Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin. - Wikidata - wikimedia - TriplyDB

Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin.

Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin.

http://www.wikidata.org/entity/Q36364583

about

Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A A quarter century of granzymes Recombinant human granzyme A binds to two putative HLA-associated proteins and cleaves one of them Granzyme M mediates a novel form of perforin-dependent cell death The Cytotoxicity Mechanism of 6-Shogaol-Treated HeLa Human Cervical Cancer Cells Revealed by Label-Free Shotgun Proteomics and Bioinformatics Analysis Induction of rapid histone degradation by the cytotoxic T lymphocyte protease Granzyme A.Granzyme A and B-deficient killer lymphocytes are defective in eliciting DNA fragmentation but retain potent in vivo anti-tumor capacity.Protective role of intracellular glutathione against nitric oxide-induced necrosis in rat gastric mucosal cells.Ubiquitin-proteasome inhibitor enhances tumour necrosis factor-alpha-induced apoptosis in rat gastric epithelial cells.Granzyme A activates another way to die Perforin-mediated target-cell death and immune homeostasis.Perforin deficiency and susceptibility to cancer.Perforin: structure, function, and role in human immunopathology.Japanese encephalitis virus infection induces changes of mRNA profile of mouse spleen and brain.Regulation of gene expression and inhibition of experimental prostate cancer bone metastasis by dietary genistein Mitochondria-dependent and -independent regulation of Granzyme B-induced apoptosis.Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins.Perforin and lymphohistiocytic proliferative disorders.Apoptotic pathways are selectively activated by granzyme A and/or granzyme B in CTL-mediated target cell lysis.The target cell nucleus is not required for cell-mediated granzyme- or Fas-based cytotoxicity Granzyme B (GraB) autonomously crosses the cell membrane and perforin initiates apoptosis and GraB nuclear localization.In vitro- and ex vivo-derived cytolytic leukocytes from granzyme A x B double knockout mice are defective in granule-mediated apoptosis but not lysis of target cells.The functional basis for hemophagocytic lymphohistiocytosis in a patient with co-inherited missense mutations in the perforin (PFN1) gene.Mechanisms of granule-dependent killing.The cytolytic enzymes granyzme A, granzyme B, and perforin: expression patterns, cell distribution, and their relationship to cell maturity and bright CD57 expression.Granzyme C supports efficient CTL-mediated killing late in primary alloimmune responses.Perforin/granzyme-dependent and independent mechanisms are both important for the development of graft-versus-host disease after murine bone marrow transplantation The possible role of granzyme B in the pathogenesis of chronic obstructive pulmonary disease.Granzyme A-deficient mice retain potent cell-mediated cytotoxicity.Expression of multiple granzymes by cytotoxic T lymphocyte implies that they activate diverse apoptotic pathways in target cells.Substituted arylsulphonamides as inhibitors of perforin-mediated lysis The molecular mechanism of apoptosis induced by xenogeneic cytotoxicity.Molecular mechanism of target lysis by cytotoxic T cells.Granzyme A expression reveals distinct cytolytic CTL subsets following influenza A virus infection.Role of the perforin/granzyme cell death pathway in D-Gal/LPS-induced inflammatory liver injury.Duodenal cytotoxic lymphocytes in cow's milk protein sensitive enteropathy and coeliac disease.Residual cytotoxicity and granzyme K expression in granzyme A-deficient cytotoxic lymphocytes.

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P2860

Synergistic roles of granzymes A and B in mediating target cell death by rat basophilic leukemia mast cell tumors also expressing cytolysin/perforin.

http://www.wikidata.org/entity/Q36364583

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1995 nî lūn-bûn

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1995年の論文

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Synergistic roles of granzymes ...... expressing cytolysin/perforin.

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Synergistic roles of granzymes ...... expressing cytolysin/perforin.

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Synergistic roles of granzymes ...... expressing cytolysin/perforin.

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Synergistic roles of granzymes ...... expressing cytolysin/perforin.

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Synergistic roles of granzymes ...... expressing cytolysin/perforin.

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Synergistic roles of granzymes ...... expressing cytolysin/perforin.

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Nakajima H

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P2860

Cloning and chromosomal assignment of a human cDNA encoding a T cell- and natural killer cell-specific trypsin-like serine protease

Purification of three cytotoxic lymphocyte granule serine proteases that induce apoptosis through distinct substrate and target cell interactions

Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction

The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme

Granzyme A binding to target cell proteins. Granzyme A binds to and cleaves nucleolin in vitro

Cytotoxicity mediated by T cells and natural killer cells is greatly impaired in perforin-deficient mice

Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3

Molecular cloning of an inducible serine esterase gene from human cytotoxic lymphocytes

Isolation and complete structure of the lymphocyte serine protease granzyme G, a novel member of the granzyme multigene family in murine cytolytic T lymphocytes. Evolutionary origin of lymphocyte proteases.

Inhibition of cytotoxic T lymphocyte-induced target cell DNA fragmentation, but not lysis, by inhibitors of DNA topoisomerases I and II.

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