Structure and chromosomal localization of the human thrombospondin gene
dc.contributor.author | Wolf, Frederick W. | en_US |
dc.contributor.author | Eddy, Roger L. | en_US |
dc.contributor.author | Shows, Thomas B. | en_US |
dc.contributor.author | Dixit, Vishva M. | en_US |
dc.date.accessioned | 2006-04-10T13:47:30Z | |
dc.date.available | 2006-04-10T13:47:30Z | |
dc.date.issued | 1990-04 | en_US |
dc.identifier.citation | Wolf, Frederick W., Eddy, Roger L., Shows, Thomas B., Dixit, Vishva M. (1990/04)."Structure and chromosomal localization of the human thrombospondin gene." Genomics 6(4): 685-691. <http://hdl.handle.net/2027.42/28657> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WG1-4DNHPWK-BJ/2/3e22091a4f53fc4b290a302889dd705d | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/28657 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2341158&dopt=citation | en_US |
dc.description.abstract | Thrombospondin (THBS1) is a large modular glycoprotein component of the extracellular matrix and contains a variety of distinct domains, including three repeating subunits (types I, II, and III) that share homology to an assortment of other proteins. Determination of THBS1 gene structure has revealed that the type I repeat modules are encoded by symmetrical exons and that the heparin-binding domain is encoded by a single exon. To further elucidate the higher level organization of THBS1, the gene was localized to the q11-qter region of chromosome 15. | en_US |
dc.format.extent | 677853 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Structure and chromosomal localization of the human thrombospondin gene | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Genetics | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pathology, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationum | Department of Pathology, The University of Michigan Medical School, Ann Arbor, Michigan 48109, USA | en_US |
dc.contributor.affiliationother | Department of Human Genetics, Roswell Park Memorial Institute, Buffalo, New York 14263, USA | en_US |
dc.contributor.affiliationother | Department of Human Genetics, Roswell Park Memorial Institute, Buffalo, New York 14263, USA | en_US |
dc.identifier.pmid | 2341158 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/28657/1/0000474.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0888-7543(90)90505-O | en_US |
dc.identifier.source | Genomics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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