about
Structure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASEStructures of Human DPP7 Reveal the Molecular Basis of Specific Inhibition and the Architectural Diversity of Proline-Specific PeptidasesA Self-compartmentalizing Hexamer Serine Protease from Pyrococcus Horikoshii: SUBSTRATE SELECTION ACHIEVED THROUGH MULTIMERIZATIONEntropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase IIICrystal structures of Trypanosoma brucei oligopeptidase B broaden the paradigm of catalytic regulation in prolyl oligopeptidase family enzymesStructural insight into how Pseudomonas aeruginosa peptidoglycanhydrolase Tse1 and its immunity protein Tsi1 functionCatalytically distinct states captured in a crystal lattice: the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionalityStructure and Mechanism of the Sphingopyxin I Lasso Peptide IsopeptidaseReciprocal influence of protein domains in the cold-adapted acyl aminoacyl peptidase from Sporosarcina psychrophila.Peptide macrocyclization catalyzed by a prolyl oligopeptidase involved in α-amanitin biosynthesis.Distribution, classification, domain architectures and evolution of prolyl oligopeptidases in prokaryotic lineages.Enzyme Tunnels and Gates As Relevant Targets in Drug Design.Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants.Parasite prolyl oligopeptidases and the challenge of designing chemotherapeuticals for Chagas disease, leishmaniasis and African trypanosomiasisLow molecular weight inhibitors of Prolyl Oligopeptidase: a review of compounds patented from 2003 to 2010.Targeted modification of wheat grain protein to reduce the content of celiac causing epitopes.Prolyl-specific peptidases for applications in food protein hydrolysis.Unveiling prolyl oligopeptidase ligand migration by comprehensive computational techniques.Automated identification of crystallographic ligands using sparse-density representations.Dynamics and ligand-induced conformational changes in human prolyl oligopeptidase analyzed by hydrogen/deuterium exchange mass spectrometrySecretory Expression, Purification, Characterization, and Application of an Aspergillus oryzae Prolyl Aminopeptidase in Bacillus subtilis.Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.Active-Site-Directed Inhibitors of Prolyl Oligopeptidase Abolish Its Conformational Dynamics.
P2860
Q27665946-A00486FE-2340-4CCF-8490-6C0B39852AFAQ27672453-B3316681-6EB0-4AB7-A04A-572EB78A7B36Q27677875-4C021729-3F3A-48F3-A174-04AB5EA9E511Q27678433-C1579515-B635-4F7F-98CA-E6987A9F4AA6Q27680672-D7D0FE51-DEEC-4EFC-85A8-93464B5CCE7BQ27682067-D5AAA485-A852-427D-A061-09230B3440D5Q27698250-85CE88B4-9E18-474C-A3A4-611C3B09D9EDQ27728024-80186A0E-6322-4A47-980A-AE3CFBE418E3Q34606653-05667118-85AE-49C8-B467-948308687FA6Q34747104-A39D4A55-3045-4403-B149-286E9D7C0175Q35434067-D301C03E-0E55-4B6D-BEDE-F18BA93A37B4Q36221405-B1473E99-4918-4073-81EF-65B93527167EQ36393589-4C9EFB09-C992-4316-8FA6-8C22F7F01C4AQ37186711-1D7D6077-8797-4420-8A57-1839D709056CQ37871597-4F8207A2-A8F3-4073-A049-CCF5DA721A9CQ38021639-82A6AF6D-930A-4151-AE93-4D640E843975Q38560146-F3BA26BC-14E2-418E-A68D-3A56B647A49BQ41996825-78AA3182-7AB2-477B-BD30-88544CDB3929Q42111041-628D2701-F050-47BB-8EF2-5C16B4F4DBA2Q42242203-5E804863-0E48-438A-94F6-29DC2D58E05FQ50270569-4BEAD5AC-F160-4382-ADC5-3C200DF5266EQ51210998-071CCE35-3004-48A4-B37C-99E9FFC68C79Q53170357-BFA158A3-87E1-40F8-9EED-7AC107519218
P2860
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Induced-fit Mechanism for Prolyl Endopeptidase
@nl
Induced-fit mechanism for prolyl endopeptidase.
@ast
Induced-fit mechanism for prolyl endopeptidase.
@en
type
label
Induced-fit Mechanism for Prolyl Endopeptidase
@nl
Induced-fit mechanism for prolyl endopeptidase.
@ast
Induced-fit mechanism for prolyl endopeptidase.
@en
prefLabel
Induced-fit Mechanism for Prolyl Endopeptidase
@nl
Induced-fit mechanism for prolyl endopeptidase.
@ast
Induced-fit mechanism for prolyl endopeptidase.
@en
P2093
P2860
P356
P1476
Induced-fit mechanism for prolyl endopeptidase.
@en
P2093
Changqing Chen
David R Davies
Thang K Chiu
P2860
P304
21487-21495
P356
10.1074/JBC.M109.092692
P407
P577
2010-05-05T00:00:00Z