A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases.
about
The prolyl isomerase domain of PpiD fromEscherichia colishows a parvulin fold but is devoid of catalytic activityStructural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerasesCyclosporin A treatment of Leishmania donovani reveals stage-specific functions of cyclophilins in parasite proliferation and viabilityProlyl isomerization as a molecular memory in the allosteric regulation of the signal adapter protein c-CrkII.Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner.Chaperone domains convert prolyl isomerases into generic catalysts of protein folding.Influence of lithium cations on prolyl peptide bonds.Dimeric Structure of the Bacterial Extracellular Foldase PrsA.Prolyl isomerases in gene transcriptionKinetics of α-globin binding to α-hemoglobin stabilizing protein (AHSP) indicate preferential stabilization of hemichrome folding intermediate.Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyDDetermination of the Full Catalytic Cycle among Multiple Cyclophilin Family Members and Limitations on the Application of CPMG-RD in Reversible Catalytic Systems.Psychrophilic enzymes: from folding to function and biotechnology.Force-dependent isomerization kinetics of a highly conserved proline switch modulates the mechanosensing region of filamin.The protein folding challenge in psychrophiles: facts and current issues.A Novel In Vitro CypD-Mediated p53 Aggregation Assay Suggests a Model for Mitochondrial Permeability Transition by Chaperone Systems.The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module.Hydrogen bonds are a primary driving force for de novo protein folding.Functional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures.
P2860
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P2860
A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases.
description
2009 nî lūn-bûn
@nan
2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
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2009年学术文章
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2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
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2009年學術文章
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name
A library of fluorescent pepti ...... ficities of prolyl isomerases.
@ast
A library of fluorescent pepti ...... ficities of prolyl isomerases.
@en
type
label
A library of fluorescent pepti ...... ficities of prolyl isomerases.
@ast
A library of fluorescent pepti ...... ficities of prolyl isomerases.
@en
prefLabel
A library of fluorescent pepti ...... ficities of prolyl isomerases.
@ast
A library of fluorescent pepti ...... ficities of prolyl isomerases.
@en
P2093
P356
P1433
P1476
A library of fluorescent pepti ...... ficities of prolyl isomerases.
@en
P2093
Christian Lücke
Gabriel Zoldák
Gunter Fischer
Jozef Hritz
Tobias Aumüller
P304
10423-10436
P356
10.1021/BI9014242
P407
P577
2009-11-01T00:00:00Z