The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism (Q27640960)

10

object named as

Hans Brandstetter

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Wolfram Bode

8

object named as

Wolfram Bode

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Robert Huber

7

object named as

Robert Huber

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author name string

Michael Engel

1

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Torsten Hoffmann

2

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Leona Wagner

3

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Michael Wermann

4

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Ulrich Heiser

5

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Reiner Kiefersauer

Proceedings of the National Academy of Sciences of the United States of America

6

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language of work or name

English

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publication date

29 April 2003

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published in

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volume

100

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issue

9

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page(s)

5063-8

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cites work

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Substrates containing phosphorylated residues adjacent to proline decrease the cleavage by proline-specific peptidases.

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The locked rotation function

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Prolyl Oligopeptidase

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Substrate recognition mechanism of prolyl aminopeptidase from Serratia marcescens.

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A prediction of DPP IV/CD26 domain structure from a physico-chemical investigation of dipeptidyl peptidase IV (CD26) from human seminal plasma

21 January 2018

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Promotion of tumor growth by murine fibroblast activation protein, a serine protease, in an animal model

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Prolonged survival and decreased invasive activity attributable to dipeptidyl peptidase IV overexpression in ovarian carcinoma.

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Truncated dipeptidyl peptidase IV is a potent anti-adhesion and anti-metastasis peptide for rat breast cancer cells

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12 December 2020

Two highly conserved glutamic acid residues in the predicted β propeller domain of dipeptidyl peptidase IV are required for its enzyme activity

1 reference

12 December 2020

Binding to human dipeptidyl peptidase IV by adenosine deaminase and antibodies that inhibit ligand binding involves overlapping, discontinuous sites on a predicted β propeller domain

1 reference

12 December 2020

Structural basis for the processive protein degradation by tricorn protease

1 reference

12 December 2020

Reactions between dipeptidyl peptidase IV and diacyl hydroxylamines: mechanistic investigations

1 reference

12 December 2020

Distribution of adenosine deaminase-complexing protein in murine tissues

1 reference

12 December 2020

Dipeptidylpeptidase IV--inactivation with N-peptidyl-O-aroyl hydroxylamines

1 reference

12 December 2020

The conformation around the peptide bond between the P1- and P2-positions is important for catalytic activity of some proline-specific proteases

1 reference

12 December 2020

Use of immobilized adenosine deaminase (EC 3.5.4.4) for the rapid purification of native human CD26/dipeptidyl peptidase IV (EC 3.4.14.5)

1 reference

12 December 2020

CD26/dipeptidyl peptidase IV does not work as an adenosine deaminase-binding protein in rat cells

1 reference

12 December 2020

Identifiers

DOI

10.1073/PNAS.0230620100

1 reference

ADS bibcode

2003PNAS..100.5063E

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1 reference

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PubMed publication ID

12690074

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