Results 241 to 250 of about 174,472 (299)

The structure of Mycobacterium thermoresistibile MmpS5 reveals a conserved disulfide bond across mycobacteria. [PDF]

Metallomics
Cuthbert BJ, Mendoza J, de Miranda R, Papavinasasundaram K, Sassetti CM, Goulding CW.   +5 more
europepmc   +1 more source

The interaction between NLRP1 and oxidized TRX1 involves a transient disulfide bond. [PDF]

Cell Chem Biol
Geeson MB, Hsiao JC, Tsamouri LP, Ball DP, Bachovchin DA.   +4 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

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

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.
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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
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MAKING AND BREAKING DISULFIDE BONDS

Annual Review of Microbiology, 1997
▪ Abstract  It is now well established that protein folding requires the assistance of folding helpers in vivo. The formation or isomerization of disulfide bonds in proteins is a slow process requiring catalysis. In nascent polypeptide chains the cysteine residues are in the thiol form.
S, Raina, D, Missiakas
openaire   +2 more sources