Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin - Test2 - elhamkhani - TriplyDB

Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

http://www.wikidata.org/entity/Q28273170

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Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13 Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed alpha-helix Solution structure of the Legionella pneumophila Mip-rapamycin complex NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35 Structure and Activity of the Peptidyl-Prolyl Isomerase Domain from the Histone Chaperone Fpr4 toward Histone H3 Proline Isomerization Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins A nuclear FK506-binding protein is a histone chaperone regulating rDNA silencing.Solution structure of FK506 bound to FKBP-12 Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast N-terminal extension changes the folding mechanism of the FK506-binding protein Tacrolimus (FK506) prevents early stages of ethanol induced hepatic fibrosis by targeting LARP6 dependent mechanism of collagen synthesis A comparison of experimental and computational methods for mapping the interactions present in the transition state for folding of FKBP12 Crystal structure of recombinant human T-cell cyclophilin A at 2.5 A resolution Cyclosporin A-cyclophilin complex formation. A model based on X-ray and NMR data.Selecting folded proteins from a library of secondary structural elements.Classification of rice (Oryza sativa L. Japonica nipponbare) immunophilins (FKBPs, CYPs) and expression patterns under water stress.Solvent Effects on the Energetics of Prolyl Peptide Bond Isomerization Protein denaturation and protein:drugs interactions from intrinsic protein fluorescence measurements at the nanolitre scale Immunophilins: switched on protein binding domains?Peptidyl-prolyl isomerases: a new twist to transcription.Structure-affinity properties of a high-affinity ligand of FKBP12 studied by molecular simulations of a binding intermediate Rapamycin inhibits vascular smooth muscle cell migration.The chemistry of signal transduction.Enthalpy of hydrogen bond formation in a protein-ligand binding reaction Sirolimus pharmacokinetics in pediatric renal transplant recipients receiving calcineurin inhibitor co-therapy.Inhibitor-induced conformational stabilization and structural alteration of a mip-like peptidyl prolyl cis-trans isomerase and its C-terminal domain Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD Water at biomolecular binding interfaces.Neisseria meningitidis encodes an FK506-inhibitable rotamase.Structures of Pathogenic Fungal FKBP12s Reveal Possible Self-Catalysis Function.In vivo incorporation of unnatural amino acids to probe structure, dynamics, and ligand binding in a large protein by nuclear magnetic resonance spectroscopy.Heat capacity changes and hydrophobic interactions in the binding of FK506 and rapamycin to the FK506 binding protein An immunophilin that binds M(r) 90,000 heat shock protein: main structural features of a mammalian p59 protein Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.Peptidyl-prolyl isomerases: functionality and potential therapeutic targets in cardiovascular disease.Catalytic and ligand binding properties of the FK506 binding protein FKBP12: effects of the single amino acid substitution of Tyr82 to Leu The wheat peptidyl prolyl cis-trans-isomerase FKBP77 is heat induced and developmentally regulated.Ensemblator v3: Robust atom-level comparative analyses and classification of protein structure ensembles.Bcl-2 and FKBP12 bind to IP3 and ryanodine receptors at overlapping sites: the complexity of protein-protein interactions for channel regulation.

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P2860

Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

http://www.wikidata.org/entity/Q28273170

description

1991 nî lūn-bûn

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1991 թուականի Մայիսին հրատարակուած գիտական յօդուած

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1991 թվականի մայիսին հրատարակված գիտական հոդված

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1991年の論文

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1991年学术文章

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1991年學術文章

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name

Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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label

Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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prefLabel

Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin

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M K Rosen

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S L Schreiber

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S W Michnick

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T J Wandless

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P2860

A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase

Structure of the human class I histocompatibility antigen, HLA-A2

Molecular cloning and overexpression of the human FK506-binding protein FKBP

Cloning, expression, and purification of human cyclophilin in Escherichia coli and assessment of the catalytic role of cysteines by site-directed mutagenesis

Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin

Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution

Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry

A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin

Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex

beta-Sheet topology and the relatedness of proteins

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10.1126/SCIENCE.1709301

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