Role of a propeller loop in the quaternary structure and enzymatic activity of prolyl dipeptidases DPP-IV and DPP9 (Q24293344)

GOA release 2020-03-11

Dipeptidyl peptidase 4

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identical protein binding

GOA release 2020-03-11

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GOA release 2020-03-11

author name string

Hung-Kuan Tang

1

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Ku-Chuan Chen

2

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Gan-Guang Liou

3

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Shu-Chun Cheng

4

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Chia-Hui Chien

5

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Hsiang-Yun Tang

6

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Li-Hao Huang

7

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Hui-Ping Chang

8

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Chi-Yuan Chou

9

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Xin Chen

Prolyl peptidases: a serine protease subfamily with high potential for drug discovery.

10

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language of work or name

English

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publication date

4 November 2011

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published in

FEBS Letters

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volume

585

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page(s)

3409-14

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issue

21

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cites work

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Pharmacokinetic and pharmacodynamic properties of multiple oral doses of sitagliptin, a dipeptidyl peptidase-IV inhibitor: a double-blind, randomized, placebo-controlled study in healthy male volunteers

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Mice lacking dipeptidyl peptidase IV are protected against obesity and insulin resistance

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Enhanced insulin secretion and improved glucose tolerance in mice lacking CD26.

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Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig.

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

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One site mutation disrupts dimer formation in human DPP-IV proteins

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Identification of hydrophobic residues critical for DPP-IV dimerization.

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Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV

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Biochemical properties and expression profile of human prolyl dipeptidase DPP9.

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The cytoplasmic peptidase DPP9 is rate-limiting for degradation of proline-containing peptides.

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Investigation of the dimer interface and substrate specificity of prolyl dipeptidase DPP8.

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Targeting fibroblast activation protein inhibits tumor stromagenesis and growth in mice

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The prolyl oligopeptidase family

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

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The dimeric transmembrane domain of prolyl dipeptidase DPP-IV contributes to its quaternary structure and enzymatic activities.

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Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

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Yeast actin with a mutation in the "hydrophobic plug" between subdomains 3 and 4 (L266D) displays a cold-sensitive polymerization defect

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Measuring and increasing protein stability

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Crystal structure of CD26/dipeptidyl-peptidase IV in complex with adenosine deaminase reveals a highly amphiphilic interface

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Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha

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Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family

21 January 2018

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Structure, function and biological relevance of prolyl oligopeptidase

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Structural and mechanistic analysis of two prolyl endopeptidases: role of interdomain dynamics in catalysis and specificity.

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Homology models of dipeptidyl peptidases 8 and 9 with a focus on loop predictions near the active site

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inferred from DOI database lookup

7 January 2021

based on heuristic

Prolyl Oligopeptidase

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2011.10.009