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S-nitrosohemoglobin

Known as: S-Nitrosated Hemoglobin, S-Nitroso-Hemoglobin, S-nitrosylhemoglobin 
Hemoglobin that has a nitric oxide bound to the cysteine at position 93 in the beta-globin chain.(Circulation Research. 2004; 94: 851-855.)
National Institutes of Health

Papers overview

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Highly Cited
2014
Highly Cited
2014
Protein sulfenic acids are formed by the reaction of biologically relevant reactive oxygen species with protein thiols. Sulfenic… Expand
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Highly Cited
2008
Highly Cited
2008
Recent evidence suggests that the reaction of nitrite with deoxygenated hemoglobin and myoglobin contributes to the generation of… Expand
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Highly Cited
2007
Highly Cited
2007
RBCs distribute oxygen to tissues, but, paradoxically, blood transfusion does not always improve oxygen delivery and is… Expand
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Review
2006
Review
2006
The ability of oxyhemoglobin to inhibit nitric oxide (NO)-dependent activation of soluble guanylate cyclase and vasodilation… Expand
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Highly Cited
2006
Highly Cited
2006
S-Nitrosation of mitochondrial proteins has been proposed to contribute to the pathophysiological interactions of nitric oxide… Expand
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Highly Cited
2005
Highly Cited
2005
S-Nitrosation of protein sulfhydryl groups is an established response to oxidative/nitrosative stress. The transient nature and… Expand
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Highly Cited
2000
Highly Cited
2000
To determine the relative contributions of endothelial-derived nitric oxide (NO) vs. intravascular nitrogen oxide species in the… Expand
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Highly Cited
1999
Highly Cited
1999
S-Nitrosation of cysteine beta93 in hemoglobin (S-nitrosohemoglobin (SNO-Hb)) occurs in vivo, and transnitrosation reactions of… Expand
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Highly Cited
1999
Highly Cited
1999
The oxidation of nitric oxide (NO) to nitrate by oxyhemoglobin is a fundamental reaction that shapes our understanding of NO… Expand
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Highly Cited
1997
Highly Cited
1997
The binding of oxygen to heme irons in hemoglobin promotes the binding of nitric oxide (NO) to cysteinebeta93, forming S… Expand
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