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ribonuclease B

Known as: RNase B 
 
National Institutes of Health

Papers overview

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2007
2007
An improved method for site-specific characterization of protein glycosylation has been devised using nonspecific digestion with… Expand
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Highly Cited
2006
Highly Cited
2006
The synthesis of proteins in the endoplasmic reticulum (ER) is limited by the rate of correct disulfide bond formation. This… Expand
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2003
2003
RNase A oligomerizes via the three-dimensional domain-swapping mechanism to form a variety of oligomers, including two dimers… Expand
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Highly Cited
2000
Highly Cited
2000
The endoplasmic reticulum (ER) contains a stringent quality control system that ensures the correct folding of newly synthesized… Expand
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Highly Cited
1998
Highly Cited
1998
The endoplasmic reticulum is the site of folding, disulfide bond formation, and N-glycosylation of secretory proteins. Correctly… Expand
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Highly Cited
1997
Highly Cited
1997
Calnexin is a membrane protein of the endoplasmic reticulum that associates transiently with newly synthesized N-linked… Expand
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1997
1997
The thermal stabilities of ribonuclease A (RNase A) and ribonuclease B (RNase B), which possess identical protein structures but… Expand
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Highly Cited
1994
Highly Cited
1994
The structures of ribonuclease B oligosaccharides have previously been shown to be high mannose type by methylation analyses and… Expand
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1993
1993
In an attempt to elucidate the role of carbohydrates on protein structure and dynamics in glycoproteins, ribonuclease B (RNase B… Expand
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1986
1986
Peptide N-glycosidase from Flavobacterium meningosepticum cleaves complex as well as neutral glycoproteins (Plummer, T.H., Jr… Expand
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