Photo: Secreted Trx may participate in removing inhibitors of collagen-degrading metalloproteinases. PMID: 14503974 http://www.uniprot.org/citations/14503974
the molecular mechanisms underlying functional the TR1-Trx1 redox pair and structure determination of an active site of the ligand mini-stromelysin-1 TR-1 augmentation composed of TR (Trx reductase activities) the main function of TR1 here is to reduce Trx1 also validated as a ligand PMID; 23105116, have been characterized between ligand bound and free structures PMID; 20661909, for specific isolation of  C35S selenocysteine (SeCys)-containing protein http://www.rcsb.org/pdb/ligand/ligandsummary.do?hetId=TR1 shows the best docking position found, consists of one strand at position [PROline]76:A.side chain: from the four-stranded antiparallel beta sheet was with wild-type TrxA C32-35S located in the Thioredoxin_fold (PDB accession code 1XOB: PMID: 15987909) , TR1 as a single hybrid PDB (Cys32 and Cys35 for Trx1, and for TR1) pubmed/20536427 investigate the possible mechanism. {{{During this reduction, the thiol-disulfide oxidoreductase thioredoxin-1 (Trx1) linked thioredoxin reductase (TRR2) a working model suggesting that deregulation of the thioredoxin reductase TXNRD1 and|}}} its characteristic substrate thioredoxin (TR [1]), concomitant with diminution of their Trx reductase cellular contents is highly related to glutamate excitotoxicity PMID: 20620191; TR1: hStromelysin-1
Photo: (Fig.2) An ET (electron transfer) mechanism from NADPH and another enzyme thioredoxin reductase pubmed/17369362 the charged residue aspartate D60 (Fig.2) http://www.ncbi.nlm.nih.gov/pubmed/9369469/
The initial methionine) Met is located at the N-terminal - PMID: 11807942, 2684271.
Photo: An ET (electron transfer) mechanism from NADPH and another enzyme thioredoxin reductase pubmed/17369362 the charged residue aspartate D60 (Fig.2) pubmed/9369469/ plays a role in the degradation of proteins and in apoptotic processes induced by oxidative stress PMID: 16263712  to determine the effect of  zerumbone ZSD1 http://www.ncbi.nlm.nih.gov/pubmed/21527993
(from shampoo ginger; Name: Alpha-humulene) http://www.uniprot.org/uniprot/E3W9C4  on NADP-malate dehydrogenase, TRX dependent oxidoreductase, that NADPH does not contain. Monomeric Thioredoxin is present across phyla from humans to plants PMID: 20661909, 11012661 mediated in vivo by thioredoxin-catalyzed reduction and re-oxidation of cystine residues PubMed id: 10196131 (Fig.3-1CIV:PDB, NADP). Trx is able to activate vegetal NADP-malate dehydrogenase PMID: 3170595 (excluding the initial methionine) Met is located at the N-terminal - PMID: 11807942, 2684271.
http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl?pdbcode=1CIV
Photo: PubMed id: 10196131 (Fig.3-1CIV:PDB, NADP). Trx is able to activate vegetal NADP-malate dehydrogenase PMID: 3170595
Photo: Zerumbone-loaded nanostructured lipid carriers
Int J Nanomedicine. 2013;8:2769-81. doi: 10.2147/IJN.S45313. Epub 2013 Aug 2
PMID:23946649 [PubMed - indexed for MEDLINE]
PMCID:PMC3739459
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Mark Brenneman
Public
Secreted Trx may participate in removing inhibitors of collagen-degrading metalloproteinases. PMID: 14503974 http://www.uniprot.org/citations/14503974
the molecular mechanisms underlying functional the TR1-Trx1 redox pair and structure determination of an active site of the ligand mini-stromelysin-1 TR-1 augmentation composed of TR (Trx reductase activities) the main function of TR1 here is to reduce Trx1 also validated as a ligand PMID; 23105116, have been characterized between ligand bound and free structures PMID; 20661909, for specific isolation of  C35S selenocysteine (SeCys)-containing protein http://www.rcsb.org/pdb/ligand/ligandsummary.do?hetId=TR1 shows the best docking position found, consists of one strand at position [PROline]76:A.side chain: from the four-stranded antiparallel beta sheet was with wild-type TrxA C32-35S located in the Thioredoxin_fold (PDB accession code 1XOB: PMID: 15987909) , TR1 as a single hybrid PDB (Cys32 and Cys35 for Trx1, and for TR1) pubmed/20536427 investigate the possible mechanism. {{{During this reduction, the thiol-disulfide oxidoreductase thioredoxin-1 (Trx1) linked thioredoxin reductase (TRR2) a working model suggesting that deregulation of the thioredoxin reductase TXNRD1 and|}}} its characteristic substrate thioredoxin (TR [1]), concomitant with diminution of their Trx reductase cellular contents is highly related to glutamate excitotoxicity PMID: 20620191; TR1: hStromelysin-1