Characterization of mouse cathepsin R, a new member of a family of placentally expressed cysteine proteases (Q28585681)

31 January 2017

title

Characterization of mouse cathepsin R, a new member of a family of placentally expressed cysteine proteases (English)

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31 January 2017

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GOA release 2020-03-11

K. Sol-Church

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31 January 2017

J. Frenck

series ordinal

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31 January 2017

G. Bertenshaw

series ordinal

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31 January 2017

R. W. Mason

series ordinal

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31 January 2017

language of work or name

English

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publication date

24 July 2000

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Biochimica et Biophysica Acta

31 January 2017

published in

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31 January 2017

volume

1492

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31 January 2017

issue

2-3

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31 January 2017

page(s)

488–492

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Inhibition of bone resorption by selective inactivators of cysteine proteinases

31 January 2017

cites work

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Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus

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In vitro embryotoxicity of the cysteine proteinase inhibitors benzyloxycarbonyl-phenylalanine-alanine-diazomethane (Z-Phe-Ala-CHN2) and benzyloxycarbonyl-phenylalanine-phenylalanine-diazomethane (Z-Phe-Phe-CHN2).

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Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation

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Cathepsin P, a novel protease in mouse placenta

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Cathepsin Q, a novel lysosomal cysteine protease highly expressed in placenta

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Mouse cathepsin M, a placenta-specific lysosomal cysteine protease related to cathepsins L and P

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Comparison of cathepsin L synthesized by normal and transformed cells at the gene, message, protein, and oligosaccharide levels

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Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment

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Cathepsin B, Cathepsin H, and cathepsin L

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Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain

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Identifiers

DOI

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