Thiosulfate Sulfurtransferase

Known as: Cyanide Transsulphurase, Thiosulfate, thiosulfate thiotransferase, Thiosulfate Sulphurtransferase 
An enzyme that catalyzes the transfer of the planetary sulfur atom of thiosulfate ion to cyanide ion to form thiocyanate ion. EC 2.8.1.1.
National Institutes of Health

Topic mentions per year

Topic mentions per year

1948-2017
0102019482016

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2006
2006
Rhodanese or thiosulfate sulfurtransferase (TST) is a mitochondrial matrix enzyme that plays roles in cyanide detoxification, the… (More)
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Highly Cited
2001
Highly Cited
2001
Heat stress inhibits photosynthesis by reducing the activation of Rubisco by Rubisco activase. To determine if loss of activase… (More)
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Highly Cited
2000
Highly Cited
2000
The chaperonin GroEL binds nonnative substrate protein in the central cavity of an open ring through exposed hydrophobic residues… (More)
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Highly Cited
1996
Highly Cited
1996
The chaperonin GroEL is able to mediate protein folding in its central cavity. GroEL-bound dihydrofolate reductase assumes its… (More)
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1996
Highly Cited
1996
The effects of the human DnaJ homolog, Hsp40, on the ATPase and chaperone functions of the constitutively expressed Hsp70 homolog… (More)
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1995
1995
Protein disulfide-isomerase (PDI) in near stoichiometric concentrations promotes reactivation and prevents aggregation of… (More)
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1988
1988
Electrostatic interactions between pairs of atoms in proteins are calculated with a model based on the linearized Poisson… (More)
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1987
Highly Cited
1987
A new method for comparing and aligning protein sequences is described. This method, hydrophobic cluster analysis (HCA), relies… (More)
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1986
1986
Murine carrier erythrocytes, prepared by hypotonic dialysis, were employed in the encapsulation of several compounds including… (More)
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Highly Cited
1983
Highly Cited
1983
The degree of similarity in the three-dimensional structures of two proteins can be examined by comparing the patterns of… (More)
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