Structural diversity in the type IV pili of multidrug-resistant Acinetobacter [PDF]
, 2016 Acinetobacter baumannii is a Gram-negative coccobacillus found primarily in hospital settings that has recently emerged as a source of hospital-acquired infections. A.
Feldman, Mario F +10 more
core +3 more sources
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 +2 more
core +1 more source
Thioredoxin-1 maintains mechanistic target of rapamycin (mTOR) function during oxidative stress in cardiomyocytes [PDF]
, 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
FEBS Letters, EarlyView.In this study, we found that human cervical‐derived adipocytes maintain intracellular iron level by regulating the expression of iron transport‐related proteins during adrenergic stimulation. Melanotransferrin is predicted to interact with transferrin receptor 1 based on in silico analysis.
Rahaf Alrifai +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 +5 more
doaj +1 more source
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 +4 more
doaj +1 more source
Controlled functional expression of the bacteriocins pediocin PA-1 and bactofencin A in Escherichia coli [PDF]
, 2017 peer-reviewedThe bacteriocins bactofencin A (class IId) and pediocin PA-1 (class IIa) are encoded by operons with a similarly clustered gene organization including a structural peptide, an immunity protein, an ABC transporter and accessory bacteriocin ...
Cotter, Paul D. +5 more
core +3 more sources
Structural insights into an engineered feruloyl esterase with improved MHET degrading properties
FEBS Letters, EarlyView.A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa +5 more
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
Oxidative protein folding in the mitochondrial intermembrane space [PDF]
, 2010 Disulfide bond formation is a crucial step for oxidative folding and necessary for the acquisition of a protein's native conformation. Introduction of disulfide bonds is catalyzed in specialized subcellular compartments and requires the coordinated ...
Anfinsen CB +4 more
core +1 more source