Publications
60. Colón, W., Church, J., Sen, J., Thibeault, J., Trasatti, H., and Xia, K. (2017) Biological Roles of Protein Kinetic Stability. Biochemistry, 56, 6179-6186.
59. Gouveia, M., Xia, K., Colón, W., Vieira, S., and Ribeiro, F. (2017) Protein aggregation, cardiovascular diseases, and exercise training: Where do we stand? Ageing Res Rev., 40,1-10.
58. Thibeault, J., Church, J., Ortiz-Perez, B., Addo, S., Hill, S., Khalil, A., Young, M., Xia, K., and Colón, W. (2017) Analyzing bean extracts using time-dependent SDS trapping to quantify the kinetic stability of phaseolin proteins. Biochem Biophys Res Commun., 491, 994-999.
57. Xia, K., Pittelli, S., Church, J., and Colón, W. (2016) Kinetic Stability of Proteins in Beans and Peas: Implications for Protein Digestibility, Seed Germination, and Plant Adaptation. J. Agric. Food Chem., 64, 7649-7657.
56. Xia, K., Trasatti, H., Wymer, J.P., and Colón, W. (2016) Increased levels of hyper-stable protein aggregates in plasma of older adults. AGE, 38.
55. Broom, A., Ma, S.M., Xia, K., Rafalia, H., Trainor, K., Colón, W., Gosavi, S., and Meiering, E.M. (2015) Designed protein reveals structural determinants of extreme kinetic stability. Proc. Natl. Acad. Sci., 112, 14605-14610.
54. Colón, W., Aguilera, J.J., and Srinivasan, S. (2015) Intrinsic Stability, Oligomerization, and Amyloidogenicity of HDL-Free Serum Amyloid A. In: Gursky O. (eds) Lipids in Protein Misfolding. Advances in Experimental Medicine and Biology, vol 855. Springer, Cham.
53. Aguilera, J., Zhang, F., Beaudet, J.M., Linhardt, R.J. and Colón, W. (2014) Divergent effect of glycosaminoglycans on the in vitro aggregation of Serum Amyloid A. Biochimie, 104, 70-80.
52. Rosenman D.J., Huang Y.M., Xia K., Fraser K., Jones V.E., Lamberson C.M., Van Roey P., Colón, W., Bystroff C. (2014) Green-lighting green fluorescent protein: faster and more efficient folding by eliminating a cis-trans peptide isomerization event. Prot. Science 23, 400-410.
51. Zhang, F., Aguilera, J., Beaudet, J.M., Xie, Q., Lerch, T.F., Davulcu, O., Colón, W., Chapman, M.S., and Linhardt, R.J. (2013) Characterization of Interactions between Heparin/Glycosaminoglycan and Adeno-associated Virus. Biochemistry, 52, 6275–6285.
50. Patke, S., Srinivasan, S., Maheshwari, R., Srivastava, S.K., Aguilera, J. J., Colón, W.*, and Kane, R.S..* (2013) Characterization of the Oligomerization and Aggregation of Human Serum Amyloid A. PLoS One, 8:e64974. doi: 10.1371.
49. Srinivasan, S., Patke, S., Wang, Y., Ye, Z., Litt, J., S.K. Srivastava, Lopez, M.M., Kurouski, D., Lednev, I.K., Kane, R.S. * and Colón, W. * (2013) Pathogenic SAA1.1 shows a longer oligomer-rich fibrillation lag phase contrary to the non-pathogenic SAA2.2. J. Biol. Chem.,288, 2744-2755.
48. Patke, S., Maheshwari, R., Litt, J., Srinivasan, S., Aguilera, J.J., Colón, W. * and Kane, R.S. * (2012) Influence of the Carboxy-Terminus of Serum Amyloid A on Protein Oligomerization, Misfolding, and Aggregation. Biochemistry, 51, 3092−3099.
47. Ramakrishnan V., Srinivasan, S., Salem, S.M., Matthews, S. J., Colón, W, Zaki M.J. and Bystroff C. (2012) GeoFold: Topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability. Proteins, 80, 920-934.
46. Xia, K., Manning, M., Zhang, S. and Colón, W. (2012) Proteomics Analysis of Kinetically Stable Proteins, Integrative Proteomics, Hon-Chiu Eastwood Leung, Subject editors: Tsz-Kwong Man and Ricardo J. Flores (Ed.), ISBN: 978-953-51-0070-6, InTech.
45. Xia, K, Zhang, S., Bathrick, B., Liu, S., Garcia, Y., and Colon, W. (2012) Quantifying the kinetic stability of hyperstable proteins via time-dependent SDS-trapping. Biochemistry, 51, 100-107.
44. Ye, Z, Bayron, D., Aguilera, J.J., Srinivasan, S., Wang, Y., Serpell, L.C and Colón, W. (2011) Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature. Biochemistry, 50, 9184−9191.
43. Sroga, G.E., Karim, L., Colón, W. and Vashishth, D. (2011) Biochemical characterization of major bone-matrix proteins using nanoscale-size bone samples and proteomics methodology. Molec. Cell. Proteom. 10, M110.006718.
42. Wang, Y., Srinivasan, S., Ye, Z., Aguilera, J.J., Lopez, M. and Colón, W. (2011) Serum amyloid A 2.2 refolds into a octameric oligomer that slowly converts to a more stable hexamer. Biochem. Biophys. Res. Commun. 407, 725-729.
41. Vassall, K.A, Stubbs, H.A., Primmer, H.A., Tong, M.S., Sullivan, S.M,, Sobering, R., Srinivasan, S., Briere, L.K., Dunn, S.D., Colòn, W., and Meiering, E.M. (2011) Decreased stability and increased formation of soluble aggregates by immature SOD1 do not account for disease severity in ALS. Proc. Natl. Acad. Sci., 108, 2210-2215.
40. Muñiz, V.A., Srinivasan, S. Boswell, S.A., Meinhold, D.W., Childs, T., Osuna, R. and Colón, W. (2011) The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS. Prot. Science, 20, 302-312.
39. Xia, K., Zhang, S, Solina, B., Barquera, B., and Colón, W. (2010) Do Prokaryotes have more hyperstable proteins than eukaryotic organisms? Biochemistry, 49, 7239-7241.
38. Zhang, S., Xia, K., Chung, W., Cramer, S.M., and Colón, W. (2010) Identifying kinetically stable proteins with capillary zone electrophoresis. Prot. Science, 19, 888-892.
37. Shang, W., Nuffer, J.H., Muñiz-Papandrea, V.A., Colón, W., Siegel, R.W., and Dordick, J.S. (2009) Cytochrome c on silica nanoparticles: Influence of nanoparticle size on protein structure, stability, and activity. Small, 4, 470-476.
36. Colón, W., Chitnis, P., Collins, J.P., Hicks, J., Chan, T. and Tornow, J.S. (2008) Chemical Biology at the US National Science Foundation. Nat. Chem. Biol. 4, 511-514.
35. Xia, K, Manning, M., Hesham, H., Bystroff, C., Lin, Q. and Colón, W. (2007) Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS-PAGE. Proc. Natl. Acad. Sci., 104, 17329-17334.
34. Wang L. and Colón, W. (2007) Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A. Biochemistry, 46, 5562-5569.
33. Moriarty, D.F, Fiorillo, C., Miller, C, and Colón, W. (2007) A truncated peptide model of the mutant P61A FIS forms a stable dimer. Biochim. Biophys. Acta, 1774, 78-85.
32. Meinhold, D., Beach, M., Shao, Y., Osuna, R., and Colón W. (2006) The location of an engineered inter-subunit disulfide bond in FIS affects the denaturation pathway and cooperativity. Biochemistry, 46, 9767-9777.
31. Feldman-Cohen, L. S., Shao, Y., Meinhold, D., Miller, C., Colón, W. and Osuna, R. (2006) Common and variable contributions by Fis residues on high-affinity binding at different DNA sequences. J. Bacteriol., 188, 2081-2095.
30. Lynch, S. M. and Colón, W. (2006) Dominant role of copper in the kinetic stability of Cu/Zn superoxide dismutase. Biochem. Biophys. Res. Commun., 340, 457-461.
29. Meinhold, D, Boswell, S., and Colón, W. (2005) P61A mutation in the factor for inversion stimulation results in a thermostable dimeric intermediate. Biochemistry, 44, 14715-14724.
28. Wang, L., Lashuel, H.A, Walz, T. and Colón, W. (2005) From Hexamer to amyloid: The mechanism of serum amyloid A fibril formation. Amyloid, 12, 139-148.
27. Moriarty, D.F. and Colón, W. (2005) Structural intermediates of globular proteins as precursors to amyloid formation in “Amyloid proteins: The beta pleated sheet conformation and disease”. Chapter 12, pages 275-300, Editors Jean Sipe, VCH-Wiley.
26. Wang L. and Colón, W. (2005) Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer. Prot. Science, 14, 1811-1817.
25. Lynch, S.M., Boswell, S.A. and Colón, W. (2004) Kinetic stability of SOD is dependent on its metal ligands: Implications for ALS. Biochemistry, 43, 16525-16531.
24. Manning, M and Colón, W. (2004) Structural basis of protein kinetic stability: Resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias towards -sheet structure. Biochemistry, 43, 11248-11254.
23. Boswell, S. A., Mathew, J., Beach, M., Osuna R., and Colón W. (2004) Variable contributions of tyrosine residues to the structural and spectroscopic properties of the factor for inversion stimulation. Biochemistry, 43, 2964-2977.
22. Wang L. and Colón, W. (2004) The interaction between apolipoprotein serum amyloid A and high-density lipoprotein. Biochem. Biophys. Res. Commun., 317, 157-161.
21. De Beus, M. D., Chung, J., and Colón, W. (2004) Modification of cysteine 111 in Cu/Zn superoxide dismutase results in altered spectroscopic and biophysical properties. Prot. Science, 13, 1347-1355.
20. Chung, J., Yang, H., deBeus, M. D., Ryu, C. Y., Cho, H., and Colón, W. (2003) Cu/Zn superoxide dismutase can form pore-like structures. Biochem. Biophys. Res. Commun., 312, 873-876.
19. Cheng, C-H., Battaglioli, G., Martin, D.L., Hobart, S. A. and Colón, W. (2003) Distinctive interactions in the holoenzyme formation for two isoforms of glutamate decarboxylase. Biochim. Biophys. Acta, 1645, 63-71.
18. Wang, L., Lashuel, H.A, Walz, T. and Colón, W. (2002) Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel. Proc. Natl. Acad. Sci., 99, 15947-15952.
17. Hobart, S. A., Meinhold, D., Moriarty D. F., Osuna R., and Colón W. (2002) From two-state to three-state: Effect of P61A mutation on the dynamics and stability of the factor for inversion stimulation results in an altered equilibrium denaturation mechanism. Biochemistry, 41, 13744-13754.
16. Hobart, S. A., Ilin S., Moriarty D. F., Osuna R., and Colón W. (2002) Equilibrium denaturation studies of the E. coli factor for inversion stimulation: Implications for in vivo function. Prot. Science, 11, 1671-1680.
15. Colón, W. Solving the protein folding problem. (2001) Chemical & Engineering News, page 225 (March 26).
14. Cheng, C-H, Colón, W., Myer, Y.P. and Martin, D.L. (2000) ATP’s impact on the conformation and holoenzyme formation in relation to the regulation of brain glutamate decarboxylase. Arch. Biochem. Biophys. 380, 285-293.
13. Colón, W. (1999) Analysis of protein structure by solution spectroscopy. Methods Enzymol. 310, 316-340.
12. Dolggikh, D. A., Latypov, R. F., Abdullaev, A. K., Colón, W., Roder, H., and Kirpichnikov, M. P. (1998) Expression of mutant horse cytochrome c genes in Escherichia coli. Bioorg. Khim. 24, 756-759.
11. Kelly, J.W., Colón, W., Lai, Z., Lashuel, H. A., McCulloch, J., McCutchen, S. L., Miroy, G. J. and Peterson, S. A. (1997) Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Adv. Prot. Chem. 50, 161-181.
10. Colón, W., Wakem, P., Sherman, F. and Roder, H. (1997) Identification of the predominant non-native histidine ligand of unfolded cytochrome c. Biochemistry, 36, 12535-12541.
9. Roder, H. and Colón, W. (1997) Kinetic role of early intermediates in protein folding. Curr. Opinion Struct. Biol., 7, 15-28.
8. Colón, W. and Roder, H. (1996) Kinetic intermediates in the formation of the cytochrome c molten globule. Nat. Struct. Biol., 3, 1019-1025.
7. Colón, W., Elöve, G. E., Waken, L. P., Sherman, F. and Roder, H. (1996) Side chain packing of the n- and c- terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry, 35, 5538-5549.
6. Colón, W., Lai, Z., McCutchen, S. L., Miroy, G. J., Strang, C. and Kelly, J.W. (1996) FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation. Ciba Found Symp. 199, 228-242.
5. Lai, Z., Colón, W. and Kelly, J.W. (1996) The acid–mediated denaturation pathway of transthyretin yields an intermediate which can self-assemble into amyloid. Biochemistry, 35, 6470-6482.
4. McCutchen, S. L., Lai, Z., Miroy, G. J., Kelly, J.W. and Colón, W. (1995) Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry, 34, 13527-13536.
3. McCutchen, S. L., Colón, W. and Kelly, J.W. (1993) The transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry, 32, 12119-12127.
2. Colón, W. and Kelly, J.W. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry, 31, 8654-8660 (1992).
1. Colón, W. and Kelly, J.W. (1991) Transthyretin Acid Induced Denaturation is Required for Amyloid Fibril Formation In Vitro. in Applications of Enzyme Biotechnology , pp 99-108, Editors, Jeffery W. Kelly and Thomas O. Baldwin (Plenum, New York).
Issued Patents
1. Patent Number 7,217,348 B2 (May 15, 2007) Methods of identifying kinetically stable proteins. Wilfredo Colón and Marta Manning, Rensselaer Polytechnic Institute.
2. Patent Number 7,393,443 B2 (July 1, 2008) Methods of identifying kinetically stable proteins. Wilfredo Colón and Marta Manning, Rensselaer Polytechnic Institute.
59. Gouveia, M., Xia, K., Colón, W., Vieira, S., and Ribeiro, F. (2017) Protein aggregation, cardiovascular diseases, and exercise training: Where do we stand? Ageing Res Rev., 40,1-10.
58. Thibeault, J., Church, J., Ortiz-Perez, B., Addo, S., Hill, S., Khalil, A., Young, M., Xia, K., and Colón, W. (2017) Analyzing bean extracts using time-dependent SDS trapping to quantify the kinetic stability of phaseolin proteins. Biochem Biophys Res Commun., 491, 994-999.
57. Xia, K., Pittelli, S., Church, J., and Colón, W. (2016) Kinetic Stability of Proteins in Beans and Peas: Implications for Protein Digestibility, Seed Germination, and Plant Adaptation. J. Agric. Food Chem., 64, 7649-7657.
56. Xia, K., Trasatti, H., Wymer, J.P., and Colón, W. (2016) Increased levels of hyper-stable protein aggregates in plasma of older adults. AGE, 38.
55. Broom, A., Ma, S.M., Xia, K., Rafalia, H., Trainor, K., Colón, W., Gosavi, S., and Meiering, E.M. (2015) Designed protein reveals structural determinants of extreme kinetic stability. Proc. Natl. Acad. Sci., 112, 14605-14610.
54. Colón, W., Aguilera, J.J., and Srinivasan, S. (2015) Intrinsic Stability, Oligomerization, and Amyloidogenicity of HDL-Free Serum Amyloid A. In: Gursky O. (eds) Lipids in Protein Misfolding. Advances in Experimental Medicine and Biology, vol 855. Springer, Cham.
53. Aguilera, J., Zhang, F., Beaudet, J.M., Linhardt, R.J. and Colón, W. (2014) Divergent effect of glycosaminoglycans on the in vitro aggregation of Serum Amyloid A. Biochimie, 104, 70-80.
52. Rosenman D.J., Huang Y.M., Xia K., Fraser K., Jones V.E., Lamberson C.M., Van Roey P., Colón, W., Bystroff C. (2014) Green-lighting green fluorescent protein: faster and more efficient folding by eliminating a cis-trans peptide isomerization event. Prot. Science 23, 400-410.
51. Zhang, F., Aguilera, J., Beaudet, J.M., Xie, Q., Lerch, T.F., Davulcu, O., Colón, W., Chapman, M.S., and Linhardt, R.J. (2013) Characterization of Interactions between Heparin/Glycosaminoglycan and Adeno-associated Virus. Biochemistry, 52, 6275–6285.
50. Patke, S., Srinivasan, S., Maheshwari, R., Srivastava, S.K., Aguilera, J. J., Colón, W.*, and Kane, R.S..* (2013) Characterization of the Oligomerization and Aggregation of Human Serum Amyloid A. PLoS One, 8:e64974. doi: 10.1371.
49. Srinivasan, S., Patke, S., Wang, Y., Ye, Z., Litt, J., S.K. Srivastava, Lopez, M.M., Kurouski, D., Lednev, I.K., Kane, R.S. * and Colón, W. * (2013) Pathogenic SAA1.1 shows a longer oligomer-rich fibrillation lag phase contrary to the non-pathogenic SAA2.2. J. Biol. Chem.,288, 2744-2755.
48. Patke, S., Maheshwari, R., Litt, J., Srinivasan, S., Aguilera, J.J., Colón, W. * and Kane, R.S. * (2012) Influence of the Carboxy-Terminus of Serum Amyloid A on Protein Oligomerization, Misfolding, and Aggregation. Biochemistry, 51, 3092−3099.
47. Ramakrishnan V., Srinivasan, S., Salem, S.M., Matthews, S. J., Colón, W, Zaki M.J. and Bystroff C. (2012) GeoFold: Topology-based protein unfolding pathways capture the effects of engineered disulfides on kinetic stability. Proteins, 80, 920-934.
46. Xia, K., Manning, M., Zhang, S. and Colón, W. (2012) Proteomics Analysis of Kinetically Stable Proteins, Integrative Proteomics, Hon-Chiu Eastwood Leung, Subject editors: Tsz-Kwong Man and Ricardo J. Flores (Ed.), ISBN: 978-953-51-0070-6, InTech.
45. Xia, K, Zhang, S., Bathrick, B., Liu, S., Garcia, Y., and Colon, W. (2012) Quantifying the kinetic stability of hyperstable proteins via time-dependent SDS-trapping. Biochemistry, 51, 100-107.
44. Ye, Z, Bayron, D., Aguilera, J.J., Srinivasan, S., Wang, Y., Serpell, L.C and Colón, W. (2011) Inflammation protein SAA2.2 spontaneously forms marginally stable amyloid fibrils at physiological temperature. Biochemistry, 50, 9184−9191.
43. Sroga, G.E., Karim, L., Colón, W. and Vashishth, D. (2011) Biochemical characterization of major bone-matrix proteins using nanoscale-size bone samples and proteomics methodology. Molec. Cell. Proteom. 10, M110.006718.
42. Wang, Y., Srinivasan, S., Ye, Z., Aguilera, J.J., Lopez, M. and Colón, W. (2011) Serum amyloid A 2.2 refolds into a octameric oligomer that slowly converts to a more stable hexamer. Biochem. Biophys. Res. Commun. 407, 725-729.
41. Vassall, K.A, Stubbs, H.A., Primmer, H.A., Tong, M.S., Sullivan, S.M,, Sobering, R., Srinivasan, S., Briere, L.K., Dunn, S.D., Colòn, W., and Meiering, E.M. (2011) Decreased stability and increased formation of soluble aggregates by immature SOD1 do not account for disease severity in ALS. Proc. Natl. Acad. Sci., 108, 2210-2215.
40. Muñiz, V.A., Srinivasan, S. Boswell, S.A., Meinhold, D.W., Childs, T., Osuna, R. and Colón, W. (2011) The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS. Prot. Science, 20, 302-312.
39. Xia, K., Zhang, S, Solina, B., Barquera, B., and Colón, W. (2010) Do Prokaryotes have more hyperstable proteins than eukaryotic organisms? Biochemistry, 49, 7239-7241.
38. Zhang, S., Xia, K., Chung, W., Cramer, S.M., and Colón, W. (2010) Identifying kinetically stable proteins with capillary zone electrophoresis. Prot. Science, 19, 888-892.
37. Shang, W., Nuffer, J.H., Muñiz-Papandrea, V.A., Colón, W., Siegel, R.W., and Dordick, J.S. (2009) Cytochrome c on silica nanoparticles: Influence of nanoparticle size on protein structure, stability, and activity. Small, 4, 470-476.
36. Colón, W., Chitnis, P., Collins, J.P., Hicks, J., Chan, T. and Tornow, J.S. (2008) Chemical Biology at the US National Science Foundation. Nat. Chem. Biol. 4, 511-514.
35. Xia, K, Manning, M., Hesham, H., Bystroff, C., Lin, Q. and Colón, W. (2007) Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS-PAGE. Proc. Natl. Acad. Sci., 104, 17329-17334.
34. Wang L. and Colón, W. (2007) Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A. Biochemistry, 46, 5562-5569.
33. Moriarty, D.F, Fiorillo, C., Miller, C, and Colón, W. (2007) A truncated peptide model of the mutant P61A FIS forms a stable dimer. Biochim. Biophys. Acta, 1774, 78-85.
32. Meinhold, D., Beach, M., Shao, Y., Osuna, R., and Colón W. (2006) The location of an engineered inter-subunit disulfide bond in FIS affects the denaturation pathway and cooperativity. Biochemistry, 46, 9767-9777.
31. Feldman-Cohen, L. S., Shao, Y., Meinhold, D., Miller, C., Colón, W. and Osuna, R. (2006) Common and variable contributions by Fis residues on high-affinity binding at different DNA sequences. J. Bacteriol., 188, 2081-2095.
30. Lynch, S. M. and Colón, W. (2006) Dominant role of copper in the kinetic stability of Cu/Zn superoxide dismutase. Biochem. Biophys. Res. Commun., 340, 457-461.
29. Meinhold, D, Boswell, S., and Colón, W. (2005) P61A mutation in the factor for inversion stimulation results in a thermostable dimeric intermediate. Biochemistry, 44, 14715-14724.
28. Wang, L., Lashuel, H.A, Walz, T. and Colón, W. (2005) From Hexamer to amyloid: The mechanism of serum amyloid A fibril formation. Amyloid, 12, 139-148.
27. Moriarty, D.F. and Colón, W. (2005) Structural intermediates of globular proteins as precursors to amyloid formation in “Amyloid proteins: The beta pleated sheet conformation and disease”. Chapter 12, pages 275-300, Editors Jean Sipe, VCH-Wiley.
26. Wang L. and Colón, W. (2005) Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer. Prot. Science, 14, 1811-1817.
25. Lynch, S.M., Boswell, S.A. and Colón, W. (2004) Kinetic stability of SOD is dependent on its metal ligands: Implications for ALS. Biochemistry, 43, 16525-16531.
24. Manning, M and Colón, W. (2004) Structural basis of protein kinetic stability: Resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias towards -sheet structure. Biochemistry, 43, 11248-11254.
23. Boswell, S. A., Mathew, J., Beach, M., Osuna R., and Colón W. (2004) Variable contributions of tyrosine residues to the structural and spectroscopic properties of the factor for inversion stimulation. Biochemistry, 43, 2964-2977.
22. Wang L. and Colón, W. (2004) The interaction between apolipoprotein serum amyloid A and high-density lipoprotein. Biochem. Biophys. Res. Commun., 317, 157-161.
21. De Beus, M. D., Chung, J., and Colón, W. (2004) Modification of cysteine 111 in Cu/Zn superoxide dismutase results in altered spectroscopic and biophysical properties. Prot. Science, 13, 1347-1355.
20. Chung, J., Yang, H., deBeus, M. D., Ryu, C. Y., Cho, H., and Colón, W. (2003) Cu/Zn superoxide dismutase can form pore-like structures. Biochem. Biophys. Res. Commun., 312, 873-876.
19. Cheng, C-H., Battaglioli, G., Martin, D.L., Hobart, S. A. and Colón, W. (2003) Distinctive interactions in the holoenzyme formation for two isoforms of glutamate decarboxylase. Biochim. Biophys. Acta, 1645, 63-71.
18. Wang, L., Lashuel, H.A, Walz, T. and Colón, W. (2002) Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel. Proc. Natl. Acad. Sci., 99, 15947-15952.
17. Hobart, S. A., Meinhold, D., Moriarty D. F., Osuna R., and Colón W. (2002) From two-state to three-state: Effect of P61A mutation on the dynamics and stability of the factor for inversion stimulation results in an altered equilibrium denaturation mechanism. Biochemistry, 41, 13744-13754.
16. Hobart, S. A., Ilin S., Moriarty D. F., Osuna R., and Colón W. (2002) Equilibrium denaturation studies of the E. coli factor for inversion stimulation: Implications for in vivo function. Prot. Science, 11, 1671-1680.
15. Colón, W. Solving the protein folding problem. (2001) Chemical & Engineering News, page 225 (March 26).
14. Cheng, C-H, Colón, W., Myer, Y.P. and Martin, D.L. (2000) ATP’s impact on the conformation and holoenzyme formation in relation to the regulation of brain glutamate decarboxylase. Arch. Biochem. Biophys. 380, 285-293.
13. Colón, W. (1999) Analysis of protein structure by solution spectroscopy. Methods Enzymol. 310, 316-340.
12. Dolggikh, D. A., Latypov, R. F., Abdullaev, A. K., Colón, W., Roder, H., and Kirpichnikov, M. P. (1998) Expression of mutant horse cytochrome c genes in Escherichia coli. Bioorg. Khim. 24, 756-759.
11. Kelly, J.W., Colón, W., Lai, Z., Lashuel, H. A., McCulloch, J., McCutchen, S. L., Miroy, G. J. and Peterson, S. A. (1997) Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. Adv. Prot. Chem. 50, 161-181.
10. Colón, W., Wakem, P., Sherman, F. and Roder, H. (1997) Identification of the predominant non-native histidine ligand of unfolded cytochrome c. Biochemistry, 36, 12535-12541.
9. Roder, H. and Colón, W. (1997) Kinetic role of early intermediates in protein folding. Curr. Opinion Struct. Biol., 7, 15-28.
8. Colón, W. and Roder, H. (1996) Kinetic intermediates in the formation of the cytochrome c molten globule. Nat. Struct. Biol., 3, 1019-1025.
7. Colón, W., Elöve, G. E., Waken, L. P., Sherman, F. and Roder, H. (1996) Side chain packing of the n- and c- terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry, 35, 5538-5549.
6. Colón, W., Lai, Z., McCutchen, S. L., Miroy, G. J., Strang, C. and Kelly, J.W. (1996) FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formation. Ciba Found Symp. 199, 228-242.
5. Lai, Z., Colón, W. and Kelly, J.W. (1996) The acid–mediated denaturation pathway of transthyretin yields an intermediate which can self-assemble into amyloid. Biochemistry, 35, 6470-6482.
4. McCutchen, S. L., Lai, Z., Miroy, G. J., Kelly, J.W. and Colón, W. (1995) Comparison of lethal and nonlethal transthyretin variants and their relationship to amyloid disease. Biochemistry, 34, 13527-13536.
3. McCutchen, S. L., Colón, W. and Kelly, J.W. (1993) The transthyretin mutation Leu-55-Pro significantly alters tetramer stability and increases amyloidogenicity. Biochemistry, 32, 12119-12127.
2. Colón, W. and Kelly, J.W. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry, 31, 8654-8660 (1992).
1. Colón, W. and Kelly, J.W. (1991) Transthyretin Acid Induced Denaturation is Required for Amyloid Fibril Formation In Vitro. in Applications of Enzyme Biotechnology , pp 99-108, Editors, Jeffery W. Kelly and Thomas O. Baldwin (Plenum, New York).
Issued Patents
1. Patent Number 7,217,348 B2 (May 15, 2007) Methods of identifying kinetically stable proteins. Wilfredo Colón and Marta Manning, Rensselaer Polytechnic Institute.
2. Patent Number 7,393,443 B2 (July 1, 2008) Methods of identifying kinetically stable proteins. Wilfredo Colón and Marta Manning, Rensselaer Polytechnic Institute.