Connection
Ram Nagaraj to Protein Structure, Secondary
This is a "connection" page, showing publications Ram Nagaraj has written about Protein Structure, Secondary.
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Connection Strength |
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0.418 |
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Nahomi RB, Huang R, Nandi SK, Wang B, Padmanabha S, Santhoshkumar P, Filipek S, Biswas A, Nagaraj RH. Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human aB-crystallin. Biochemistry. 2013 Nov 12; 52(45):8126-38.
Score: 0.093
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Nagaraj RH, Panda AK, Shanthakumar S, Santhoshkumar P, Pasupuleti N, Wang B, Biswas A. Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics. PLoS One. 2012; 7(1):e30257.
Score: 0.083
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Nagaraj RH, Nahomi RB, Shanthakumar S, Linetsky M, Padmanabha S, Pasupuleti N, Wang B, Santhoshkumar P, Panda AK, Biswas A. Acetylation of aA-crystallin in the human lens: effects on structure and chaperone function. Biochim Biophys Acta. 2012 Feb; 1822(2):120-9.
Score: 0.082
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Biswas A, Goshe J, Miller A, Santhoshkumar P, Luckey C, Bhat MB, Nagaraj RH. Paradoxical effects of substitution and deletion mutation of Arg56 on the structure and chaperone function of human alphaB-crystallin. Biochemistry. 2007 Feb 06; 46(5):1117-27.
Score: 0.059
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Biswas A, Miller A, Oya-Ito T, Santhoshkumar P, Bhat M, Nagaraj RH. Effect of site-directed mutagenesis of methylglyoxal-modifiable arginine residues on the structure and chaperone function of human alphaA-crystallin. Biochemistry. 2006 Apr 11; 45(14):4569-77.
Score: 0.055
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Nagaraj RH, Oya-Ito T, Padayatti PS, Kumar R, Mehta S, West K, Levison B, Sun J, Crabb JW, Padival AK. Enhancement of chaperone function of alpha-crystallin by methylglyoxal modification. Biochemistry. 2003 Sep 16; 42(36):10746-55.
Score: 0.046
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Connection Strength
The connection strength for concepts is the sum of the scores for each matching publication.
Publication scores are based on many factors, including how long ago they were written and whether the person is a first or senior author.
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