Zobrazeno 1 - 10 of 84 pro vyhledávání: '"Qing Xin Hua"'
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Akademický článek
Mutant INS-gene induced diabetes of youth: proinsulin cysteine residues impose dominant-negative inhibition on wild-type proinsulin transport.
Autor: Ming Liu, Leena Haataja, Jordan Wright, Nalinda P Wickramasinghe, Qing-Xin Hua, Nelson F Phillips, Fabrizio Barbetti, Michael A Weiss, Peter Arvan
Publikováno v: PLoS ONE, Vol 5, Iss 10, p e13333 (2010)
Recently, a syndrome of Mutant INS-gene-induced Diabetes of Youth (MIDY, derived from one of 26 distinct mutations) has been identified as a cause of insulin-deficient diabetes, resulting from expression of a misfolded mutant proinsulin protein in th
Externí odkaz: https://doaj.org/article/647217a66bd7465a9fc4fe391357fca2
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3
Deciphering the Hidden Informational Content of Protein Sequences
Autor: Michael A. Weiss, Yanwu Yang, Sunil Evan Saith, Wenhua Jia, Qing Xin Hua, Ming Liu, Shi Quan Hu, Peter Arvan, Jonathan Whittaker
Publikováno v: Journal of Biological Chemistry. 285:30989-31001
Protein sequences encode both structure and foldability. Whereas the interrelationship of sequence and structure has been extensively investigated, the origins of folding efficiency are enigmatic. We demonstrate that the folding of proinsulin require
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d11b6127be1cb3b629cabd00c9914a75
https://doi.org/10.1074/jbc.m110.152645
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5
Supramolecular Protein Engineering
Autor: Nelson B. Phillips, Michael A. Weiss, Qing Xin Hua, Faramarz Ismail-Beigi, Jonathan Whittaker, Zhu Li Wan, Kun Huang, Linda Whittaker, Shi Quan Hu
Publikováno v: Journal of Biological Chemistry. 285:11755-11759
Bottom-up control of supramolecular protein assembly can provide a therapeutic nanobiotechnology. We demonstrate that the pharmacological properties of insulin can be enhanced by design of “zinc staples” between hexamers. Paired (i, i+4) His subs
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::373891fc4c438315c2152ddf7916df51
https://doi.org/10.1074/jbc.c110.105825
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6
An Achilles' Heel in an Amyloidogenic Protein and Its Repair
Autor: Robert Tycko, Yanwu Yang, Michael A. Weiss, Faramarz Ismail-Beigi, Panayotis G. Katsoyannis, Aneta T. Petkova, Bin Xu, Robert B. Mackin, Nelson B. Phillips, Jonathan Whittaker, Ying-Chi Chu, Qing-xin Hua, Kun Huang, Shi-Quan Hu, I-Ju Ye
Publikováno v: Journal of Biological Chemistry. 285:10806-10821
Insulin fibrillation provides a model for a broad class of amyloidogenic diseases. Conformational distortion of the native monomer leads to aggregation-coupled misfolding. Whereas β-cells are protected from proteotoxicity by hexamer assembly, fibril
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c95faf22a5d3c763db5a752b6d197100
https://doi.org/10.1074/jbc.m109.067850
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7
Solution Structure of Proinsulin
Autor: Yanwu Yang, Qing Xin Hua, Eri H. Shimizu, Robert B. Mackin, Michael A. Weiss, Jin Liu, Meredith H. Choquette
Publikováno v: Journal of Biological Chemistry. 285:7847-7851
The folding of proinsulin, the single-chain precursor of insulin, ensures native disulfide pairing in pancreatic β-cells. Mutations that impair folding cause neonatal diabetes mellitus. Although the classical structure of insulin is well established
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1d56a8ef626b2f6dd0697929a015836a
https://doi.org/10.1074/jbc.c109.084921
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8
Contribution of Residue B5 to the Folding and Function of Insulin and IGF-I
Autor: Michael A. Weiss, Ming Liu, Linda Whittaker, Charles T. Roberts, Peter Arvan, Aubree A. Ng, Nelson B. Phillips, Stephen B. H. Kent, Youhei Sohma, Jonathan Whittaker, Qing Xin Hua, Shi Quan Hu
Publikováno v: Journal of Biological Chemistry. 285:5040-5055
Proinsulin exhibits a single structure, whereas insulin-like growth factors refold as two disulfide isomers in equilibrium. Native insulin-related growth factor (IGF)-I has canonical cystines (A6—A11, A7–B7, and A20—B19) maintained by IGF-bindi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b87f4a0507e50f0cdbfcc400440f1bca
https://doi.org/10.1074/jbc.m109.062992
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9
Crystal Structure of a 'Nonfoldable' Insulin
Autor: J. Sunil Rao, Panayotis G. Katsoyannis, Birgit Klaproth, Michael A. Weiss, Ying Chi Chu, Meredith H. Choquette, Pierre De Meyts, Peter Arvan, Ming Liu, Zhu Ii Wan, Qing Xin Hua, Robert B. Mackin, Hassan Aladdin
Publikováno v: Journal of Biological Chemistry. 284:35259-35272
Protein evolution is constrained by folding efficiency (“foldability”) and the implicit threat of toxic misfolding. A model is provided by proinsulin, whose misfolding is associated with β-cell dysfunction and diabetes mellitus. An insulin analo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::485e6b75ff4fa94f495cde6ecf1bed11
https://doi.org/10.1074/jbc.m109.046888
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10
Enhancing the Activity of a Protein by Stereospecific Unfolding
Autor: Panayotis G. Katsoyannis, Shuhua Wang, Michael A. Weiss, Satoe Nakagawa, Wenhua Jia, Qing Xin Hua, Shi Quan Hu, Jonathan Whittaker, Bin Xu, Kun Huang
Publikováno v: Journal of Biological Chemistry. 284:14586-14596
A central tenet of molecular biology holds that the function of a protein is mediated by its structure. An inactive ground-state conformation may nonetheless be enjoined by the interplay of competing biological constraints. A model is provided by ins
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f98944a8be78e0dd0b1340f023708c36
https://doi.org/10.1074/jbc.m900085200
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