Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme (Q24682970)

2

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R Huber

3

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G P Bourenkov

4

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H Bartunik

5

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G A Ellestad

6

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P Reddy

7

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M F Wolfson

8

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C T Rauch

9

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B J Castner

10

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R Davis

11

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H R Clarke

12

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M Petersen

13

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J N Fitzner

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D P Cerretti

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C J March

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R J Paxton

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R A Black

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W Bode

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

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language of work or name

English

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publication date

31 March 1998

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published in

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volume

95

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issue

7

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page(s)

3408-12

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cites work

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The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

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Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

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Crystal structure of H2-proteinase from the venom of Trimeresurus flavoviridis

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First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases

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Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)

7 April 2017

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X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design

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Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases

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Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'

7 April 2017

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Kuzbanian Controls Proteolytic Processing of Notch and Mediates Lateral Inhibition during Drosophila and Vertebrate Neurogenesis

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Purification of ADAM 10 from bovine spleen as a TNFalpha convertase

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Relaxed specificity of matrix metalloproteinases (MMPS) and TIMP insensitivity of tumor necrosis factor-alpha (TNF-alpha) production suggest the major TNF-alpha converting enzyme is not an MMP.

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Human pro-tumor necrosis factor is a homotrimer

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A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T lymphocytes

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ADAMs in fertilization and development

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Membrane protein secretases

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Protection against a lethal dose of endotoxin by an inhibitor of tumour necrosis factor processing

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Structure of tumour necrosis factor

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A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contact

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Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin

30 May 2018

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12 December 2020

Treatment of Rheumatoid Arthritis with a Recombinant Human Tumor Necrosis Factor Receptor (p75)–Fc Fusion Protein

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12 December 2020

Anti-arthritic activity of hydroxamic acid-based pseudopeptide inhibitors of matrix metalloproteinases and TNFα processing

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12 December 2020

Length of the linking domain of human pro-tumor necrosis factor determines the cleavage processing

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12 December 2020

Identifiers

DOI

10.1073/PNAS.95.7.3408

1 reference

ADS bibcode

1998PNAS...95.3408M

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1 reference

1 reference

PubMed publication ID

9520379

1 reference