Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

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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?

P2860

Q42028017-D2F05678-528C-4012-98EE-4748BBE70B94

P2860

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

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http://www.wikidata.org/entity/Q51210998

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

@en

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

@nl

type

Item

label

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

@en

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

@nl

prefLabel

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

@en

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

@nl

P1476

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

@en

P2093

A M Lambeir

http://www.w3.org/2001/XMLSchema#string

E Schoenmakers

http://www.w3.org/2001/XMLSchema#string

I Brandt

http://www.w3.org/2001/XMLSchema#string

R Van Elzen

http://www.w3.org/2001/XMLSchema#string

P2860

Catalysis of serine oligopeptidases is controlled by a gating filter mechanism

Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue

Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog

Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding

Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation

Induced-fit mechanism for prolyl endopeptidase.

Molecular dynamics, crystallography and mutagenesis studies on the substrate gating mechanism of prolyl oligopeptidase

The loops facing the active site of prolyl oligopeptidase are crucial components in substrate gating and specificity

P2-substituted N-acylprolylpyrrolidine inhibitors of prolyl oligopeptidase: biochemical evaluation, binding mode determination, and assessment in a cellular model of synucleinopathy

Prolyl endopeptidase catalysis. A physical rather than a chemical step is rate-limiting.

P304

217-224

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P31

scholarly article

P356

10.1093/PROTEIN/GZW079

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Pieter Van der Veken

P577

2017-01-05T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

28062644

http://www.w3.org/2001/XMLSchema#string

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

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P2860

P2860

Ligand-induced conformational changes in prolyl oligopeptidase: a kinetic approach.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698