Wilfredo Colon, Ph.D. - Publications

Affiliations: 
Chemistry Rensselaer Polytechnic Institute, Troy, NY, United States 
Area:
Protein Folding/Misfolding
Website:
http://www.rpi.edu/dept/chem/chem_faculty/profiles/colon.html

54 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2017 Colon W, Church J, Sen J, Thibeault J, Trasatti HS, Xia K. Biological roles of protein kinetic stability. Biochemistry. PMID 29087706 DOI: 10.1021/acs.biochem.7b00942  0.8
2016 Xia K, Pittelli S, Church J, Colon W. Kinetic Stability of Proteins in Beans and Peas: Implications for Protein Digestibility, Seed Germination, and Plant Adaptation. Journal of Agricultural and Food Chemistry. PMID 27643830 DOI: 10.1021/acs.jafc.6b01965  0.8
2015 Broom A, Ma SM, Xia K, Rafalia H, Trainor K, Colón W, Gosavi S, Meiering EM. Designed protein reveals structural determinants of extreme kinetic stability. Proceedings of the National Academy of Sciences of the United States of America. PMID 26554002 DOI: 10.1073/pnas.1510748112  1
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  1
2014 Aguilera JJ, Zhang F, Beaudet JM, Linhardt RJ, Colón W. Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A. Biochimie. 104: 70-80. PMID 24878279 DOI: 10.1016/j.biochi.2014.05.007  1
2014 Rosenman DJ, Huang YM, Xia K, Fraser K, Jones VE, Lamberson CM, Van Roey P, Colón W, Bystroff C. Green-lighting green fluorescent protein: faster and more efficient folding by eliminating a cis-trans peptide isomerization event. Protein Science : a Publication of the Protein Society. 23: 400-10. PMID 24408076 DOI: 10.1002/pro.2421  1
2013 Zhang F, Aguilera J, Beaudet JM, Xie Q, Lerch TF, Davulcu O, Colón W, Chapman MS, Linhardt RJ. Characterization of interactions between heparin/glycosaminoglycan and adeno-associated virus. Biochemistry. 52: 6275-85. PMID 23952613 DOI: 10.1021/bi4008676  1
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  1
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  1
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  1
2012 Ramakrishnan V, Srinivasan SP, Salem SM, Matthews SJ, Colón W, Zaki M, Bystroff C. Geofold: topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability. Proteins. 80: 920-34. PMID 22189917 DOI: 10.1002/prot.23249  1
2012 Xia K, Zhang S, Bathrick B, Liu S, Garcia Y, Colón W. Quantifying the kinetic stability of hyperstable proteins via time-dependent SDS trapping. Biochemistry. 51: 100-7. PMID 22106876 DOI: 10.1021/bi201362z  1
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  1
2011 Sroga GE, Karim L, Colón W, Vashishth D. Biochemical characterization of major bone-matrix proteins using nanoscale-size bone samples and proteomics methodology. Molecular & Cellular Proteomics : McP. 10: M110.006718. PMID 21606484 DOI: 10.1074/mcp.M110.006718  1
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  1
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  1
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  1
2010 Xia K, Zhang S, Solina BA, Barquera B, Colón W. Do prokaryotes have more kinetically stable proteins than eukaryotic organisms? Biochemistry. 49: 7239-41. PMID 20677776 DOI: 10.1021/bi1010877  1
2010 Zhang S, Xia K, Chung WK, Cramer SM, Colón W. Identifying kinetically stable proteins with capillary electrophoresis. Protein Science : a Publication of the Protein Society. 19: 888-92. PMID 20091769 DOI: 10.1002/pro.336  1
2009 Shang W, Nuffer JH, Muñiz-Papandrea VA, Colón W, Siegel RW, Dordick JS. Cytochrome C on silica nanoparticles: influence of nanoparticle size on protein structure, stability, and activity. Small (Weinheim An Der Bergstrasse, Germany). 5: 470-6. PMID 19189325 DOI: 10.1002/smll.200800995  1
2008 Colón W, Chitnis P, Collins JP, Hicks J, Chan T, Tornow JS. Chemical biology at the US National Science Foundation. Nature Chemical Biology. 4: 511-4. PMID 18711373 DOI: 10.1038/nchembio0908-511  0.56
2008 Delgado JA, Shaffer M, Hu C, Lavado R, Cueto-Wong J, Joosse P, Sotomayor D, Colon W, Follett R, DelGrosso S, Li X, Rimski-Korsakov H. An index approach to assess nitrogen losses to the environment Ecological Engineering. 32: 108-120. DOI: 10.1016/j.ecoleng.2007.10.006  0.48
2007 Xia K, Manning M, Hesham H, Lin Q, Bystroff C, Colón W. Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE. Proceedings of the National Academy of Sciences of the United States of America. 104: 17329-34. PMID 17956990 DOI: 10.1073/pnas.0705417104  1
2007 Wang L, Colón W. Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A. Biochemistry. 46: 5562-9. PMID 17425332 DOI: 10.1021/bi602629y  0.76
2007 Moriarty DF, Fiorillo C, Miller C, Colón W. A truncated peptide model of the mutant P61A FIS forms a stable dimer. Biochimica Et Biophysica Acta. 1774: 78-85. PMID 17118726 DOI: 10.1016/j.bbapap.2006.09.012  1
2006 Meinhold D, Beach M, Shao Y, Osuna R, Colón W. The location of an engineered inter-subunit disulfide bond in factor for inversion stimulation (FIS) affects the denaturation pathway and cooperativity. Biochemistry. 45: 9767-77. PMID 16893178 DOI: 10.1021/bi060672n  1
2006 Feldman-Cohen LS, Shao Y, Meinhold D, Miller C, Colón W, Osuna R. Common and variable contributions of Fis residues to high-affinity binding at different DNA sequences. Journal of Bacteriology. 188: 2081-95. PMID 16513738 DOI: 10.1128/JB.188.6.2081-2095.2006  1
2006 Lynch SM, Colón W. Dominant role of copper in the kinetic stability of Cu/Zn superoxide dismutase. Biochemical and Biophysical Research Communications. 340: 457-61. PMID 16375856 DOI: 10.1016/j.bbrc.2005.12.024  1
2006 Delgado JA, Shaffer M, Hu C, Lavado RS, Wong JC, Joosse P, Li X, Rimski-Korsakov H, Follett R, Colon W, Sotomayor D. A decade of change in nutrient management: A new nitrogen index Journal of Soil and Water Conservation. 61: 62A-71A.  0.48
2005 Meinhold D, Boswell S, Colón W. P61A mutation in the factor for inversion stimulation results in a thermostable dimeric intermediate. Biochemistry. 44: 14715-24. PMID 16274219 DOI: 10.1021/bi050640k  1
2005 Wang L, Lashuel HA, Colón W. From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 12: 139-48. PMID 16194868 DOI: 10.1080/13506120500223084  1
2005 Wang L, Colón W. Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer. Protein Science : a Publication of the Protein Society. 14: 1811-7. PMID 15937280 DOI: 10.1110/ps.051387005  0.88
2004 Lynch SM, Boswell SA, Colón W. Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS. Biochemistry. 43: 16525-31. PMID 15610047 DOI: 10.1021/bi048831v  1
2004 Manning M, Colón W. Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure. Biochemistry. 43: 11248-54. PMID 15366934 DOI: 10.1021/bi0491898  1
2004 de Beus MD, Chung J, Colón W. Modification of cysteine 111 in Cu/Zn superoxide dismutase results in altered spectroscopic and biophysical properties. Protein Science : a Publication of the Protein Society. 13: 1347-55. PMID 15096637 DOI: 10.1110/ps.03576904  0.56
2004 Wang L, Colón W. The interaction between apolipoprotein serum amyloid A and high-density lipoprotein. Biochemical and Biophysical Research Communications. 317: 157-61. PMID 15047161 DOI: 10.1016/j.bbrc.2004.03.027  0.68
2004 Boswell S, Mathew J, Beach M, Osuna R, Colón W. Variable contributions of tyrosine residues to the structural and spectroscopic properties of the factor for inversion stimulation. Biochemistry. 43: 2964-77. PMID 15005633 DOI: 10.1021/bi035441k  1
2003 Chung J, Yang H, de Beus MD, Ryu CY, Cho K, Colón W. Cu/Zn superoxide dismutase can form pore-like structures. Biochemical and Biophysical Research Communications. 312: 873-6. PMID 14651952  0.56
2003 Chen CH, Battaglioli G, Martin DL, Hobart SA, Colón W. Distinctive interactions in the holoenzyme formation for two isoforms of glutamate decarboxylase. Biochimica Et Biophysica Acta. 1645: 63-71. PMID 12535612 DOI: 10.1016/S1570-9639(02)00522-8  1
2002 Wang L, Lashuel HA, Walz T, Colon W. Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel. Proceedings of the National Academy of Sciences of the United States of America. 99: 15947-52. PMID 12456883 DOI: 10.1073/pnas.252508399  1
2002 Hobart SA, Meinhold DW, Osuna R, Colón W. From two-state to three-state: the effect of the P61A mutation on the dynamics and stability of the factor for inversion stimulation results in an altered equilibrium denaturation mechanism. Biochemistry. 41: 13744-54. PMID 12427037 DOI: 10.1021/bi0265224  1
2002 Hobart SA, Ilin S, Moriarty DF, Osuna R, Colón W. Equilibrium denaturation studies of the Escherichia coli factor for inversion stimulation: implications for in vivo function. Protein Science : a Publication of the Protein Society. 11: 1671-80. PMID 12070319 DOI: 10.1110/ps.5050102  1
2000 Chen CH, Colón W, Myer YP, Martin DL. ATP's impact on the conformation and holoenzyme formation in relation to the regulation of brain glutamate decarboxylase. Archives of Biochemistry and Biophysics. 380: 285-93. PMID 10933883 DOI: 10.1006/abbi.2000.1931  0.56
1999 Colón W. Analysis of protein structure by solution optical spectroscopy. Methods in Enzymology. 309: 605-32. PMID 10507051  0.56
1997 Colón W, Wakem LP, Sherman F, Roder H. Identification of the predominant non-native histidine ligand in unfolded cytochrome c. Biochemistry. 36: 12535-41. PMID 9376358 DOI: 10.1021/bi971697c  0.56
1997 Kelly JW, Colon W, Lai Z, Lashuel HA, McCulloch J, McCutchen SL, Miroy GJ, Peterson SA. Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Advances in Protein Chemistry. 50: 161-81. PMID 9338081  1
1997 Roder H, Colón W. Kinetic role of early intermediates in protein folding. Current Opinion in Structural Biology. 7: 15-28. PMID 9032062 DOI: 10.1016/S0959-440X(97)80004-8  1
1996 Colón W, Roder H. Kinetic intermediates in the formation of the cytochrome c molten globule. Nature Structural Biology. 3: 1019-25. PMID 8946855 DOI: 10.1038/nsb1296-1019  1
1996 Colon W, Lai Z, McCutchen SL, Miroy GJ, Strang C, Kelly JW. FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation. Ciba Foundation Symposium. 199: 228-38; discussion 2. PMID 8915613  1
1996 Lai Z, Colón W, Kelly JW. The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid. Biochemistry. 35: 6470-82. PMID 8639594 DOI: 10.1021/bi952501g  1
1996 Colón W, Elöve GA, Wakem LP, Sherman F, Roder H. Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry. 35: 5538-49. PMID 8611545 DOI: 10.1021/bi960052u  0.56
1995 McCutchen SL, Lai Z, Miroy GJ, Kelly JW, Colón W. Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry. 34: 13527-36. PMID 7577941 DOI: 10.1021/bi00041a032  1
1993 McCutchen SL, Colon W, Kelly JW. Transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry. 32: 12119-27. PMID 8218290  1
1992 Colon W, Kelly JW. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry. 31: 8654-60. PMID 1390650  1
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