Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding
about
Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidaseStructural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidaseMolecular dynamics study of prolyl oligopeptidase with inhibitor in binding cavity.A link between hinge-bending domain motions and the temperature dependence of catalysis in 3-isopropylmalate dehydrogenase.Low molecular weight inhibitors of Prolyl Oligopeptidase: a review of compounds patented from 2003 to 2010.Kinetic Landscape of a Peptide Bond-Forming Prolyl Oligopeptidase.Mechanism of Action of Prolyl Oligopeptidase (PREP) in Degenerative Brain Diseases: Has Peptidase Activity Only a Modulatory Role on the Interactions of PREP with Proteins?Selective Homogeneous Assay for Circulating Endopeptidase Fibroblast Activation Protein (FAP).Dynamics and ligand-induced conformational changes in human prolyl oligopeptidase analyzed by hydrogen/deuterium exchange mass spectrometryProperties of the prolyl oligopeptidase homologue from Pyrococcus furiosus.Primary structure, recombinant expression and homology modelling of human brain prolyl oligopeptidase, an important therapeutic target in the treatment of neuropsychiatric diseases.Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation.Exploration of the chlorpyrifos escape pathway from acylpeptide hydrolases using steered molecular dynamics simulations.
P2860
Q27643647-4747DAA8-3A2B-466E-BF53-7D7DB059D7EFQ27662174-43753969-0D71-426D-8FE7-5C545E39F52EQ30383681-EAA10946-CF57-4181-8DDB-D04FCA8113EBQ37265353-B6FA1417-B937-4D07-86C0-2AE96CD8D251Q37871597-637D07E6-2098-4CF9-BA2F-B84C10F94130Q41997695-D6837224-FBDD-4CD9-98DC-EF88D7D62342Q42028017-869832BC-04EA-4658-B045-CE42AFA0BB7DQ42172295-59D95A3C-8CFC-4197-8B4A-A3EB5283B2E4Q42242203-1C8F062D-276D-45E1-B32D-89BFE86F81BCQ43020368-370BF717-6522-4F8D-8EB8-CA6DD9764B6EQ46444548-1FDB1F95-708B-47BC-A2D2-86793C9A5F35Q51210998-F4BADEC1-57EE-4E28-B727-4AE66860DC18Q51212407-F1B0B773-4E5A-4F6E-ABCD-98ECCB7DCA59Q52810253-F456DEEE-D648-4EC9-937C-0B22C25292A3
P2860
Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Electrostatic environment at t ...... ntial during substrate binding
@ast
Electrostatic environment at t ...... ntial during substrate binding
@en
Electrostatic environment at t ...... ntial during substrate binding
@nl
type
label
Electrostatic environment at t ...... ntial during substrate binding
@ast
Electrostatic environment at t ...... ntial during substrate binding
@en
Electrostatic environment at t ...... ntial during substrate binding
@nl
prefLabel
Electrostatic environment at t ...... ntial during substrate binding
@ast
Electrostatic environment at t ...... ntial during substrate binding
@en
Electrostatic environment at t ...... ntial during substrate binding
@nl
P2093
P2860
P356
P1476
Electrostatic environment at t ...... ntial during substrate binding
@en
P2093
Laszló Polgár
Luiz Juliano
Veronika Renner
Vilmos Fülop
Zoltán Szeltner
P2860
P304
P356
10.1074/JBC.M309555200
P407
P577
2003-12-05T00:00:00Z