Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase. (Q52229363)

27 April 2018

title

Role of the COOH-terminal domains of meprin A in folding, secretion, and activity of the metalloendopeptidase. (English)

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27 April 2018

author name string

Tsukuba T

series ordinal

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Bond JS

series ordinal

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language of work or name

English

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publication date

1 December 1998

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Journal of Biological Chemistry

published in

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volume

273

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issue

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page(s)

35260-35267

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The astacin family of metalloendopeptidases

cites work

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Identification of the cysteine residues implicated in the formation of alpha 2 and alpha/beta dimers of rat meprin

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COOH-terminal proteolytic processing of secreted and membrane forms of the alpha subunit of the metalloprotease meprin A. Requirement of the I domain for processing in the endoplasmic reticulum

21 January 2018

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Activation mechanism of meprins, members of the astacin metalloendopeptidase family

21 January 2018

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Maturation of secreted meprin alpha during biosynthesis: role of the furin site and identification of the COOH-terminal amino acids of the mouse kidney metalloprotease subunit.

21 January 2018

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Homophilic interactions mediated by receptor tyrosine phosphatases mu and kappa. A critical role for the novel extracellular MAM domain

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TRAF proteins and meprins share a conserved domain

21 January 2018

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Involvement of CRAF1, a relative of TRAF, in CD40 signaling

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The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction

21 January 2018

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Multiple modes of activation of latent human fibroblast collagenase: evidence for the role of a Cys73 active-site zinc complex in latency and a "cysteine switch" mechanism for activation

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Cytosolic Degradation of T-cell Receptor α Chains by the Proteasome

21 January 2018

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C‐Cytosolic and Transmembrane Domains of the N‐benzoyl‐L‐tyrosyl‐p‐aminobenzoic Acid Hydrolase α Subunit (Human Meprin α)are Essential for its Retention in the Endoplasmic Reticulum and C‐Terminal Processing

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Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.52.35260

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27 April 2018

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27 April 2018