| Year |
Citation |
Score |
| 2023 |
Gouveia M, Schmidt C, Basilio PG, Aveiro SS, Domingues P, Xia K, Colón W, Vitorino R, Ferreira R, Santos M, Vieira SI, Ribeiro F. Exercise training decreases the load and changes the content of circulating SDS-resistant protein aggregates in patients with heart failure with reduced ejection fraction. Molecular and Cellular Biochemistry. PMID 37902886 DOI: 10.1007/s11010-023-04884-z |
0.449 |
|
| 2022 |
Gouveia M, Schmidt C, Teixeira M, Lopes M, Aveiro SS, Domingues P, Xia K, Colón W, Vitorino R, Ferreira R, Santos M, Vieira S, Ribeiro F. Characterization of Plasma SDS-Protein Aggregation Profile of Patients with Heart Failure with Preserved Ejection Fraction. Journal of Cardiovascular Translational Research. PMID 36271180 DOI: 10.1007/s12265-022-10334-w |
0.473 |
|
| 2020 |
Colon W, Rugaber EG, Xia K. Proteomics Analyses of Kinetic Stability: from Molecular to Organism Longevity Biophysical Journal. 118: 181a. DOI: 10.1016/J.Bpj.2019.11.1104 |
0.533 |
|
| 2019 |
Thibeault J, Patrick J, Martin A, Ortiz-Perez B, Hill S, Zhang S, Xia K, Colón W. Sarkosyl: A milder detergent than SDS for identifying proteins with moderately high hyperstability using gel electrophoresis. Analytical Biochemistry. PMID 30779907 DOI: 10.1016/J.Ab.2019.02.008 |
0.801 |
|
| 2019 |
Thibeault J, Barquera B, Colón W. Hyperstable Proteins in the Gut Microbiota: An Examination of the Bacterium Bacteroides fragilis Biophysical Journal. 116: 321a. DOI: 10.1016/J.Bpj.2018.11.1744 |
0.35 |
|
| 2018 |
Yu Y, Zhang F, Colón W, Linhardt RJ, Xia K. Glycosaminoglycans in human cerebrospinal fluid determined by LC-MS/MS MRM. Analytical Biochemistry. PMID 30571946 DOI: 10.1016/J.Ab.2018.12.013 |
0.526 |
|
| 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 |
0.639 |
|
| 2017 |
Thibeault J, Church J, Ortiz-Perez B, Addo S, Hill S, Khalil A, Young M, Xia K, Colón W. Analyzing bean extracts using time-dependent SDS trapping to quantify the kinetic stability of phaseolin proteins. Biochemical and Biophysical Research Communications. PMID 28774556 DOI: 10.1016/J.Bbrc.2017.07.166 |
0.606 |
|
| 2017 |
Gouveia M, Xia K, Colón W, Vieira SI, Ribeiro F. Protein aggregation, cardiovascular diseases, and exercise training: where do we stand? Ageing Research Reviews. PMID 28757291 DOI: 10.1016/J.Arr.2017.07.005 |
0.516 |
|
| 2017 |
Colón W, Xia K, Church J, Sen J, Thibeault J, Trasatti HS. Biological Roles of Protein Hyperstability: Implications for Biotechnology Biophysical Journal. 112: 56a. DOI: 10.1016/J.Bpj.2016.11.340 |
0.642 |
|
| 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 |
0.608 |
|
| 2016 |
Xia K, Trasatti H, Wymer JP, Colón W. Increased levels of hyper-stable protein aggregates in plasma of older adults. Age (Dordrecht, Netherlands). 38: 56. PMID 27179971 DOI: 10.1007/S11357-016-9919-9 |
0.562 |
|
| 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 |
0.615 |
|
| 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 |
0.615 |
|
| 2015 |
Xia K, Wilcox J, Kobovitch K, Ortiz B, Khalil A, Colon W. Proteomics-Level Identification of Degradation-Resistant Proteins Provide Insight about their Potential Roles in Organismal Adaptation to Stress Biophysical Journal. 108: 501a. DOI: 10.1016/J.Bpj.2014.11.2745 |
0.604 |
|
| 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 |
0.492 |
|
| 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 |
0.634 |
|
| 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 |
0.421 |
|
| 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 |
0.625 |
|
| 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 |
0.808 |
|
| 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 |
0.708 |
|
| 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 |
0.714 |
|
| 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 |
0.787 |
|
| 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 |
0.614 |
|
| 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 |
0.788 |
|
| 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 |
0.81 |
|
| 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 |
0.716 |
|
| 2008 |
Page-McCaw PS, Valakh V, Mann K, Ye Z, Colon W. Serum Amyloid A is required for hedgehog signaling in zebrafish morphogenesis Developmental Biology. 319: 517. DOI: 10.1016/J.Ydbio.2008.05.181 |
0.392 |
|
| 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 |
0.754 |
|
| 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 |
0.536 |
|
| 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 |
0.795 |
|
| 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 |
0.803 |
|
| 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 |
0.76 |
|
| 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 |
0.59 |
|
| 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 |
0.802 |
|
| 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 |
0.657 |
|
| 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 |
0.553 |
|
| 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 |
0.771 |
|
| 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 |
0.704 |
|
| 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 |
0.736 |
|
| 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 |
0.464 |
|
| 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 |
0.728 |
|
| 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 DOI: 10.1016/J.Bbrc.2003.11.008 |
0.739 |
|
| 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 |
0.312 |
|
| 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 |
0.648 |
|
| 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 |
0.809 |
|
| 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 |
0.786 |
|
| 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 |
0.329 |
|
| 1999 |
Colón W. Analysis of protein structure by solution optical spectroscopy. Methods in Enzymology. 309: 605-32. PMID 10507051 DOI: 10.1016/S0076-6879(99)09041-2 |
0.436 |
|
| 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 DOI: 10.1016/S0065-3233(08)60321-6 |
0.694 |
|
| 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 |
0.471 |
|
| 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 |
0.425 |
|
| 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 |
0.522 |
|
| 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 |
0.559 |
|
| 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 |
0.37 |
|
| 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 |
0.558 |
|
| 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 DOI: 10.1021/Bi00096A024 |
0.599 |
|
| 1992 |
Colon W, Kelly JW. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry. 31: 8654-60. PMID 1390650 DOI: 10.1021/Bi00151A036 |
0.549 |
|
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