Remarkable roles of proteolysis on and beyond the cell surface.
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[1] M. Citron,et al. Expression Analysis of BACE2 in Brain and Peripheral Tissues* , 2000, The Journal of Biological Chemistry.
[2] R. W. Rauser,et al. Impaired endochondral ossification and angiogenesis in mice deficient in membrane-type matrix metalloproteinase I. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[3] A. Parks,et al. Ligand endocytosis drives receptor dissociation and activation in the Notch pathway. , 2000, Development.
[4] B. Fingleton,et al. Matrix metalloproteinases: biologic activity and clinical implications. , 2000, Journal of clinical oncology : official journal of the American Society of Clinical Oncology.
[5] Z. Werb,et al. The matrix metalloproteinase stromelysin-1 acts as a natural mammary tumor promoter , 2000, Oncogene.
[6] G. Giannelli,et al. Role of Cell Surface Metalloprotease Mt1-Mmp in Epithelial Cell Migration over Laminin-5 , 2000, The Journal of cell biology.
[7] A Cumano,et al. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. , 2000, Molecular cell.
[8] P. Primakoff,et al. The ADAM gene family: surface proteins with adhesion and protease activity. , 2000, Trends in genetics : TIG.
[9] Raphael Kopan,et al. A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1. , 2000, Molecular cell.
[10] B. Fingleton,et al. Matrix metalloproteinase-7-dependent release of tumor necrosis factor-alpha in a model of herniated disc resorption. , 2000, The Journal of clinical investigation.
[11] B. Fingleton,et al. The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis , 1999, Current Biology.
[12] Alfredo G. Tomasselli,et al. Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity , 1999, Nature.
[13] R. Barbour,et al. Purification and cloning of amyloid precursor protein β-secretase from human brain , 1999, Nature.
[14] David G. Tew,et al. Identification of a Novel Aspartic Protease (Asp 2) as β-Secretase , 1999, Molecular and Cellular Neuroscience.
[15] J. Hodgkin,et al. The gon-1 gene is required for gonadal morphogenesis in Caenorhabditis elegans. , 1999, Developmental biology.
[16] C. Blobel,et al. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. , 1999, Journal of cell science.
[17] J. Treanor,et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. , 1999, Science.
[18] L. Matrisian,et al. Cancer biology: Extracellular proteinases in malignancy , 1999, Current Biology.
[19] L. Matrisian,et al. Regulation of intestinal alpha-defensin activation by the metalloproteinase matrilysin in innate host defense. , 1999, Science.
[20] J. Ward,et al. MT1-MMP-Deficient Mice Develop Dwarfism, Osteopenia, Arthritis, and Connective Tissue Disease due to Inadequate Collagen Turnover , 1999, Cell.
[21] R. Blelloch,et al. Control of cell migration during Caenorhabditis elegans development. , 1999, Current opinion in cell biology.
[22] D. Moerman. Organ morphogenesis: A metalloprotease prepares the way , 1999, Current Biology.
[23] R. Wynn,et al. Cloning and Characterization of ADAMTS11, an Aggrecanase from the ADAMTS Family* , 1999, The Journal of Biological Chemistry.
[24] Timo Sorsa,et al. Tumor targeting with a selective gelatinase inhibitor , 1999, Nature Biotechnology.
[25] D. Pinkel,et al. The Stromal Proteinase MMP3/Stromelysin-1 Promotes Mammary Carcinogenesis , 1999, Cell.
[26] T. Seifert,et al. Matrix metalloproteinases in inflammatory demyelination , 1999, Neurology.
[27] Robert Blelloch,et al. Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans , 1999, Nature.
[28] R. Wynn,et al. Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. , 1999, Science.
[29] G. Schneider,et al. Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed. , 1999, Science.
[30] C. Coeshott,et al. Converting enzyme-independent release of tumor necrosis factor alpha and IL-1beta from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[31] D. Lauffenburger,et al. Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[32] D. Selkoe,et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity , 1999, Nature.
[33] Iva Greenwald,et al. Presenilin is required for activity and nuclear access of Notch in Drosophila , 1999, Nature.
[34] William J. Ray,et al. A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain , 1999, Nature.
[35] E. Kojro,et al. Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[36] David C. Lee,et al. An essential role for ectodomain shedding in mammalian development. , 1998, Science.
[37] D. Selkoe,et al. The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease , 1998 .
[38] Joseph D. Buxbaum,et al. Evidence That Tumor Necrosis Factor α Converting Enzyme Is Involved in Regulated α-Secretase Cleavage of the Alzheimer Amyloid Protein Precursor* , 1998, The Journal of Biological Chemistry.
[39] R. Black,et al. ADAMs: focus on the protease domain. , 1998, Current opinion in cell biology.
[40] J. Baselga,et al. Pro-Tumor Necrosis Factor-α Processing Activity Is Tightly Controlled by a Component That Does Not Affect Notch Processing* , 1998, The Journal of Biological Chemistry.
[41] Y. Jan,et al. Roles for Proteolysis and Trafficking in Notch Maturation and Signal Transduction , 1998, Cell.
[42] A. Israël,et al. The Notch1 receptor is cleaved constitutively by a furin-like convertase. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[43] I. Greenwald,et al. LIN-12/Notch signaling: lessons from worms and flies. , 1998, Genes & development.
[44] Raphael Kopan,et al. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain , 1998, Nature.
[45] G. Struhl,et al. Nuclear Access and Action of Notch In Vivo , 1998, Cell.
[46] S. Bray. A Notch Affair , 1998, Cell.
[47] Julian Lewis. Notch signalling: A short cut to the nucleus , 1998, Nature.
[48] J. Foidart,et al. In Vivo Evidence That the Stromelysin-3 Metalloproteinase Contributes in a Paracrine Manner to Epithelial Cell Malignancy , 1998, The Journal of cell biology.
[49] Neil D. Rawlings,et al. Handbook of proteolytic enzymes , 1998 .
[50] Z. Werb. ECM and Cell Surface Proteolysis: Regulating Cellular Ecology , 1997, Cell.
[51] M. T. Brewer,et al. Identification and Characterization of a Pro-tumor Necrosis Factor-α-processing Enzyme from the ADAM Family of Zinc Metalloproteases* , 1997, The Journal of Biological Chemistry.
[52] S. Artavanis-Tsakonas,et al. Intracellular Cleavage of Notch Leads to a Heterodimeric Receptor on the Plasma Membrane , 1997, Cell.
[53] G. Giannelli,et al. Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. , 1997, Science.
[54] M. Lambert,et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α , 1997, Nature.
[55] Nicole Nelson,et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells , 1997, Nature.
[56] G. Rubin,et al. KUZ, a Conserved Metalloprotease-Disintegrin Protein with Two Roles in Drosophila Neurogenesis , 1996, Science.
[57] L. Coussens,et al. Matrix metalloproteinases and the development of cancer. , 1996, Chemistry & biology.
[58] P. Reinemer,et al. The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases , 1995, Protein science : a publication of the Protein Society.