Results 11 to 20 of about 1,788 (179)

ReDisulphID: A discovery platform for thiol redox sensors identifies a druggable site regulating p53 activation [PDF]

open access: yesRedox Biology
Thiol redox sensors in proteins are emerging as key therapeutic targets, as they govern fundamental signalling pathways and provide crucial sites for covalent drug development. A key mediator of their function is the presence of redox-active disulphides,
Pierre Coleman   +7 more
doaj   +2 more sources

Scientific Opinion on Flavouring Group Evaluation 08, Revision 5 (FGE.08Rev5): Aliphatic and alicyclic mono-, di-, tri-, and polysulphides with or without additional oxygenated functional groups from chemical groups 20 and 30 [PDF]

open access: yesEFSA Journal, 2012
<p>The CEF Panel of the European Food Safety Authority was requested to evaluate 80 flavouring substances in the Flavouring Group Evaluation 08, Revision 4, using the Procedure in Commission Regulation (EC) No 1565/2000.
EFSA Panel on Food Contact Materials, Enzymes, Flavourings and Processing Aids (CEF)
doaj   +1 more source

On the disulphide bonds of rhodopsins [PDF]

open access: yesBiochemical Journal, 1987
Carboxymethylation using 14C- or 3H-labelled iodoacetic acid has been used to identify the cysteine residues in bovine rhodopsin involved in the formation of the two intramolecular disulphide bridges. Iodo[2-14C]acetic acid was used to modify 5.8-5.9 residues of cysteine under non-reducing conditions.
S, Al-Saleh, M, Gore, M, Akhtar
openaire   +2 more sources

Secretion of the disulphide bond generating catalyst QSOX1 from pancreatic tumour cells into the extracellular matrix: Association with extracellular vesicles and matrix proteins

open access: yesJournal of Extracellular Biology, 2022
Quiescin sulfhydryl oxidase 1 (QSOX1) is a disulphide bond generating catalyst that is overexpressed in solid tumours. Expression of QSOX1 is linked to cancer cell invasion, tumour grade, and aberrant extracellular matrix (ECM) protein deposition.
Catherine S. Millar‐Haskell   +4 more
doaj   +1 more source

Characterisation of reduction state of cystine linkages on wool fibre surface under heterogeneous reaction conditions

open access: yesPolymer Testing, 2022
As a natural biomaterial with outstanding properties, keratin fibres hold promising potential in many application fields. The reduction of disulphides in keratin to the corresponding thiols plays a central role e.g.
Madita Buchacher   +2 more
doaj   +1 more source

Persian Asafoetida vs. Sagapenum: Challenges and Opportunities [PDF]

open access: yesResearch Journal of Pharmacognosy, 2020
Asafoetida and sagapenum as valuable Iranian oleo-gum-resins from Ferula spp. (F. assa-foetida, F. persica, F. foetida and F. alliacea) have received interest during the history for producing valuable perfumes and common spices or as pharmaceutical ...
Alireza Barzegar   +7 more
doaj   +1 more source

An alternative chemical redox method for the production of bispecific antibodies: implication in rapid detection of food borne pathogens. [PDF]

open access: yesPLoS ONE, 2014
Bi-functional antibodies with the ability to bind two unrelated epitopes have remarkable potential in diagnostic and bio-sensing applications. In the present study, bispecific antibodies that recognize human red blood cell (RBC) and the food borne ...
Mohammad Owais   +3 more
doaj   +1 more source

DisCoTune: versatile auxiliary plasmids for the production of disulphide‐containing proteins and peptides in the E. coli T7 system

open access: yesMicrobial Biotechnology, 2021
Summary Secreted proteins and peptides hold large potential both as therapeutics and as enzyme catalysts in biotechnology. The high stability of many secreted proteins helps maintain functional integrity in changing chemical environments and is a ...
Andreas B. Bertelsen   +10 more
doaj   +1 more source

Protein disulphide isomerase [PDF]

open access: yesCurrent Biology, 2003
What is it? Protein disulphide isomerase is an enzyme with two interrelated activities: as an oxidoreductase, it can catalyse the formation, reduction and isomerisation of disulphide bonds; and as a polypeptide binding protein, it can function as a molecular chaperone which assists the folding of polypeptides.
openaire   +2 more sources

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