Zobrazeno 1 - 10
of 79
pro vyhledávání: '"You-min Feng"'
Autor:
Sheng He, Bo Hu, Chao Li, Ping Lin, Wei-Guo Tang, Yun-Fan Sun, Fang-You-Min Feng, Wei Guo, Jia Li, Yang Xu, Qian-Lan Yao, Xin Zhang, Shuang-Jian Qiu, Jian Zhou, Jia Fan, Yi-Xue Li, Hong Li, Xin-Rong Yang
Publikováno v:
BMC Cancer, Vol 18, Iss 1, Pp 1-9 (2018)
Abstract Background Liver cancer is the second leading cause of cancer-related deaths and characterized by heterogeneity and drug resistance. Patient-derived xenograft (PDX) models have been widely used in cancer research because they reproduce the c
Externí odkaz:
https://doaj.org/article/1ec6149bf5984fbbaf61757bbf35315a
Publikováno v:
Protein & Peptide Letters. 17:874-880
The in vitro insulin unfolding had been studied using the "equilibrium unfolding" method where protein is unfolded by reducing reagents in the presence of trace amounts of oxidants such as oxidized glutathione. Nine intermediates were captured in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a047078752f4041b2c1609d4fc997e6a
https://doi.org/10.2174/092986610791306724
https://doi.org/10.2174/092986610791306724
Publikováno v:
Antioxidants & Redox Signaling. 10:127-140
Insulin and related proteins, which have been found not only in mammals, birds, reptiles, amphibians, fish, and cephalochordate, but also in mollusca, insects, and Caenorhabditis elegans, form a large protein family, the insulin superfamily. In compa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::258a583f97e0f9ae13def2a8c3e45640
https://doi.org/10.1089/ars.2007.1860
https://doi.org/10.1089/ars.2007.1860
Publikováno v:
The Protein Journal. 27:192-196
Contributions of the evolutionarily conserved A16Leu and B17Leu to insulin foldability were characterized by evaluating folding properties of single-chain insulin analogs. The results showed A16Leu had much more significant effects on the foldability
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e156f229c6a501c8ec8adf738485d31
https://doi.org/10.1007/s10930-007-9124-x
https://doi.org/10.1007/s10930-007-9124-x
Publikováno v:
Science in China Series C: Life Sciences. 50:717-725
The in vitro refolding process of the double-chain insulin was studied based on the investigation of in vitro single-chain insulin refolding. Six major folding intermediates, named P1A, P2B, P3A, P4B, P5B, and P6B, were captured during the folding pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03f83e04b8a46d878654cf0baeebe4f3
https://doi.org/10.1007/s11427-007-0092-3
https://doi.org/10.1007/s11427-007-0092-3
Publikováno v:
Protein & Peptide Letters. 13:423-429
Insulin is a double-chain (designated A and B chain respectively) protein hormone containing three disulfides, while insulin is synthesized in vivo as a single-chain precursor and folded well before being released from B-cells. Although the structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3959d55e083f8553f2f02b1992e90d3b
https://doi.org/10.2174/092986606776819583
https://doi.org/10.2174/092986606776819583
Publikováno v:
Acta Biochimica et Biophysica Sinica. 37:673-679
B8Gly is absolutely conserved in insulins during evolution. Moreover, its corresponding position is always occupied by a Gly residue in other members of insulin superfamily. Previous work showed that Ala replacement of B8Gly significantly decreased b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f993f867417c38eafb6f1008f3972249
https://doi.org/10.1111/j.1745-7270.2005.00093.x
https://doi.org/10.1111/j.1745-7270.2005.00093.x
Publikováno v:
Journal of Biological Chemistry. 279:55224-55233
Amphioxus insulin-like peptide (AILP) belongs to the insulin superfamily and is proposed as the common ancestor of insulin and insulin-like growth factor 1. Herein, the studies on oxidative refolding and reductive unfolding of AILP are reported. Duri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb3e4e91747fde5c8507e20463d452c2
https://doi.org/10.1074/jbc.m409030200
https://doi.org/10.1074/jbc.m409030200
Publikováno v:
Biological Chemistry. 385:1171-1175
Insulin contains three disulfide bonds, one intrachain bond, A6–A11, and two interchain bonds, A7–B7 and A20–B19. Site-directed mutagenesis results (the two cysteine residues of disulfide A7–B7 were replaced by serine) showed that disulfide A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1a751e7810132253493059427505f12
https://doi.org/10.1515/bc.2004.151
https://doi.org/10.1515/bc.2004.151
Publikováno v:
Biochemistry. 43:9225-9233
Although insulin and insulin-like growth factor-1 (IGF-1) belong to one family, insulin folds into one thermodynamically stable structure, while IGF-1-folds into two thermodynamically stable structures (native and swap forms). We have demonstrated pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6464dd8615ec7ac84222c21c418e676
https://doi.org/10.1021/bi049710y
https://doi.org/10.1021/bi049710y