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Year Number of Results
1948 2
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1955 5
1956 4
1957 4
1958 3
1959 4
1960 2
1961 3
1962 3
1963 3
1965 3
1966 6
1967 4
1968 2
1969 1
1970 3
1971 8
1972 8
1973 5
1974 7
1975 19
1976 17
1977 12
1978 13
1979 8
1980 18
1981 8
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1983 23
1984 16
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1986 12
1987 18
1988 14
1989 16
1990 18
1991 22
1992 28
1993 20
1994 29
1995 35
1996 33
1997 21
1998 27
1999 23
2000 38
2001 24
2002 32
2003 32
2004 34
2005 22
2006 30
2007 30
2008 34
2009 30
2010 37
2011 27
2012 37
2013 15
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2015 21
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2017 30
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1,177 results

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Page 1
The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations.
Bordo D, Bork P. Bordo D, et al. EMBO Rep. 2002 Aug;3(8):741-6. doi: 10.1093/embo-reports/kvf150. EMBO Rep. 2002. PMID: 12151332 Free PMC article. Review.
Rhodanese domains are ubiquitous structural modules occurring in the three major evolutionary phyla. ...Recent investigations have shown that rhodanese domains are also structurally related to the catalytic subunit of Cdc25 phosphatase enzymes and that the two enzym …
Rhodanese domains are ubiquitous structural modules occurring in the three major evolutionary phyla. ...Recent investigations have sh …
Common themes and variations in the rhodanese superfamily.
Cipollone R, Ascenzi P, Visca P. Cipollone R, et al. IUBMB Life. 2007 Feb;59(2):51-9. doi: 10.1080/15216540701206859. IUBMB Life. 2007. PMID: 17454295 Free article. Review.
Although rhodanese-like proteins share evolutionary relationships, analysis of their sequences highlights that they are so heterogeneous to form the rhodanese superfamily. ...Given the highly variable organization of the rhodanese domain(s) and the context wh …
Although rhodanese-like proteins share evolutionary relationships, analysis of their sequences highlights that they are so heterogene …
Rhodanese as a thioredoxin oxidase.
Nandi DL, Horowitz PM, Westley J. Nandi DL, et al. Int J Biochem Cell Biol. 2000 Apr;32(4):465-73. doi: 10.1016/s1357-2725(99)00035-7. Int J Biochem Cell Biol. 2000. PMID: 10762072
A major catalytic difference between the two most common isoforms of bovine liver mitochondrial rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) has been observed. ...These activities are understood in terms of the established persulfide structu …
A major catalytic difference between the two most common isoforms of bovine liver mitochondrial rhodanese (thiosulfate: cyanid …
Roles of Sulfur Metabolism and Rhodanese in Detoxification and Anti-Oxidative Stress Functions in the Liver: Responses to Radiation Exposure.
Nakajima T. Nakajima T. Med Sci Monit. 2015 Jun 14;21:1721-5. doi: 10.12659/MSM.893234. Med Sci Monit. 2015. PMID: 26071878 Free PMC article. Review.
Radiation is a source of oxidative stress and is known to affect the liver and induce anti-oxidative responses. The detoxification enzyme rhodanese, which is also called thiosulfate sulfurtransferase (TST), has been demonstrated to be induced in the liver in …
Radiation is a source of oxidative stress and is known to affect the liver and induce anti-oxidative responses. The detoxification enzyme …
Rhodanese-Mediated sulfur transfer to succinate dehydrogenase.
Bonomi F, Pagani S, Cerletti P, Cannella C. Bonomi F, et al. Eur J Biochem. 1977 Jan 3;72(1):17-24. doi: 10.1111/j.1432-1033.1977.tb11219.x. Eur J Biochem. 1977. PMID: 318999 Free article.
Succinate dehydrogenase incorporates the sulfane sulfur of [35S]rhodanese and, in the presence of unlabelled rhodanese, also incorporates that of [35S]thiosulfate. Rhodanese releases most of its transferable sulfur and is re-loaded in the presence of …
Succinate dehydrogenase incorporates the sulfane sulfur of [35S]rhodanese and, in the presence of unlabelled rhodanese, also i …
Enzymatic detoxification of cyanide: clues from Pseudomonas aeruginosa Rhodanese.
Cipollone R, Ascenzi P, Tomao P, Imperi F, Visca P. Cipollone R, et al. J Mol Microbiol Biotechnol. 2008;15(2-3):199-211. doi: 10.1159/000121331. Epub 2008 Jul 28. J Mol Microbiol Biotechnol. 2008. PMID: 18685272 Review.
Enzymatic pathways involving hydrolytic, oxidative, reductive, and substitution/transfer reactions are implicated in detoxification of cyanide by bacteria and fungi. Amongst enzymes involved in transfer reactions, rhodanese catalyzes sulfane sulfur transfer from thiosul …
Enzymatic pathways involving hydrolytic, oxidative, reductive, and substitution/transfer reactions are implicated in detoxification of cyani …
Urm1: A Non-Canonical UBL.
Termathe M, Leidel SA. Termathe M, et al. Biomolecules. 2021 Jan 22;11(2):139. doi: 10.3390/biom11020139. Biomolecules. 2021. PMID: 33499055 Free PMC article. Review.
Uba4, the activating enzyme of Urm1, contains two domains: a classical E1-like domain (AD), which activates Urm1, and a rhodanese homology domain (RHD). This sulfurtransferase domain catalyzes the formation of a C-terminal thiocarboxylate on Urm1. ...
Uba4, the activating enzyme of Urm1, contains two domains: a classical E1-like domain (AD), which activates Urm1, and a rhodanese hom …
Rhodanese-thioredoxin system and allyl sulfur compounds.
Sabelli R, Iorio E, De Martino A, Podo F, Ricci A, Viticchiè G, Rotilio G, Paci M, Melino S. Sabelli R, et al. FEBS J. 2008 Aug;275(15):3884-99. doi: 10.1111/j.1742-4658.2008.06535.x. Epub 2008 Jul 4. FEBS J. 2008. PMID: 18616471 Free article.
Sodium 2-propenyl thiosulfate was also found to induce inhibition of the sulfurtransferase activity in tumor cells. Interestingly, in vitro experiments using fluorescence spectroscopy, kinetic studies and MS analysis showed that sodium 2-propenyl thiosulfate …
Sodium 2-propenyl thiosulfate was also found to induce inhibition of the sulfurtransferase activity in tumor cells. Interestin …
Rhodanese activity in different tissues of the ostrich.
Eskandarzade N, Aminlari M, Golami S, Tavana M. Eskandarzade N, et al. Br Poult Sci. 2012;53(2):270-3. doi: 10.1080/00071668.2012.682722. Br Poult Sci. 2012. PMID: 22646793
Rhodanese was present in all tissues, and the highest activity was observed in the kidney and liver. Other tissues which contained significant activities of rhodanese were the duodenum, pancreas, heart, caecum and rectum. 4. ...
Rhodanese was present in all tissues, and the highest activity was observed in the kidney and liver. Other tissues which contained si …
MdRDH1, a HSP67B2-like rhodanese homologue plays a positive role in maintaining redox balance in Musca domestica.
Tang T, Sun H, Li Y, Chen P, Liu F. Tang T, et al. Mol Immunol. 2019 Mar;107:115-122. doi: 10.1016/j.molimm.2019.01.016. Epub 2019 Feb 1. Mol Immunol. 2019. PMID: 30716562
Rhodanese homology domains (RHODs) are the structural modules of ubiquitous tertiary that occur in three major evolutionary phyla. ...The E. coli with MdRDH1 and the mutant MdRDH1(C135A) are transformed, with significant rhodanese activity of the recombinant protein …
Rhodanese homology domains (RHODs) are the structural modules of ubiquitous tertiary that occur in three major evolutionary phyla. .. …
1,177 results

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