Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. (Q53581862)

15 May 2018

title

Mouse and human granzyme B have distinct tetrapeptide specificities and abilities to recruit the bid pathway. (English)

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15 May 2018

author name string

Livia Casciola-Rosen

1

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15 May 2018

Margarita Garcia-Calvo

2

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15 May 2018

Herbert G Bull

3

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15 May 2018

Joseph W Becker

4

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15 May 2018

Tonie Hines

5

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15 May 2018

Nancy A Thornberry

6

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15 May 2018

Antony Rosen

7

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15 May 2018

language of work or name

English

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publication date

19 December 2006

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15 May 2018

Journal of Biological Chemistry

published in

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volume

282

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15 May 2018

issue

7

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15 May 2018

page(s)

4545-4552

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15 May 2018

Granzyme B: pro-apoptotic, antiviral and antitumor functions

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Lymphocyte-mediated cytotoxicity.

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Granzyme B-mediated cytochrome c release is regulated by the Bcl-2 family members bid and Bax.

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Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation.

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Granzyme B induces BID-mediated cytochrome c release and mitochondrial permeability transition

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Granzyme B-mediated apoptosis proceeds predominantly through a Bcl-2-inhibitable mitochondrial pathway

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Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B.

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Proteolytic activation of the cell death protease Yama/CPP32 by granzyme B.

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Granzyme B directly and efficiently cleaves several downstream caspase substrates: implications for CTL-induced apoptosis

21 January 2018

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Cleavage by granzyme B is strongly predictive of autoantigen status: implications for initiation of autoimmunity

21 January 2018

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DFF45/ICAD can be directly processed by granzyme B during the induction of apoptosis

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Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation

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The cytotoxic lymphocyte protease, granzyme B, targets the cytoskeleton and perturbs microtubule polymerization dynamics

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A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis

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Cytotoxic lymphocytes require granzyme B for the rapid induction of DNA fragmentation and apoptosis in allogeneic target cells.

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Molecular ordering of the caspase activation cascade initiated by the cytotoxic T lymphocyte/natural killer (CTL/NK) protease granzyme B.

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Serpins prevent granzyme-induced death in a species-specific manner

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The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1

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Cell binding, internalization and cytotoxic activity of human granzyme B expressed in the yeast Pichia pastoris

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Potentiation of a tumor cell susceptibility to autologous CTL killing by restoration of wild-type p53 function.

21 January 2018

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Regulation of survivin function by Hsp90

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Maintenance of caspase-3 proenzyme dormancy by an intrinsic "safety catch" regulatory tripeptide

21 January 2018

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The structure of the pro-apoptotic protease granzyme B reveals the molecular determinants of its specificity

21 January 2018

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Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue

21 January 2018

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Characterization of structural determinants of granzyme B reveals potent mediators of extended substrate specificity

21 January 2018

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A proteomic approach for the discovery of protease substrates

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21 January 2018

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Granzyme B can cause mitochondrial depolarization and cell death in the absence of BID, BAX, and BAK.

21 January 2018

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Filamin (280-kDa Actin-binding Protein) Is a Caspase Substrate and Is Also Cleaved Directly by the Cytotoxic T Lymphocyte Protease Granzyme B during Apoptosis

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M606564200

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15 May 2018

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15 May 2018