Results 41 to 50 of about 179,181 (346)
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. +3 more
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Microbial Cell Factories, 2010 Background The formation of native disulfide bonds is a complex and essential post-translational modification for many proteins. The large scale production of these proteins can be difficult and depends on targeting the protein to a compartment in which ...
Hatahet Feras +3 more
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Molecules, 2020 The polypeptide backbone of proteins is held together by two main types of covalent bonds: the peptide bonds that link the amino acid residues and the disulfide bonds that link pairs of cysteine amino acids. Disulfide bonds form as a protein folds in the
Philip J. Hogg
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, 2020 The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R +13 more
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Disulfide bond isomerization in prokaryotes
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2008 Proteins with multiple cysteine residues often require disulfide isomerization reactions before they attain their correct conformation. In prokaryotes this reaction is catalyzed mainly by DsbC, a protein that shares many similarities in structure and mechanism to the eukaryotic protein disulfide isomerase.
Gleiter, Stefan, Bardwell, James C.A.
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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. +3 more
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Electron Transport Chain Is Biochemically Linked to Pilus Assembly Required for Polymicrobial Interactions and Biofilm Formation in the Gram-Positive Actinobacterium Actinomyces oris. [PDF]
, 2017 The Gram-positive actinobacteria Actinomyces spp. are key colonizers in the development of oral biofilms due to the inherent ability of Actinomyces to adhere to receptor polysaccharides on the surface of oral streptococci and host cells.
Belkys C. Sanchez +5 more
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Single-molecule studies of disulfide bond reduction pathways used by human thioredoxin [PDF]
, 2013 Disulfide bond reduction pathways used by human thioredoxin (hTrx) are studied at the single molecule level using a recombinant protein (I27[subscript SS])[subscript 8].
Szoszkiewicz, Robert
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Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space [PDF]
, 2016 Mitochondria are organelles that play a central role in cellular metabolism, as they are responsible for processes such as iron/sulfur cluster biogenesis, respiration and apoptosis.
MacPherson, Lisa +2 more
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Bioengineering, 2021 Glucose oxidase (GOx) holds considerable advantages for various applications. Nevertheless, the thermal instability of the enzyme remains a grand challenge, impeding the success in applications outside the well-controlled laboratories, particularly in ...
Sirawit Ittisoponpisan +1 more
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