000			03445nam a22004215i 4500
001			978-0-387-25151-6
003			DE-He213
005			20250710083932.0
007			cr nn 008mamaa
008			100301s2005 xxu| s |||| 0|eng d
020			_a9780387251516 _a99780387251516
024	7		_a10.1007/b106833 _2doi
082	0	4	_a572 _223
100	1		_aHooper, Nigel M. _eeditor.
245	1	4	_aThe ADAM Family of Proteases _h[recurso electrónico] / _cedited by Nigel M. Hooper, Uwe Lendeckel.
264		1	_aBoston, MA : _bSpringer US, _c2005.
300			_aXIX, 344 p. _bonline resource.
336			_atext _btxt _2rdacontent
337			_acomputer _bc _2rdamedia
338			_arecurso en línea _bcr _2rdacarrier
347			_atext file _bPDF _2rda
490	1		_aProteases in Biology and Disease ; _v4
505	0		_aContributing Authors -- Preface -- Introduction to the ADAM Family, Judith White, Lance Bridges, Douglas DeSimone, Monika Tomczuk and Tyra Wolfsberg -- Studies from ADAM Knockout Mice, Keisuke Hoiruchi and Carl P. Blobel -- ADAM8/MS2/CD156a, Jörg W. Bartsch, Silvia Naus, Andrea Rittger, Uwe Schlomann, Dirk Wildeboer -- ADAM9, Shoichi Ishiura -- ADAM10, Paul Saftig and Dieter Hartmann -- ADAM12, Ulla M. Wewer, Reidar Albrechtsen and Eva Engvall -- Adam13 function in development, Dominique Alfandari, ADAM 17, Joaquín Arribas and Soraya Ruiz-Paz -- ADAM19, Tiebang Kang, Robert G. Newcomer, Yun-Ge Zhao and Qing-Xiang Amy Sang -- ADAM28, Anne M. Fourie -- Mammalian ADAMS with Testis-Specific Or -Predominant Expression, Chunghee Cho -- Overview OF ADAMTS Proteinases and ADAMTS-2, Daniel S. Greenspan and Wei-Man Wang -- ADAMTS-3 AND ADAMTS-14, Carine Le Goff and Suneel S. Apte -- ADAMTS-4 and ADAMTS-5, Anne-Marie Malfait, Micky Tortorella and Elizabeth Arner -- ADAMTS-13, Han-Mou Tsai -- Index.
520			_aThe ADAM Family of Proteases provides the first comprehensive review of the roles of ADAMs and the related ADAMTS proteases in biology and disease. Although a few members of the ADAM (a disintegrin and metalloprotease) family have been known for some time, it is only in recent years through advances in genome sequencing that the large size of this family of zinc metalloproteases has become apparent. These proteins have multiple domains including a protease domain and a disintegrin domain. A branch of the family, called ADAMTS, also have thrombospondin-like motifs. The role of ADAMs and ADAMTS members in a diversity of biological processes is gradually coming to light. For example, some ADAMs have critical roles in the ectodomain shedding of membrane proteins including tumour necrosis factor-a, the cell signalling molecule Notch and the Alzheimer's amyloid precursor protein. Other ADAM and ADAMTS family members have key roles to play in sperm function and fertility, collagen processing, development, cardiac hypertrophy and arthritis.
650		0	_aLIFE SCIENCES.
650		0	_aBIOCHEMISTRY.
650	1	4	_aLIFE SCIENCES.
650	2	4	_aBIOCHEMISTRY, GENERAL.
700	1		_aLendeckel, Uwe. _eeditor.
710	2		_aSpringerLink (Online service)
773	0		_tSpringer eBooks
776	0	8	_iPrinted edition: _z9780387251493
830		0	_aProteases in Biology and Disease ; _v4
856	4	0	_uhttp://dx.doi.org/10.1007/b106833 _zVer el texto completo en las instalaciones del CICY
912			_aZDB-2-SBL
942			_2ddc _cER
999			_c56400 _d56400