Results 31 to 40 of about 174,472 (299)

Folding of small disulfide-rich proteins : clarifying the puzzle [PDF]

, 2006
Premi a l'excel·lència investigadora. Àmbit de les Ciències Experimentals. 2008The process by which small proteins fold to their native conformations has been intensively studied over the last few decades.
Apuy, Arolas, Arolas, Arolas, Arolas, Baneyx, Bardwell, Cemazar, Cemazar, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chang, Chatrenet, Creighton, Creighton, Creighton, Creighton, Creighton, Daggett, Daly, Darby, Dobson, Ellgaard, Francesc X. Aviles, Fuller, Gehrmann, Goldberg, Goldenberg, Heitz, Hogg, Houry, Joan L. Arolas, Jui-Yoa Chang, Klein-Seetharaman, Kortemme, Kuhlman, Laity, Li, Lu, Matagne, Narayan, Narayan, Narayan, Narayan, Onuchic, Permyakov, Ross, Ruoppolo, Ruoppolo, Salamanca, Salvador Ventura, Scheraga, Shimotakahara, Shin, van den Berg, van den Berg, van Mierlo, van Mierlo, Venhudova, Wedemeyer, Weissman, Welker, Welker, Wu, Yang, Zavodszky   +73 more
core   +2 more sources

Oxidative protein folding in the mitochondrial intermembrane space [PDF]

, 2010
Disulfide bond formation is a crucial step for oxidative folding and necessary for the acquisition of a protein's native conformation. Introduction of disulfide bonds is catalyzed in specialized subcellular compartments and requires the coordinated ...
Anfinsen CB, Dionisia P. Sideris, Giorda R, Kamitani S, Kostas Tokatlidis   +4 more
core   +1 more source

Thioredoxin-1 maintains mechanistic target of rapamycin (mTOR) function during oxidative stress in cardiomyocytes [PDF]

, 2017
Thioredoxin 1 (Trx1) is a 12-kDa oxidoreductase that catalyzes thiol-disulfide exchange reactions to reduce proteins with disulfide bonds. As such, Trx1 helps protect the heart against stresses, such as ischemia and pressure overload.
Bhat, Santosh, Chen, Yanbin, Chin, Adave, Hirabayashi, Yoko, Hirata, Tsuyoshi, Nagarajan, Narayani, Naito, Daichi, Oka, Shin-Ichi, Sadoshima, Junichi, Saito, Toshiro, Schesing, Kevin, Sciarretta, Sebastiano, Shao, Dan, Suzuki, Wataru, Yaginuma, Hiroaki, Yodoi, Junji, Zhai, Peiyong   +16 more
core   +1 more source

Bridging Small Molecules to Modified Bacterial Microparticles Using a Disulphide Linkage: MIS416 as a Cargo Delivery System.

PLoS ONE, 2015
MIS416 is an intact minimal cell wall skeleton derived from Proprionibacterium acnes that is phagocytosed by antigen presenting cells, including dendritic cells (DCs).
Francesco Mainini, David S Larsen, Gill A Webster, Sarah L Young, Michael R Eccles   +4 more
doaj   +1 more source

Distinct roles and actions of protein disulfide isomerase family enzymes in catalysis of nascent-chain disulfide bond formation

iScience, 2021
Summary: The mammalian endoplasmic reticulum (ER) harbors more than 20 members of the protein disulfide isomerase (PDI) family that act to maintain proteostasis.
Chihiro Hirayama, Kodai Machida, Kentaro Noi, Tadayoshi Murakawa, Masaki Okumura, Teru Ogura, Hiroaki Imataka, Kenji Inaba   +7 more
doaj   +1 more source

Model building of disulfide bonds in proteins with known three-dimensional structure [PDF]

, 1988
As an aid in the selection of sites in a protein where a disulfide bond might be engineered, a computer program has been developed. The algorithm starts with the generation of Cβ positions from the N, Cα and C atom coordinates available from a three ...
Dijkstra, Bauke W., Hazes, Bart
core   +2 more sources

Disulfide bond formation and ToxR activity in Vibrio cholerae. [PDF]

PLoS ONE, 2012
Virulence factor production in Vibrio cholerae is complex, with ToxRS being an important part of the regulatory cascade. Additionally, ToxR is the transcriptional regulator for the genes encoding the major outer membrane porins OmpU and OmpT.
Vera H I Fengler, Eva C Boritsch, Sarah Tutz, Andrea Seper, Hanna Ebner, Sandro Roier, Stefan Schild, Joachim Reidl   +7 more
doaj   +1 more source

Synthesis of the Most Potent Isomer of μ-Conotoxin KIIIA Using Different Strategies

Molecules, 2023
In the chemical synthesis of conotoxins with multiple disulfide bonds, the oxidative folding process can result in diverse disulfide bond connectivities, which presents a challenge for determining the natural disulfide bond connectivities and leads to ...
Xunxun Jian, Yong Wu, Zaoli Mei, Xiaopeng Zhu, Dongting Zhangsun, Sulan Luo   +5 more
doaj   +1 more source

Maternal nicotine exposure leads to impaired disulfide bond formation and augmented endoplasmic reticulum stress in the rat placenta.

PLoS ONE, 2015
Maternal nicotine exposure has been associated with many adverse fetal and placental outcomes. Although underlying mechanisms remain elusive, recent studies have identified that augmented endoplasmic reticulum (ER) stress is linked to placental ...
Michael K Wong, Catherine J Nicholson, Alison C Holloway, Daniel B Hardy   +3 more
doaj   +1 more source

Review

, 2020
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R, Arai K, Baskakov IV, Creighton TE, Dittmer K, Du Vigneaud V, Janeček J, Metanis N, Musiol HJ, Muttenthaler M, Nygard B, O'Donnell ME, Welch M, Yang F   +13 more
core   +1 more source