Results 51 to 60 of about 174,472 (299)

Preventing disulfide bond formation weakens non-covalent forces among lysozyme aggregates. [PDF]

PLoS ONE, 2014
Nonnative disulfide bonds have been observed among protein aggregates in several diseases like amyotrophic lateral sclerosis, cataract and so on. The molecular mechanism by which formation of such bonds promotes protein aggregation is poorly understood ...
Vijay Kumar Ravi, Mohit Goel, Hema Chandra Kotamarthi, Sri Rama Koti Ainavarapu, Rajaram Swaminathan   +4 more
doaj   +1 more source

Solvent Induced Disulfide Bond Formation in 2,5-dimercapto-1,3,4-thiadiazole [PDF]

, 2007
Disulfide bond formation is the decisive event in the protein folding to determine the conformation and stability of protein. To achieve this disulfide bond formation in vitro, we took 2,5-dimercapto-1,3,4-thiadiazole (DMcT) as a model compound. We found
Palanisamy Kalimuthu, Palraj Kalimuthu, S. Abraham John   +2 more
core   +1 more source

Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation [PDF]

, 2017
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested pre-existing disulfide links are absolutely required to allow protein folding and ...
Bulleid, Neil J., Pringle, Marie Anne, Robinson, Philip J., Woolhead, Cheryl A.   +3 more
core   +1 more source

Disulfide Bonds Enable Accelerated Protein Evolution [PDF]

Molecular Biology and Evolution, 2017
The different proteins of any proteome evolve at enormously different rates. What factors contribute to this variability, and to what extent, is still a largely open question. We hypothesized that disulfide bonds, by increasing protein stability, should make proteins' structures relatively independent of their amino acid sequences, thus acting as ...
Felix, Feyertag, David, Alvarez-Ponce
openaire   +2 more sources

Function‐driven design of a surrogate interleukin‐2 receptor ligand

FEBS Letters, EarlyView.
Interleukin (IL)‐2 signaling can be achieved and precisely fine‐tuned through the affinity, distance, and orientation of the heterodimeric receptors with their ligands. We designed a biased IL‐2 surrogate ligand that selectively promotes effector T and natural killer cell activation and differentiation. Interleukin (IL) receptors play a pivotal role in
Ziwei Tang, Zelin Cheng, Teng Li, Fulian Wang, Liangminghui Zhang, Xiuxiu He, Lili Liu, Wei Wang, Aibin Liang, Guang Yang   +9 more
wiley   +1 more source

Forcing the reversibility of a mechanochemical reaction

Nature Communications, 2018
Mechanical force can facilitate thermodynamically unfavourable reactions. Here, the authors found that a stretching force can promote the SN2 cleavage of a protein disulfide bond by weak nucleophilic thiols, and that removing this force reverses the ...
Amy E. M. Beedle, Marc Mora, Colin T. Davis, Ambrosius P. Snijders, Guillaume Stirnemann, Sergi Garcia-Manyes   +5 more
doaj   +1 more source

Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073 [PDF]

, 2009
Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the proper folding and functioning of secreted and membrane-associated bacterial proteins.
Totsika, Makrina, Heras, Begona, Wurpel, Daniel J., Schembri, Mark A.   +3 more
core   +2 more sources

Organ‐specific redox imbalances in spinal muscular atrophy mice are partially rescued by SMN antisense oligonucleotides

FEBS Letters, EarlyView.
We identified a systemic, progressive loss of protein S‐glutathionylation—detected by nonreducing western blotting—alongside dysregulation of glutathione‐cycle enzymes in both neuronal and peripheral tissues of Taiwanese SMA mice. These alterations were partially rescued by SMN antisense oligonucleotide therapy, revealing persistent redox imbalance as ...
Sofia Vrettou, Brunhilde Wirth
wiley   +1 more source

Disulfide bond in SUN2 regulates dynamic remodeling of LINC complexes at the nuclear envelope

Life Science Alliance, 2023
The LINC complex tethers the cell nucleus to the cytoskeleton to regulate mechanical forces during cell migration, differentiation, and various diseases.
Rahul Sharma, Martin W Hetzer
doaj   +1 more source

Elucidation of the disulfide folding pathway of hirudin by a topology-based approach [PDF]

, 2003
A theoretical model for the folding of proteins containing disulfide bonds is introduced. The model exploits the knowledge of the native state to favour the progressive establishment of native interactions.
De Filippis, V., Maritan, A., Micheletti, C., Seno, F.   +3 more
core   +2 more sources