MDC-L, a novel metalloprotease disintegrin cysteine-rich protein family member expressed by human lymphocytes (Q28145371)

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L C Bridges

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Z Laszik

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R D Bowditch

Journal of Biological Chemistry

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language of work or name

English

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publication date

8 October 1999

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published in

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volume

274

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issue

41

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page(s)

29251-9

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cites work

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A metalloprotease-disintegrin participating in myoblast fusion

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Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion

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Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor.

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Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3

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KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis

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Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis

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Processing of the notch ligand delta by the metalloprotease Kuzbanian

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Membrane protein secretases

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Downregulation of Fas ligand by shedding

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Human native soluble CD40L is a biologically active trimer, processed inside microsomes

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A family of cellular proteins related to snake venom disintegrins

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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ADAM 20 and 21; two novel human testis-specific membrane metalloproteases with similarity to fertilin-alpha

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The sequence 5'-AAUAAA-3'forms parts of the recognition site for polyadenylation of late SV40 mRNAs

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Human ADAM 12 (meltrin alpha) is an active metalloprotease.

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A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo

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An essential role for ectodomain shedding in mammalian development

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Identifiers

DOI

10.1074/JBC.274.41.29251

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

10506182

1 reference

Consolidated OpenCitations Corpus – April 2017