Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Khadar M. Abdi"'
Autor:
Gwangrog Lee, Khadar M. Abdi, Ming Yang, Christopher J. Schofield, Vann Bennett, Piotr E. Marszalek, Whasil Lee, Minkyu Kim, Mahir Rabbi
Publikováno v:
Biophysical Journal. 98(12):3086-3092
Anfinsen's thermodynamic hypothesis implies that proteins can encode for stretching through reversible loss of structure. However, large in vitro extensions of proteins that occur through a progressive unfolding of their domains typically dissipate a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdf11dad5db5f642924af5f704d784ce
Publikováno v:
Journal of Biological Chemistry. 281:5741-5749
Ankyrins contain significant amino acid identity and are co-expressed in many cell types yet maintain unique functions in vivo. Recent studies have identified the highly divergent C-terminal domain in ankyrin-B as the key domain for driving ankyrin-B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b769408743aa5958497ba09eab59965f
https://doi.org/10.1074/jbc.m506697200
https://doi.org/10.1074/jbc.m506697200
Autor:
Peter J. Mohler, Khadar M. Abdi, Vann Bennett, Lydia Davis, Karen F. Roberts, Sarah K. Jones, Chong-Rak Kim, Janis A. Hoffman, Jonathan Q. Davis
Publikováno v:
Journal of Biological Chemistry. 279:25798-25804
Ankyrins-R, -B, and -G are a family of membrane-associated adaptors required for localization of structurally diverse proteins to specialized membrane domains, including axon initial segments, cardiomyocyte T-tubules, and epithelial cell lateral memb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4d8d61d749390e039c06338ba0a70262
https://doi.org/10.1074/jbc.m401296200
https://doi.org/10.1074/jbc.m401296200
Autor:
Mischa Machius, Chad A. Brautigam, Khadar M. Abdi, Diana R. Tomchick, Peter Michaely, Vann Bennett, Lydia Davis
Publikováno v:
The Journal of biological chemistry. 284(11)
Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a48132cc09badc3e9df92a42e385f44
https://pubmed.ncbi.nlm.nih.gov/19098307
https://pubmed.ncbi.nlm.nih.gov/19098307
Autor:
Khadar M. Abdi, Vann Bennett
Adducin promotes assembly of spectrin-actin complexes, and is a target for regulation by calmodulin, protein kinase C, and rho kinase. We demonstrate here that adducin is required to stabilize preformed lateral membranes of human bronchial epithelial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ec64370e1bfa164f9f5cdda5a55ef37
https://europepmc.org/articles/PMC2230604/
https://europepmc.org/articles/PMC2230604/
Publikováno v:
The Journal of biological chemistry. 281(9)
Ankyrins contain significant amino acid identity and are co-expressed in many cell types yet maintain unique functions in vivo. Recent studies have identified the highly divergent C-terminal domain in ankyrin-B as the key domain for driving ankyrin-B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a10f33eb3f8cdd3e9bf1e3ad553c3bdd
https://pubmed.ncbi.nlm.nih.gov/16368689
https://pubmed.ncbi.nlm.nih.gov/16368689
Autor:
Peter J, Mohler, Janis A, Hoffman, Jonathan Q, Davis, Khadar M, Abdi, Chong-Rak, Kim, Sarah K, Jones, Lydia H, Davis, Karen F, Roberts, Vann, Bennett
Publikováno v:
The Journal of biological chemistry. 279(24)
Ankyrins-R, -B, and -G are a family of membrane-associated adaptors required for localization of structurally diverse proteins to specialized membrane domains, including axon initial segments, cardiomyocyte T-tubules, and epithelial cell lateral memb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6793b50b63ddc397be3518a7b5d2f8ab
https://pubmed.ncbi.nlm.nih.gov/15075330
https://pubmed.ncbi.nlm.nih.gov/15075330