ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function (Q24618923)

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English	ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function	scientific article

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instance of

scholarly article

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title

ADAMTS-1: a metalloproteinase-disintegrin essential for normal growth, fertility, and organ morphology and function (English)

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author name string

T Shindo

series ordinal

1

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H Kurihara

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2

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K Kuno

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3

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H Yokoyama

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4

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T Wada

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5

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Y Kurihara

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6

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T Imai

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7

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Y Wang

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8

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M Ogata

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9

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H Nishimatsu

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10

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N Moriyama

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11

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Y Oh-hashi

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12

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H Morita

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13

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T Ishikawa

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14

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R Nagai

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15

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Y Yazaki

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16

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K Matsushima

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17

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language of work or name

English

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publication date

May 2000

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published in

Journal of Clinical Investigation

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volume

105

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issue

10

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page(s)

1345-52

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cites work

METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity

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Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins

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Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene

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ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions

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A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells

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7 April 2017

ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix

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ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats

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ADAMTS-1 protein anchors at the extracellular matrix through the thrombospondin type I motifs and its spacing region

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Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF alpha and Notch

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Gene targeting in mice reveals a requirement for angiotensin in the development and maintenance of kidney morphology and growth factor regulation

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Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis

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Procollagen N-proteinase and procollagen C-proteinase. Two unusual metalloproteinases that are essential for procollagen processing probably have important roles in development and cell signaling

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The exon/intron organization and chromosomal mapping of the mouse ADAMTS-1 gene encoding an ADAM family protein with TSP motifs

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Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans

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KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis

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Angiotensinogen gene null-mutant mice lack homeostatic regulation of glomerular filtration and tubular reabsorption

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Structural changes of collagen components and diminution of nerves in congenital ureteropelvic junction obstruction

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Identifiers

DOI

10.1172/JCI8635

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PMC publication ID

315464

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PubMed publication ID

10811842

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