Results 21 to 30 of about 1,312,330 (378)

Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction

FEBS Open Bio, 2014
Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
doaj   +1 more source

The role of a disulfide bridge in the stability and folding kinetics of Arabidopsis thaliana cytochrome c6A [PDF]

, 2011
Cytochrome c 6A is a eukaryotic member of the Class I cytochrome c family possessing a high structural homology with photosynthetic cytochrome c 6 from cyanobacteria, but structurally and functionally distinct through the presence of a disulfide bond and
Arslan, Babul, Barker, Bartalesi, Beasty, Bertini, Betz, Bialek, Borgia, Brems, Carter, Chen, Chida, Christopher J. Howe, Cohen, Colon, Colon, Derek S. Bendall, Ellman, Elove, Feige, Gianni, Guidry, Gupta, Hogg, Howe, Jody M. Mason, Jonathan A.R. Worrall, Lange, Lange, Marcaida, Mason, Mason, Merchant, Mines, Molina-Heredia, Moore, Myers, Ogawa, Pace, Pace, Parrini, Pascher, Ptitsyn, Roder, Russell, Russell, Santoro, Satoh, Sauder, Schlarb-Ridley, Schmidt, Sosnick, Tezcan, Travaglini-Allocatelli, Travaglini-Allocatelli, Travaglini-Allocatelli, Ullah, Ullah, Wastl, Wastl, Wastl, Williams, Worrall, Worrall   +64 more
core   +1 more source

Crystallographic Studies Evidencing the High Energy Tolerance to Disrupting the Interface Disulfide Bond of Thioredoxin 1 from White Leg Shrimp Litopenaeus vannamei

Molecules, 2014
Thioredoxin (Trx) is a small 12-kDa redox protein that catalyzes the reduction of disulfide bonds in proteins from different biological systems. A recent study of the crystal structure of white leg shrimp thioredoxin 1 from Litopenaeus vannamei (LvTrx ...
Adam A. Campos-Acevedo, Enrique Rudiño-Piñera   +1 more
doaj   +1 more source

Basis for using thioredoxin as an electron donor by Schizosaccharomyces pombe Gpx1 and Tpx1

AMB Express, 2022
Key points spGpx1 contains two conserved Cys residues (Cys36 and Cys82), which may form a disulfide bond upon oxidation and the reduction of this disulfide bond is most likely to be mediated by Trx in vivo.
Fawad Ahmad, Muhammad Faizan Latif, Ying Luo, Ying Huang   +3 more
doaj   +1 more source

Disulfides – Effective radical generators for flame retardancy of polypropylene [PDF]

, 2014
The potential of thirteen aliphatic, aromatic, thiuram and heterocyclic substituted organic disulfide derivatives of the general formula R-S-S-R’ as a new group of halogen-free flame retardants (FR) for polypropylene films have been investigated ...
Abdeli, Alabugin, Anton Holappa, Aubert, Beach, Beerheide, Bennett, Braunecker, Camino, Carl-Eric Wilén, Chandrasiri, Eichorn, Furusawa, Garcia-Ruano, German Standard DIN 4102-1, Glotova, Gouinlock, Holger Hoppe, Ingold, Ivanov, Kaur, Koval, Leino, Mak, Marney, Melanie Aubert, Miyashita, Montazerozohori, Muth, Nicolas, Parker, Pfaendner, Pfaendner, Redpath, Riddles, Rudolf Pfaendner, Step, Teija Tirri, Tirri, Tobolsky, Vandeputte, Vega, Wan, Wang, Weronika Pawelec, Xu, Štaudner   +46 more
core   +1 more source

TREATMENT OF DISULFIDE BONDS IN COARSE-GRAINED UNRES FORCE FIELD

TASK Quarterly, 2016
Disulfide bonds, despite the advances of the computational methods, are underrepresented in theoretical chemistry and the role of disulfide bonds is often diminished in bioinformatical studies.
PAWEŁ KRUPA
doaj   +1 more source

Engineering a disulfide bond in the lid hinge region of Rhizopus chinensis lipase: increased thermostability and altered acyl chain length specificity. [PDF]

PLoS ONE, 2012
The key to enzyme function is the maintenance of an appropriate balance between molecular stability and structural flexibility. The lid domain which is very important for "interfacial activation" is the most flexible part in the lipase structure. In this
Xiao-Wei Yu, Nian-Jiang Tan, Rong Xiao, Yan Xu   +3 more
doaj   +1 more source

Reductive chain separation of botulinum A toxin — a prerequisite to its inhibitory action on exocytosis in chromaffin cells [PDF]

, 1989
Cleavage of the disulfide bond linking the heavy and the light chains of tetanus toxin is necessary for its inhibitory action on exocytotic release ofcatecholamines from permeabi1ized chromaffin cells [(1989) FEBS Lett. 242, 245-248; (1989) J. Neurochern.
Ahnert-Hilger, Ahnert-Hilger, Ahnert-Hilger, Ahnert-Hilger, Ammann, B. Stecher, Bhakdi, Bhakdi, Bittner, Dreyer, Eisel, G. Ahnert-Hilger, Habermann, Habermann, Knight, Knight, Livett, M. Gratzl, Maisey, Marxen, Mellanby, Penner, Poulain, Sellin, Simpson, Weller   +25 more
core   +1 more source

Measurement of Redox States of the β3 Integrin Disulfide Bonds by Mass Spectrometry

Bio-Protocol, 2019
Functional disulfide bonds mediate a change in protein function in which they reside when cleaved or formed. To elucidate how a functional disulfide bond controls protein activity, it is critical that the redox state of the bond in the population of ...
Joyce Chiu
doaj   +1 more source

The susceptibility of disulfide bonds towards radiation damage may be explained by S...O interactions

IUCrJ, 2020
Radiation-induced damage to protein crystals during X-ray diffraction data collection is a major impediment to obtaining accurate structural information on macromolecules.
Rajasri Bhattacharyya, Jesmita Dhar, Shubhra Ghosh Dastidar, Pinak Chakrabarti, Manfred S. Weiss   +4 more
doaj   +1 more source