Results 251 to 260 of about 96,012 (310)

Dilute but Dense – Reversible Crosslinking Enables Water‐Rich (Bio)polymer Condensates

Advanced Science, EarlyView.
Reversible crosslinking between two types of (bio)polymers drives liquid–liquid phase separation even in good solvent. The arrangement of binding motifs controls condensate formation and density, and internal network structure. Simulations and theory reveal a closed‐loop coexistence phase diagram at very low monomer concentrations and re‐entrant ...
Xinxiang Chen, Jude Ann Vishnu, Pol Besenius, Julian König, Friederike Schmid   +4 more
wiley   +1 more source

Enhancing the Antibody Production Efficiency of Chinese Hamster Ovary Cells through Improvement of Disulfide Bond Folding Ability and Apoptosis Resistance. [PDF]

Cells
Zhang C, Fu Y, Zheng W, Chang F, Shen Y, Niu J, Wang Y, Ma X.   +7 more
europepmc   +1 more source

Retraction Note: A water-soluble DsbB variant that catalyzes disulfide-bond formation in vivo. [PDF]

Nat Chem Biol
Mizrachi D, Robinson MP, Ren G, Ke N, Berkmen M, DeLisa MP.   +5 more
europepmc   +1 more source

Differential effects of disulfide bond formation in TEM-1 versus CTX-M-9 β-lactamase. [PDF]

Protein Sci
Villanueva M, Vostal LE, Cohen DN, Biesbrock D, Kuwaye EP, Driver SG, Hart KM.   +6 more
europepmc   +1 more source

Improvement in Noodle Quality and Changes in Microstructure and Disulfide Bond Content through the Addition of Pepper Straw Ash Leachate. [PDF]

Foods
Li X, Wu Y, Li C, Tong S, Zhang L, Jin J.   +5 more
europepmc   +1 more source

Deep Mutational Scanning Reveals a De Novo Disulfide Bond and Combinatorial Mutations for Engineering Thermostable Myoglobin

Küng C, Protsenko O, Vanella R, Nash MA.   +3 more
europepmc   +1 more source

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Allosteric Disulfide Bonds

Biochemistry, 2006
Disulfide bonds have been generally considered to be either structural or catalytic. Structural bonds stabilize a protein, while catalytic bonds mediate thiol-disulfide interchange reactions in substrate proteins. There is emerging evidence for a third type of disulfide bond that can control protein function by triggering a conformational change when ...
Bryan, Schmidt, Lorraine, Ho, Philip J, Hogg   +2 more
openaire   +2 more sources

How Proteins Form Disulfide Bonds

Antioxidants & Redox Signaling, 2011
The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the study of oxidative protein folding. Oxidative protein folding refers to the composite process by which a protein recovers both its native structure and its native disulfide bonds.
Depuydt, Matthieu, Messens, Joris, Collet, Jean François   +2 more
openaire   +3 more sources

Allosteric Disulfide Bonds

2011
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Hogg, Philip J., Wong, Jason W.H.
openaire   +3 more sources

Disulfide bond formation in prokaryotes

Nature Microbiology, 2018
Interest in protein disulfide bond formation has recently increased because of the prominent role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that introduces disulfide bonds into cell envelope proteins consists of Escherichia coli enzymes DsbA and DsbB.
Cristina, Landeta, Dana, Boyd, Jon, Beckwith   +2 more
openaire   +2 more sources