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The Serpins Are an Expanding Superfamily of Structurally Similar but Functionally Diverse Proteins
Published, JBC Papers in Press, July 2, 2001, DOI 10.1074/jbc.R100016200 Gary A. Silverman, Phillip I. Bird, Robin W. Carrell, Frank C. Church, Paul B. Coughlin, Peter G. W. Gettins, James A Irving,Expand
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The structural basis for membrane binding and pore formation by lymphocyte perforin
Natural killer cells and cytotoxic T lymphocytes accomplish the critically important function of killing virus-infected and neoplastic cells. They do this by releasing the pore-forming proteinExpand
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Extracellular Matrix Remodeling by Human Granzyme B via Cleavage of Vitronectin, Fibronectin, and Laminin*
Human granzyme B (GrB) released from cytotoxic lymphocytes plays a key role in the induction of target cell apoptosis when internalized in the presence of perforin. Here we demonstrate that GrB alsoExpand
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Selective Regulation of Apoptosis: the Cytotoxic Lymphocyte Serpin Proteinase Inhibitor 9 Protects against Granzyme B-Mediated Apoptosis without Perturbing the Fas Cell Death Pathway
ABSTRACT Cytotoxic lymphocytes (CLs) induce caspase activation and apoptosis of target cells either through Fas activation or through release of granule cytotoxins, particularly granzyme B. CLsExpand
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The MACPF/CDC family of pore-forming toxins
Pore‐forming toxins (PFTs) are commonly associated with bacterial pathogenesis. In eukaryotes, however, PFTs operate in the immune system or are deployed for attacking prey (e.g. venoms). This reviewExpand
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A Cytosolic Granzyme B Inhibitor Related to the Viral Apoptotic Regulator Cytokine Response Modifier A Is Present in Cytotoxic Lymphocytes*
  • J. Sun, C. Bird, +5 authors P. Bird
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 1 November 1996
Using a polymerase chain reaction strategy we identified a serine proteinase inhibitor (serpin) in human bone marrow that is related to the cellular serpin proteinase inhibitor 6 (PI-6) and the viralExpand
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Human clade B serpins (ov-serpins) belong to a cohort of evolutionarily dispersed intracellular proteinase inhibitor clades that protect cells from promiscuous proteolysis
Serpins are unique among the various types of active site proteinase inhibitors because they covalently trap their targets by undergoing an irreversible conformational rearrangement. Members of theExpand
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A Role for Granzyme M in TLR4-Driven Inflammation and Endotoxicosis
Lymphocyte perforin and serine protease granzymes are well-recognized extrinsic mediators of apoptosis. We now demonstrate that cytotoxic lymphocyte granule components profoundly augment the myeloidExpand
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A Common Fold Mediates Vertebrate Defense and Bacterial Attack
Proteins containing membrane attack complex/perforin (MACPF) domains play important roles in vertebrate immunity, embryonic development, and neural-cell migration. In vertebrates, the ninth componentExpand
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A New Family of 10 Murine Ovalbumin Serpins Includes Two Homologs of Proteinase Inhibitor 8 and Two Homologs of the Granzyme B Inhibitor (Proteinase Inhibitor 9)*
Serine proteinase inhibitors (serpins) are classically regulators of extracellular proteolysis, however, recent evidence suggests that some function intracellularly. Such “ovalbumin” serpins includeExpand
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