Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Bing-Hao Luo"'
Publikováno v:
PLoS ONE, Vol 12, Iss 11, p e0187169 (2017)
Antifreeze proteins (AFPs) enhance the survival of organisms inhabiting cold environments by affecting the formation and/or structure of ice. We report the crystal structure of the first multi-domain AFP that has been characterized. The two ice bindi
Externí odkaz:
https://doaj.org/article/37d21bd5828a473a8b0a67fb1ce2a3da
Autor:
Jennifer R. Brown, Joseph D. Seymour, Timothy I. Brox, Mark L. Skidmore, Chen Wang, Brent C. Christner, Bing-Hao Luo, Sarah L. Codd
Publikováno v:
Biotechnology Reports, Vol 3, Iss C, Pp 60-64 (2014)
Liquid water present in polycrystalline ice at the interstices between ice crystals results in a network of liquid-filled veins and nodes within a solid ice matrix, making ice a low porosity porous media. Here we used nuclear magnetic resonance (NMR)
Externí odkaz:
https://doaj.org/article/40245c71820e45b39f0fb64e11586722
Autor:
Ping Hu, Bing-Hao Luo
Publikováno v:
PLoS ONE, Vol 10, Iss 1, p e0116208 (2015)
Integrins play an essential role in hemostasis, thrombosis, and cell migration, and they transmit bidirectional signals. Transmembrane/cytoplasmic domains are hypothesized to associate in the resting integrins; whereas, ligand binding and intracellul
Externí odkaz:
https://doaj.org/article/361dcab723c9494f96de50f26a0b6b71
Publikováno v:
PLoS ONE, Vol 8, Iss 10, p e76793 (2013)
The Asp of the RGD motif of the ligand coordinates with the β I domain metal ion dependent adhesion site (MIDAS) divalent cation, emphasizing the importance of the MIDAS in ligand binding. There appears to be two distinct groups of integrins that di
Externí odkaz:
https://doaj.org/article/024ec57adc3748148e3b932adc36487e
Publikováno v:
PLoS Biology, Vol 2, Iss 6, p e153 (2004)
Conformational communication across the plasma membrane between the extracellular and intracellular domains of integrins is beginning to be defined by structural work on both domains. However, the role of the alpha and beta subunit transmembrane doma
Externí odkaz:
https://doaj.org/article/4d57f8244fcc44e085211b784393fc31
Publikováno v:
Journal of Cellular Physiology. 237:4251-4261
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d254f65d81feabc087dcd26f4f0e592
https://doi.org/10.1002/jcp.30871
https://doi.org/10.1002/jcp.30871
Publikováno v:
Journal of cellular physiologyREFERENCES. 237(11)
Integrins are transmembrane proteins that transmit bi-directional signals across the cell membrane through global structural rearrangement among three different conformational states: bent, extended- closed, and extended-open conformations. However,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6d0b9176188d47ed9f8bbedd549be8bc
https://pubmed.ncbi.nlm.nih.gov/36108162
https://pubmed.ncbi.nlm.nih.gov/36108162
Autor:
Bing Hao Luo, Guannan Song
Publikováno v:
Journal of Cellular Physiology. 236:4874-4887
Integrins are heterodimeric transmembrane proteins that play important roles in various biological processes. Most integrins serve as adhesion molecules and transmit bidirectional signaling across the cell membrane through global conformational chang
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad73cfa89f93d233d121a55001864ea9
https://doi.org/10.1002/jcp.30242
https://doi.org/10.1002/jcp.30242
Autor:
Guannan, Song, Bing-Hao, Luo
Publikováno v:
Journal of cellular biochemistryREFERENCES. 122(8)
Many integrins transmit signals through global conformational changes. However, it is unclear whether integrin α
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::732162581e1181bcd2150b8c9c400f7d
https://pubmed.ncbi.nlm.nih.gov/33619784
https://pubmed.ncbi.nlm.nih.gov/33619784
Autor:
Guannan, Song, Bing-Hao, Luo
Publikováno v:
Journal of cellular physiologyREFERENCES. 236(7)
Integrins are heterodimeric transmembrane proteins that play important roles in various biological processes. Most integrins serve as adhesion molecules and transmit bidirectional signaling across the cell membrane through global conformational chang
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5e0ae7700ae0e6bca2487517fc164a32
https://pubmed.ncbi.nlm.nih.gov/33368230
https://pubmed.ncbi.nlm.nih.gov/33368230