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pro vyhledávání: '"Robert L. Church"'
Autor:
Robert L. Church
Publikováno v:
The University in Society, Volume II
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::97efe5b8919bf4e38d9169e0c435dfe9
https://doi.org/10.1515/9780691196701-007
https://doi.org/10.1515/9780691196701-007
Autor:
Robert L. Church, Heng Hsu
Publikováno v:
Progress in Natural Science. 14:1039-1052
During lens development, lens epithelial cells differentiate into fiber cells. To date, four major lens fiber cell intrinsic membrane proteins (MIP) ranging in size from 70 kD to 19 kD have been characterized. The second most abundant lens fiber cell
Publikováno v:
Genomics. 29:445-450
Four genes encoding eye lens-specific proteins, potential candidate genes for congenital cataract (CC) mutations, were mapped in the mouse genome using a panel of somatic cell hybrids and DNAs from the EU-CIB (European Collaborative Interspecific Bac
Autor:
Robert L. Church
Publikováno v:
History of Education Quarterly. 43:464-466
Autor:
Robert L. Church
Publikováno v:
History of Education Quarterly. 42:280-282
Autor:
Robert L. Church
Publikováno v:
American Journal of Education. 100:132-136
Autor:
Nancy Weber Kaye, Marian E. Durkin, Stephen L. Phillips, Albert E. Chung, Peter A. Lalley, Robert L. Church
Publikováno v:
Somatic Cell and Molecular Genetics. 16:599-603
Laminin is a multichain extracellular matrix glycoprotein found primarily in basement membranes. The molecule is made up of three subunits, designated as A, B1, and B2. Using an 850-base cDNA probe for the mouse laminin A-chain and a 1000-base cDNA p
Publikováno v:
Ophthalmic Research. 22:166-172
We have carried out limited microsequence analysis of bovine lens intrinsic membrane proteins having molecular weights of 70, 64, and 38 kD. These three polypeptides all have an identical amino acid terminal sequence, at least for the first 17 amino
Publikováno v:
Sheng wu gong cheng xue bao = Chinese journal of biotechnology. 20(4)
Using overlapping and mutant oligonucleotides as probes, gel mobility assays and competition experiments identified a sequence from -47 to -32 bp upstream of the LIM2 CAP site, which a lens protein complex bound with high affinity which appeared to b