Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
about
Catalysis of serine oligopeptidases is controlled by a gating filter mechanismThe Dipeptidyl Peptidase Family, Prolyl Oligopeptidase, and Prolyl Carboxypeptidase in the Immune System and Inflammatory Disease, Including AtherosclerosisStructures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residueElectrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding siteElectrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate bindingDesign of (omega-N-(O-acyl)hydroxy amid) aminodicarboxylic acid pyrrolidides as potent inhibitors of proline-specific peptidases.Peptidyl ammonium methyl ketones as substrate analog inhibitors of proline-specific peptidases.Molecular dynamics study of prolyl oligopeptidase with inhibitor in binding cavity.The noncatalytic beta-propeller domain of prolyl oligopeptidase enhances the catalytic capability of the peptidase domain.Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.Formation of acetyl-Ser-Asp-Lys-Pro, a new regulator of the hematopoietic system, through enzymatic processing of thymosin beta 4.Prolyl oligopeptidase is inhibited in relapsing-remitting multiple sclerosis.Effect of S 17092, a novel prolyl endopeptidase inhibitor, on substance P and alpha-melanocyte-stimulating hormone breakdown in the rat brain.Substrate recognition properties of oligopeptidase B from Salmonella enterica serovar Typhimurium.Effect of prolyl endopeptidase inhibition on arginine-vasopressin and thyrotrophin-releasing hormone catabolism in the rat brain.A cocoa peptide protects Caenorhabditis elegans from oxidative stress and β-amyloid peptide toxicity.Attacking the multi-tiered proteolytic pathology of COPD: new insights from basic and translational studies.Issues about the physiological functions of prolyl oligopeptidase based on its discordant spatial association with substrates and inconsistencies among mRNA, protein levels, and enzymatic activityLow molecular weight inhibitors of Prolyl Oligopeptidase: a review of compounds patented from 2003 to 2010.Substrate- and pH-dependent contribution of oxyanion binding site to the catalysis of prolyl oligopeptidase, a paradigm of the serine oligopeptidase family.Prolyl oligopeptidase and its role in the organism: attention to the most promising and clinically relevant inhibitors.The prolyl oligopeptidase inhibitor SUAM-14746 attenuates the proliferation of human breast cancer cell lines in vitro.Mycobacterium tuberculosis Prolyl Oligopeptidase Induces In vitro Secretion of Proinflammatory Cytokines by Peritoneal Macrophages.A prolyl oligopeptidase inhibitor, KYP-2047, reduces α-synuclein protein levels and aggregates in cellular and animal models of Parkinson's disease.An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: evidence of hydrolysis of human bioactive peptides.Modulation of inositol 1,4,5-triphosphate concentration by prolyl endopeptidase inhibition.Structure of proline iminopeptidase from Xanthomonas campestris pv. citri: a prototype for the prolyl oligopeptidase family.Effects of ionic strength on the catalysis and stability of prolyl oligopeptidaseBenzyloxycarbonylprolylprolinal, a transition-state analogue for prolyl oligopeptidase, forms a tetrahedral adduct with catalytic serine, not a reactive cysteine.Properties of the prolyl oligopeptidase homologue from Pyrococcus furiosus.Novel proline endopeptidase inhibitors do not modify Abeta40/42 formation and degradation by human cells expressing wild-type and swedish mutated beta-amyloid precursor protein.Kinetic and mechanistic studies of prolyl oligopeptidase from the hyperthermophile Pyrococcus furiosus.Prolyl endopeptidase inhibitors from green tea.Synthesis and inhibitory activity of acyl-peptidyl-pyrrolidine derivatives toward post-proline cleaving enzyme; a study of subsite specificity.Prolyl endopeptidase inhibitory peptides in wine.Effects of beta-casomorphin-5 on passive avoidance response in mice.A prolyl endopeptidase-inhibiting antioxidant from Phyllanthus ussurensis.Murine T cells expressing high activity of prolyl endopeptidase are susceptible to activation-induced cell death.Flexibility of prolyl oligopeptidase: molecular dynamics and molecular framework analysis of the potential substrate pathways.Structure and localization of the mouse prolyl oligopeptidase gene.
P2860
Q24522484-C58AA1F7-35FA-4F90-A060-F3B0CA7D04A0Q26795473-1F1DEA16-1BBB-4729-8FA7-E3532A86436CQ27627477-C8521AB4-7155-47AF-B047-EF35869E7319Q27639555-FF34F03A-5D1E-4E79-BBB0-5343DA1C5176Q27642231-C8CAA457-067B-423D-91A9-6BD3C5106BEAQ30321432-F67F0187-8A24-492E-861A-AAC6A36D6683Q30321437-D558F4C0-E149-4AFD-8D79-14DDE6B705BFQ30383681-388CC2C8-71BD-47EE-BED8-C4B4C0EB44EDQ30588751-B23862F5-AE3F-4D6C-A6FE-D17288F66C71Q33215504-7ED45110-991D-4C31-A196-EA04E6B451EFQ33652254-115FE35B-50AF-4A90-8371-DE75EC5B51BBQ33828496-95EDB31E-1C52-4660-B149-1AD56512BA63Q34179575-C963C837-6D0B-46D9-8886-DCF90D00209AQ34312329-0294ED39-F64F-4A89-998D-71A89A58D2BBQ34415768-33CAB994-3296-401A-A135-9EEE9AA4E733Q34722805-B9441F31-BA6D-406A-8A57-C1FEFB76EC28Q37332258-52C83949-5D08-4D74-91DC-5A05B8DC5DEEQ37581327-6F0ADB56-CD79-42F7-AA25-B47B952E1A4CQ37871597-9985AA9E-819E-42DD-9870-89F095CA7BF1Q38314464-9437934E-F35B-4DB3-9833-C7B792F83F73Q38668992-201F669E-DF73-4690-A202-EDC5C29F9A3DQ38722145-230E8630-2122-485D-A826-48857FCDF8B1Q38949083-EF55CFAA-C24D-46F3-8505-4D92A02C4C4DQ39414467-06FAF431-27D9-4577-A003-656C4951B799Q40376087-B9D32285-453E-4FA3-9362-222685F73E7DQ40688307-00755354-FAF9-4AD6-8474-49302EF903A5Q41834863-FD34F1AC-33D3-464F-8B0B-8DE7C9901756Q41848250-607FCBCC-2F90-4E1C-BD95-3DC98B3FEFDAQ42018806-6BEFAAEA-B05C-4D23-B3F9-13B2F6798A9CQ43020368-4E330742-2B54-46DC-A042-515AF69CD6ABQ43264634-D0297EC9-360D-4B08-AA03-8C8C08E2C6D2Q43559775-1FFCF891-7CB4-4EEF-9F4F-6AE26F48ED52Q43727229-99FB9429-EDF3-4861-93D0-8F489CB008AEQ43930557-A3D5D075-74CB-4690-B39E-943705E1CAD3Q44428034-FC4B2CC4-FAB5-4E05-880A-9947175D2DC0Q44674563-618A26BB-B670-4576-804C-D4E249DC5A35Q44727966-12815A66-9C1C-43EB-8DC7-9A7FCDDBD25BQ45711471-970B5A53-A25F-45A1-8D08-A0072D825F4DQ46560922-AC99B0BE-21DF-49D6-9213-03CF29889E23Q47938434-9EE43AD1-9729-4BB3-89A9-BFFA4869ED64
P2860
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
description
1987 nî lūn-bûn
@nan
1987 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@ast
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@en
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@nl
type
label
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@ast
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@en
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@nl
prefLabel
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@ast
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@en
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@nl
P2093
P356
P1476
Specific inhibitors for prolyl endopeptidase and their anti-amnesic effect
@en
P2093
P356
10.1248/BPB1978.10.730
P407
P577
1987-12-01T00:00:00Z