| Year |
Citation |
Score |
| 2018 |
Mettlen M, Chen PH, Srinivasan S, Danuser G, Schmid SL. Regulation of Clathrin-Mediated Endocytosis. Annual Review of Biochemistry. PMID 29661000 DOI: 10.1146/Annurev-Biochem-062917-012644 |
0.318 |
|
| 2016 |
Srinivasan S, Dharmarajan V, Reed DK, Griffin PR, Schmid SL. Identification and function of conformational dynamics in the multidomain GTPase dynamin. The Embo Journal. PMID 26783363 DOI: 10.15252/Embj.201593477 |
0.312 |
|
| 2015 |
Colón W, Aguilera JJ, Srinivasan S. Intrinsic Stability, Oligomerization, and Amyloidogenicity of HDL-Free Serum Amyloid A. Advances in Experimental Medicine and Biology. 855: 117-34. PMID 26149928 DOI: 10.1007/978-3-319-17344-3_5 |
0.706 |
|
| 2014 |
Srinivasan S, Mattila JP, Schmid SL. Intrapolypeptide interactions between the GTPase effector domain (GED) and the GTPase domain form the bundle signaling element in dynamin dimers. Biochemistry. 53: 5724-6. PMID 25171143 DOI: 10.1021/Bi500998S |
0.317 |
|
| 2014 |
Srinivasan S, Wang Y, Ye Z, Lopez M, Colon W. Molecular basis of the differences in fibrillogenicity between the pathogenic murine isoform serum amyloid A (SAA) 1.1 and its non pathogenic counterpart 2.2 F1000research. 5. DOI: 10.7490/F1000Research.1089930.1 |
0.673 |
|
| 2013 |
Patke S, Srinivasan S, Maheshwari R, Srivastava SK, Aguilera JJ, Colón W, Kane RS. Characterization of the oligomerization and aggregation of human Serum Amyloid A. Plos One. 8: e64974. PMID 23750222 DOI: 10.1371/Journal.Pone.0064974 |
0.493 |
|
| 2013 |
Srinivasan S, Patke S, Wang Y, Ye Z, Litt J, Srivastava SK, Lopez MM, Kurouski D, Lednev IK, Kane RS, Colón W. Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2. The Journal of Biological Chemistry. 288: 2744-55. PMID 23223242 DOI: 10.1074/Jbc.M112.394155 |
0.642 |
|
| 2012 |
Patke S, Maheshwari R, Litt J, Srinivasan S, Aguilera JJ, Colón W, Kane RS. Influence of the carboxy terminus of serum amyloid A on protein oligomerization, misfolding, and fibril formation. Biochemistry. 51: 3092-9. PMID 22448726 DOI: 10.1021/Bi201903S |
0.709 |
|
| 2011 |
Ye Z, Bayron Poueymiroy D, Aguilera JJ, Srinivasan S, Wang Y, Serpell LC, Colón W. Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature. Biochemistry. 50: 9184-91. PMID 21942925 DOI: 10.1021/Bi200856V |
0.72 |
|
| 2011 |
Wang Y, Srinivasan S, Ye Z, Javier Aguilera J, Lopez MM, Colón W. Serum amyloid A 2.2 refolds into a octameric oligomer that slowly converts to a more stable hexamer. Biochemical and Biophysical Research Communications. 407: 725-9. PMID 21439938 DOI: 10.1016/J.Bbrc.2011.03.090 |
0.703 |
|
| 2011 |
Muñiz VA, Srinivasan S, Boswell SA, Meinhold DW, Childs T, Osuna R, Colón W. The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS. Protein Science : a Publication of the Protein Society. 20: 302-12. PMID 21280122 DOI: 10.1002/Pro.561 |
0.573 |
|
| 2011 |
Vassall KA, Stubbs HR, Primmer HA, Tong MS, Sullivan SM, Sobering R, Srinivasan S, Briere LA, Dunn SD, Colón W, Meiering EM. Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS. Proceedings of the National Academy of Sciences of the United States of America. 108: 2210-5. PMID 21257910 DOI: 10.1073/Pnas.0913021108 |
0.675 |
|
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