Results 61 to 70 of about 1,312,330 (378)

NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra Naja naja atra [PDF]

open access: yes, 2013
The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin ...
Chang, Long-Sen   +3 more
core   +2 more sources

A pathway for disulfide bond formation in vivo. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1993
Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations in the gene for a second protein, DsbB, which is also necessary for disulfide bond formation. Evidence suggests that DsbB may act by reoxidizing DsbA, thereby regenerating its ability to donate its disulfide bond to target proteins. We
Bardwell, J.C.A.   +5 more
openaire   +3 more sources

Lysine Decarboxylase with an Enhanced Affinity for Pyridoxal 5-Phosphate by Disulfide Bond-Mediated Spatial Reconstitution. [PDF]

open access: yesPLoS ONE, 2017
Lysine decarboxylase (LDC) catalyzes the decarboxylation of l-lysine to produce cadaverine, an important industrial platform chemical for bio-based polyamides.
Hye-Young Sagong, Kyung-Jin Kim
doaj   +1 more source

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

open access: yes, 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   +2 more
core   +1 more source

Characterization of the redox activity and disulfide bond formation in Apurinic/apyrimidinic endonuclease [PDF]

open access: yes, 2012
Apurinic/apyrimidinic endonuclease (APE1) is an unusual nuclear redox factor in which the redox-active cysteines identified to date, C65 and C93, are surface inaccessible residues whose activities may be influenced by partial unfolding of APE1. To assess
Chen, Qiujia   +7 more
core   +1 more source

The intracellular domain of TLR2 is capable of high‐affinity Zn binding: possible outcomes for the receptor activation

open access: yesFEBS Letters, EarlyView.
Toll‐like receptors (TLRs) are important in the innate immune system. This study explores the zinc‐binding ability of the TLR2 TIR domain (TLR2TIR). We found that TLR2TIR binds zinc with nanomolar affinity through its cysteine residues. Two of them, C673 and C713, are vital for receptor activation, indicating that zinc may play a role in initiating ...
Vladislav A. Lushpa   +8 more
wiley   +1 more source

Forcing the reversibility of a mechanochemical reaction

open access: yesNature 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   +5 more
doaj   +1 more source

EspA acts as a critical mediator of ESX1-dependent virulence in Mycobacterium tuberculosis by affecting bacterial cell wall integrity. [PDF]

open access: yesPLoS Pathogens, 2010
Mycobacterium tuberculosis (Mtb) requires the ESX1 specialized protein secretion system for virulence, for triggering cytosolic immune surveillance pathways, and for priming an optimal CD8+ T cell response.
Alejandra Garces   +10 more
doaj   +1 more source

The genomics of disulfide bonding and protein stabilization in thermophiles. [PDF]

open access: yesPLoS Biology, 2005
Thermophilic organisms flourish in varied high-temperature environmental niches that are deadly to other organisms. Recently, genomic evidence has implicated a critical role for disulfide bonds in the structural stabilization of intracellular proteins ...
Morgan Beeby   +5 more
doaj   +2 more sources

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

open access: yes, 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   +16 more
core   +1 more source

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