Zobrazeno 1 - 10
of 990
pro vyhledávání: '"folding Intermediate"'
Publikováno v:
Frontiers in Bioscience-Landmark, Vol 29, Iss 11, p 379 (2024)
This paper is dedicated to the memory of Oleg B. Ptitsyn (1929-1999) and presents an answer to his question: “What is the role of conserved non-functional residues in protein folding?”. This answer follows from the experimental works of three lab
Externí odkaz:
https://doaj.org/article/26af94d74e4348bdb381adda9b46ff48
Akademický článek
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Autor:
Chiaki Nishimura, Takeshi Kikuchi
Publikováno v:
Molecules, Vol 28, Iss 9, p 3970 (2023)
Protein folding is essential for a polypeptide chain to acquire its proper structure and function. Globins are a superfamily of ubiquitous heme-binding α-helical proteins whose function is principally to regulate oxygen homoeostasis. In this review,
Externí odkaz:
https://doaj.org/article/d1d9c6da209446f091ab9c1d90d66e37
Autor:
Balamurugan Dhayalan, Michael D. Glidden, Alexander N. Zaykov, Yen-Shan Chen, Yanwu Yang, Nelson B. Phillips, Faramarz Ismail-Beigi, Mark A. Jarosinski, Richard D. DiMarchi, Michael A. Weiss
Publikováno v:
Frontiers in Endocrinology, Vol 13 (2022)
The mutant proinsulin syndrome is a monogenic cause of diabetes mellitus due to toxic misfolding of insulin’s biosynthetic precursor. Also designated mutant INS-gene induced diabetes of the young (MIDY), this syndrome defines molecular determinants
Externí odkaz:
https://doaj.org/article/ac8abdb348a7445ab68c20aba3dbef24
Autor:
Yanwu Yang, Michael D. Glidden, Balamurugan Dhayalan, Alexander N. Zaykov, Yen-Shan Chen, Nalinda P. Wickramasinghe, Richard D. DiMarchi, Michael A. Weiss
Publikováno v:
Frontiers in Endocrinology, Vol 13 (2022)
Toxic misfolding of proinsulin variants in β-cells defines a monogenic diabetes syndrome, designated mutant INS-gene induced diabetes of the young (MIDY). In our first study (previous article in this issue), we described a one-disulfide peptide mode
Externí odkaz:
https://doaj.org/article/81bdb69b388b4048aa3b5feb43d1bcd4
Publikováno v:
Molecules, Vol 28, Iss 8, p 3494 (2023)
Investigations of protein folding have largely involved the use of disulfide-containing proteins, since the disulfide-coupled folding of proteins allows folding intermediates to be trapped and their conformations determined. However, studies of the f
Externí odkaz:
https://doaj.org/article/2aa2171738c94356b9fcfe7dcdba4c7d
Autor:
Charlier, Cyril, Alderson, T. Reid, Courtney, Joseph M., Ying, Jinfa, Anfinrud, Philip, Bax, Adriaan
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2018 May 01. 115(18), E4169-E4178.
Externí odkaz:
https://www.jstor.org/stable/26508765
Publikováno v:
Frontiers in Chemistry, Vol 8 (2020)
AAI, the major alpha-amylase inhibitor (AAI) present in the seeds of the Mexican crop plant Amaranthus hypocondriacus is a 32-residue-long polypeptide with three disulfide bridges. Its structure is most closely related to the plant amylase inhibitor
Externí odkaz:
https://doaj.org/article/19beee9811484ecb9e14d7752122dc59
Autor:
Wilson, Corey J., Das, Payel, Clementi, Cecilia, Matthews, Kathleen S., Wittung-Stafshede, Pernilla
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2005 Oct 01. 102(41), 14563-14568.
Externí odkaz:
https://www.jstor.org/stable/4143357
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2005 Apr 01. 102(14), 5026-5031.
Externí odkaz:
https://www.jstor.org/stable/3375173