilin A (CypA) at near-atomic resolutions. ...
Enzymatic and structural characterization of non peptide ligand cyclophilin complexes ... Enzymatic and structural characterization of non peptide ligand cyclophilin complexes Coordinates. PDB Format Method. X-RAY ... Kontopidis, G. et al., Enzymatic and Structural Characterization of Non-Peptide Ligand-Cyclophilin Complexes. Acta Crystallogr ...
Crystal structure of cyclophilin D in complex with CsA analogue, JW47. ... Crystal structure of cyclophilin D in complex with CsA analogue, JW47. Coordinates. PDB Format Method. X-RAY DIFFRACTION 1.25 Å ...
Cyp: Cyclophilin; ER: Endoplasmic reticulum; FKBP: FK506-binding protein; HCV: Hepatitis C virus; HSC70: Heat shock cognate ...
Cyclophilin B (1). * DC-SIGN (2). * Factor VIII + VIII C2domain (1). * hCG Holo c2 (1). ...
RNase protection assay for ABCA1 and cyclophilin was performed on 10 μg total RNA obtained from the liver and spleen of ... and a 103-bp cyclophilin probe from Ambion Inc. (Austin, Texas, USA). The RNase protection assay was performed using a ...
Name: peptidylprolyl isomerase (cyclophilin)-like 1. Synonyms: Cypl1, 1110060O10Rik. Type: Gene. Species: Mus musculus (mouse) ...
  • Peptidylprolyl isomerases (PPIase) cyclophilin A (CypA, encoded by PPIA ) is a typical member of the Cyclophilin family and is involved in protein folding/translocation, signal transduction, inflammation, immune system regulation, apoptosis and virus replication. (chinagene.cn)
  • This gene encodes a member of the cyclophilin family. (thermofisher.com)
  • This study is designed to explore the effects of cyclophilin A (CypA) on macrophage polarization and describe the underlying mechanisms. (nih.gov)
  • Human immunodeficiency virus type 1 (HIV-1) capsid binds host proteins during infection, including cleavage and polyadenylation specificity factor 6 (CPSF6) and cyclophilin A (CypA). (ox.ac.uk)
  • Another human protein, cyclophilin A (CypA), can shield HIV capsid from premature binding to CPSF6, which can differ in CD4+ T cells and macrophages. (ox.ac.uk)
  • By devising cryo-EM methodologies for exceedingly flexible and pleomorphic assemblies, we have determined cryo-EM structures of apo-CA hexamers and in complex with cyclophilin A (CypA) at near-atomic resolutions. (ox.ac.uk)
  • Cyclophilins (CYPs) are a family of proteins named after their ability to bind to ciclosporin (cyclosporin A), an immunosuppressant which is usually used to suppress rejection after internal organ transplants. (wikipedia.org)
  • Launch Cyclophilins and FK506 binding protein (FKBPs) are mobile goals TKI-258 for the immunosuppressive medications cyclosporin A and FK506 respectively and screen a peptidyl- prolyl isomerase (PPIase) function that's thought to catalyze proteins folding (Galat and Metcalfe 1995). (techuniq.com)
  • New method finds compounds that bind and inhibit individual members of a family of key regulatory proteins, called cyclophilins, that have been difficult to target selectively. (broadinstitute.org)
  • Cyclophilin inhibitors, such as cyclosporin, are being developed to treat neurodegenerative diseases. (wikipedia.org)
  • Current inhibitors of peptidylprolyl isomerases show no selectivity between the tightly conserved cyclophilin paralogs and exhibit significant off-target effects, immunosuppression, and toxicity. (rcsb.org)
  • Ongar, UK, 10th February 2017 / Sciad Newswire / Selcia , with colleagues from Cypralis and Gilead Sciences Inc., have published in the Journal of Medicinal Chemistry a novel strategy of structural simplification of a natural product to generate synthetically tractable cyclophilin inhibitors for the treatment of HCV. (sciad.com)
  • Selcia's collaboration with Cypralis and Gilead delivered a set of synthetic macrocyclic cyclophilin inhibitors inspired by the core structure of the natural product sanglifehrin A. (sciad.com)
  • The paper describes how novel macrocyclic non-immunosuppressive cyclophilin inhibitors, with high potency in both biochemical and antiviral assays were generated by employing structure based drug design, modern synthetic methods and deep understanding of the property profile required of a successful drug. (sciad.com)
  • Mike Peel, CSO of Cypralis, said: 'The discovery of completely synthetic and very potent cyclophilin inhibitors that fully reproduce the biology of a semi-synthetic natural product lead is a major breakthrough in this field. (sciad.com)
  • The SARS-coronavirus-host interactome: identification of cyclophilins as target for pan-coronavirus inhibitors. (nih.gov)
  • Cyclophilin inhibitors restrict Middle East respiratory syndrome coronavirus via interferon-λ in vitro and in mice. (bvsalud.org)
  • Liqian Ren, Wei Liu, Wenbo Li, Wenjun Liu, Lei Sun. Peptidylprolyl cis/trans isomerase activity and molecular evolution of vertebrate Cyclophilin A[J]. Hereditas(Beijing), 2016, 38(8): 736-745. (chinagene.cn)
  • Cyclophilins catalyze the cis-trans isomerization of peptidylprolyl imide bonds in oligopeptides. (thermofisher.com)
  • Cyclophilin A is a cytosolic and highly abundant protein. (wikipedia.org)
  • The protein belongs to a family of isozymes, including cyclophilins B and C, and natural killer cell cyclophilin-related protein. (wikipedia.org)
  • Scholars@Duke publication: The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis. (duke.edu)
  • The cyclophilin-like domain (CLD) of Ran-binding protein-2 (RanBP2/Nup358) associates specifically with at least one subunit, S1, of the base subcomplex of the 19S RP, but the functional implications of this interaction on the UPS activity are elusive. (duke.edu)
  • Influences of cyclosporin A and non-immunosuppressive derivatives on cellular cyclophilins and viral nucleocapsid protein during human coronavirus 229E replication. (uni-muenchen.de)
  • This review also discusses the emerging roles of cyclophilins, which are peptidyl-prolyl isomerases with chaperone functions, in replication of selected (+)RNA viruses. (uky.edu)
  • In the Quarter Horse, HERDA is associated with a mutation in cyclophilin B (PPIB), an enzyme involved in triple helix formation of collagen. (gstsvs.ch)
  • Beim Quarter Horse ist HERDA mit einer Mutation im Cyclophilin B Gen (PPIB) assoziiert. (gstsvs.ch)
  • Positive Control #1 targets PPIB (aka Cyclophilin B). (horizondiscovery.com)
  • Cyclophilin D (PPIF, note that literature is confusing, the mitochondrial cyclophilin is encoded by the PPIF gene), which is located in the matrix of mitochondria, is only a modulatory, but may or may not be a structural component of the mitochondrial permeability transition pore. (wikipedia.org)
  • Other cyclophilins have similar structures to cyclophilin A. The cyclosporin-cyclophilin A complex inhibits a calcium/calmodulin-dependent phosphatase, calcineurin, the inhibition of which is thought to suppress organ rejection by halting the production of the pro-inflammatory molecules TNF alpha and interleukin 2. (wikipedia.org)
  • Cyclophilin D is thought to regulate the opening of the pore because cyclosporin A, which binds to CyP-D, inhibits the pore opening. (wikipedia.org)
  • Some patients have mutations in the TACI (transmembrane activator and calcium-modulator and cyclophilin ligand interactor) gene. (msdmanuals.com)
  • Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro. (usf.edu)
  • 6] Colgan J, Yuan HE, Franke EK, Luban J. Binding of the human immunodeficiency virus type 1 Gag polyprotein to cyclophilin A is mediated by the central region of capsid and requires Gag dimerization. (chinagene.cn)
  • Cytoplasmic CPSF6 Regulates HIV-1 Capsid Trafficking and Infection in a Cyclophilin A-Dependent Manner. (ox.ac.uk)
  • Intrinsic curvature of the HIV-1 CA hexamer underlies capsid topology and interaction with cyclophilin A. (ox.ac.uk)
  • and Blair, Laura J., "Human Cyclophilin 40 Unravels Neurotoxic Amyloids" (2017). (usf.edu)
  • However, mitochondria obtained from the cysts of Artemia franciscana, do not exhibit the mitochondrial permeability transition pore Overexpression of Cyclophilin A has been linked to poor response to inflammatory diseases, the progression or metastasis of cancer, and aging. (wikipedia.org)
  • Mitochondrial permeability transition pore component cyclophilin D distinguishes nigrostriatal dopaminergic death paradigms in the MPTP mouse model of Parkinson's disease. (musc.edu)
  • Calcineurin is a common target of cyclophilin-cyclosporine A and Fkbp-Fk506 complexes. (chinagene.cn)
  • 5A0E: Crystal structure of cyclophilin D in complex with CsA analogue, JW47. (rcsb.org)
  • Human Cyclophilin 40 Unravels Neurotoxic Amyloids" by Jeremy D. Baker, Lindsey B. Shelton et al. (usf.edu)
  • Cyclophilin inhibition may also be a therapy for liver diseases. (wikipedia.org)
  • Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury. (musc.edu)
  • Cyclophilin D as a drug target. (musc.edu)
  • This graph shows the total number of publications written about "Cyclophilins" by people in this website by year, and whether "Cyclophilins" was a major or minor topic of these publications. (musc.edu)
  • Below are the most recent publications written about "Cyclophilins" by people in Profiles. (musc.edu)
  • Fragment-based screening by SPR enabled the discovery of chemical diverse fragment hits with millimolar binding affinities to the peptidyl-prolyl isomerase Cyclophilin D (CypD). (nih.gov)
  • Cyclophilin D (CypD) is a mitochondrial matrix proteins implicated in cell death but a potential part in bioenergetics is not understood. (sciencepop.org)
  • Other cyclophilins have similar structures to cyclophilin A. The cyclosporin-cyclophilin A complex inhibits a calcium/calmodulin-dependent phosphatase, calcineurin, the inhibition of which is thought to suppress organ rejection by halting the production of the pro-inflammatory molecules TNF alpha and interleukin 2. (wikipedia.org)
  • Cyclophilin inhibition may also be a therapy for liver diseases. (wikipedia.org)
  • Inhibition of cyclophilin D has been shown to prevent cell death. (selcia.com)
  • Cyclophilin D inhibition rescues cardiac function in neonatal hypoxia. (rochester.edu)
  • Cyclophilin D is thought to regulate the opening of the pore because cyclosporin A, which binds to CyP-D, inhibits the pore opening. (wikipedia.org)
  • Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D". J. Biol. (wikipedia.org)
  • Cyclophilin D is an integral constituent of the MPTP, maintaining the pore in a state of high responsiveness to opening stimuli. (selcia.com)
  • Overexpression of Cyclophilin A has been linked to poor response to inflammatory diseases, the progression or metastasis of cancer, and aging. (wikidoc.org)
  • A strong correlation has been found for cyclophilin overexpression and malignant transformation (reviewed by Lee & Kim, 2010). (selcia.com)
  • In the extracellular space cyclophilins bind to CD147, a membrane receptor expressed on many cells and elicit the production of matrix metalloproteinases and white blood cell chemotaxis. (selcia.com)
  • The Cyclophilin A-CD147 complex promotes the proliferation and homing. (yasni.de)
  • Cyclophilin A is also known to be recruited by the Gag polyprotein during HIV-1 virus infection, and its incorporation into new virus particles is essential for HIV-1 infectivity. (wikipedia.org)
  • Is the cis-trans isomerization of cyclophilin involved in HIV-1 infectivity? (cas.cz)
  • Structural insights into the catalytic mechanism of cyclophilin A. Nat.Struct.Biol. (expasy.org)
  • Tigen (BCMA), transmembrane activator and calcium modulator and cyclophilin ligand interactor (TACI), and BAFF-R (BR3). (igf-1r.com)
  • TACi, transmembrane activator and calcium modulator and cyclophilin ligand interactor.have enhanced serum levels of BAFF through the onset and progression of SLE. (igf-1r.com)
  • Cytoplasmic CPSF6 Regulates HIV-1 Capsid Trafficking and Infection in a Cyclophilin A-Dependent Manner. (ox.ac.uk)
  • Cyclophilins are used by some viruses for infection and replication purposes and represent attractive targets for antiviral therapy. (selcia.com)
  • 2. Target cell cyclophilins facilitate human papillomavirus type 16 infection. (nih.gov)
  • 10. Furin Cleavage of L2 during Papillomavirus Infection: Minimal Dependence on Cyclophilins. (nih.gov)
  • Human Cyclophilin-D produced in E. Coli is a single, non-glycosylated, polypeptide chain (amino acids 1-370) containing 390 amino acids and having a molecular mass of 42.9kDa. (enquirebio.com)
  • Cysteine 202 of cyclophilin D is a site of multiple post-translational modifications and plays a role in cardioprotection. (nih.gov)
  • Both cyclophilin and FKBP have leukocyte chemotactic activity which is inhibited by cyclosporins and FK506. (selcia.com)
  • Bioinformatic and expression analysis of the Brassica napus L. cyclophilins. (mpg.de)