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|a 9780387251516
|9 978-0-387-25151-6
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|a 10.1007/b106833
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|a The ADAM Family of Proteases
|h [electronic resource] /
|c edited by Nigel M Hooper, Uwe Lendeckel.
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|a 1st ed. 2005.
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|a New York, NY :
|b Springer US :
|b Imprint: Springer,
|c 2005.
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|a XIV, 344 p.
|b online resource.
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|a text
|b txt
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|a computer
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|a online resource
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|a text file
|b PDF
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|a Proteases in Biology and Disease ;
|v 4
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|a Contributing 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.
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|a The 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.
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|a Biochemistry.
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|a Biochemistry.
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|a Hooper, Nigel M.
|e editor.
|4 edt
|4 http://id.loc.gov/vocabulary/relators/edt
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|a Lendeckel, Uwe.
|e editor.
|4 edt
|4 http://id.loc.gov/vocabulary/relators/edt
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|a SpringerLink (Online service)
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|t Springer Nature eBook
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|i Printed edition:
|z 9780387505855
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|i Printed edition:
|z 9781441937759
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|i Printed edition:
|z 9780387251493
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|a Proteases in Biology and Disease ;
|v 4
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|u https://doi.uam.elogim.com/10.1007/b106833
|z Texto Completo
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|a ZDB-2-SBL
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|a ZDB-2-SXB
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|a Biomedical and Life Sciences (SpringerNature-11642)
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|a Biomedical and Life Sciences (R0) (SpringerNature-43708)
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