Year |
Citation |
Score |
2022 |
Narayan M. The Non-native Disulfide-Bond-Containing Landscape Orthogonal to the Oxidative Protein-Folding Trajectory: A Necessary Evil? The Journal of Physical Chemistry. B. PMID 36472840 DOI: 10.1021/acs.jpcb.2c04648 |
0.369 |
|
2021 |
Narayan M. Securing Native Disulfide Bonds in Disulfide-Coupled Protein Folding Reactions: The Role of Intrinsic and Extrinsic Elements vis-à-vis Protein Aggregation and Neurodegeneration. Acs Omega. 6: 31404-31410. PMID 34869967 DOI: 10.1021/acsomega.1c05269 |
0.336 |
|
2021 |
Narayan M. The Formation of Native Disulfide Bonds: Treading a Fine Line in Protein Folding. The Protein Journal. PMID 33765253 DOI: 10.1007/s10930-021-09976-7 |
0.332 |
|
2021 |
Narayan M, Berliner LJ. Supplement to the Special Issue on Protein Folding and Harold A. Scheraga. The Protein Journal. PMID 33723695 DOI: 10.1007/s10930-021-09977-6 |
0.55 |
|
2020 |
Narayan M, Berliner LJ. Introduction to the Special Issue on Protein Folding and Harold A. Scherega. The Protein Journal. PMID 33141423 DOI: 10.1007/s10930-020-09941-w |
0.555 |
|
2020 |
Henríquez G, Gomez A, Guerrero ED, Narayan M. The Potential Role of Natural Polyphenols Against Protein Aggregation Toxicity: In Vitro, In Vivo, and Clinical studies. Acs Chemical Neuroscience. PMID 32822152 DOI: 10.1021/Acschemneuro.0C00381 |
0.369 |
|
2020 |
Henríquez G, Mendez L, Varela-Ramirez A, Guerrero E, Narayan M. Neuroprotective Effect of Brazilin on Amyloid β (25-35)-Induced Pathology in a Human Neuroblastoma Model. Acs Omega. 5: 13785-13792. PMID 32566844 DOI: 10.1021/acsomega.0c00396 |
0.31 |
|
2020 |
Ahlawat J, Neupane R, Deemer E, Sreenivasan ST, Narayan M. Chitosan-Ellagic Acid Nanohybrid for Mitigating Rotenone-induced Oxidative Stress. Acs Applied Materials & Interfaces. PMID 32216327 DOI: 10.1021/Acsami.9B21215 |
0.381 |
|
2020 |
Henriquez G, Mendez L, Narayan M. A Hybrid Model to Study Amyloid Cross-Toxicity. Acs Chemical Neuroscience. PMID 31920071 DOI: 10.1021/Acschemneuro.9B00692 |
0.386 |
|
2019 |
Sreenivasan S, Narayan M. Learnings from Protein Folding Projected onto Amyloid Misfolding. Acs Chemical Neuroscience. PMID 31456389 DOI: 10.1021/Acschemneuro.9B00445 |
0.429 |
|
2019 |
Narayan M. The Era of Neurodegenerative Metastasis. Acs Chemical Neuroscience. PMID 31305063 DOI: 10.1021/Acschemneuro.9B00371 |
0.305 |
|
2019 |
Sreeprasad S, Narayan M. Nanoscopic Portrait of an Amyloidogenic Pathway Visualized through Tip-Enhanced Raman Spectroscopy. Acs Chemical Neuroscience. PMID 31290321 DOI: 10.1021/Acschemneuro.9B00353 |
0.36 |
|
2018 |
Xiong L, Yan W, Zubia E, Zhou Y, Zhang Y, Duan Q, Narayan M, Xu G. Quantitative proteomics and biochemical analyses reveal the role of endoplasmin in the regulation of the expression and secretion of A Disintegrin And Metalloproteinase 12. Journal of Proteomics. PMID 29729432 DOI: 10.1016/J.Jprot.2018.04.033 |
0.333 |
|
2017 |
Narayan M. The Structure-Forming Juncture in Oxidative Protein Folding: What Happens in the ER? Advances in Experimental Medicine and Biology. PMID 28815511 DOI: 10.1007/5584_2017_88 |
0.479 |
|
2016 |
Koebel MR, Cooper A, Schmadeke G, Jeon S, Narayan M, Sirimulla S. S···O and S···N Sulfur Bonding Interactions in Protein-Ligand Complexes: Empirical Considerations and Scoring Function. Journal of Chemical Information and Modeling. PMID 27936771 DOI: 10.1021/Acs.Jcim.6B00236 |
0.327 |
|
2016 |
Kabiraj P, Marin JE, Varela-Ramirez A, Narayan M. A 11-mer amyloid beta peptide fragment provokes chemical mutations and Parkinsonian biomarker aggregation in dopaminergic cells: a novel roadmap for "transfected" Parkinson's. Acs Chemical Neuroscience. PMID 27635664 DOI: 10.1021/Acschemneuro.6B00159 |
0.755 |
|
2016 |
Khalil MF, Valenzuela C, Sisniega D, Skouta R, Narayan M. ER Protein Processing Under Oxidative Stress: Implications and Prevention. Cell Biochemistry and Biophysics. PMID 26983927 DOI: 10.1007/S12013-016-0726-9 |
0.471 |
|
2015 |
Kabiraj P, Valenzuela CA, Marin JE, Ramirez DA, Mendez L, Hwang MS, Varela-Ramirez A, Fenelon K, Narayan M, Skouta R. The Neuroprotective Role of Ferrostatin-1 Under Rotenone-Induced Oxidative Stress in Dopaminergic Neuroblastoma Cells. The Protein Journal. 34: 349-58. PMID 26385697 DOI: 10.1007/S10930-015-9629-7 |
0.779 |
|
2014 |
Kabiraj P, Marin JE, Varela-Ramirez A, Zubia E, Narayan M. Ellagic acid mitigates SNO-PDI induced aggregation of Parkinsonian biomarkers. Acs Chemical Neuroscience. 5: 1209-20. PMID 25247703 DOI: 10.1021/Cn500214K |
0.765 |
|
2014 |
Arumugam A, Agullo P, Boopalan T, Nandy S, Lopez R, Gutierrez C, Narayan M, Rajkumar L. Neem leaf extract inhibits mammary carcinogenesis by altering cell proliferation, apoptosis, and angiogenesis. Cancer Biology & Therapy. 15: 26-34. PMID 24146019 DOI: 10.4161/Cbt.26604 |
0.306 |
|
2013 |
Sirimulla S, Bailey JB, Vegesna R, Narayan M. Halogen interactions in protein-ligand complexes: Implications of halogen bonding for rational drug design Journal of Chemical Information and Modeling. 53: 2781-2791. PMID 24134121 DOI: 10.1021/Ci400257K |
0.304 |
|
2012 |
Sirimulla S, Pal R, Raparla M, Bailey JB, Duran R, Altamirano AM, Herndon WC, Narayan M. Identification of Novel Nitrosative Stress Inhibitors through Virtual Screening and Experimental Evaluation. Molecular Informatics. 31: 167-72. PMID 27476961 DOI: 10.1002/Minf.201100044 |
0.572 |
|
2012 |
Kabiraj P, Pal R, Varela-Ramirez A, Miranda M, Narayan M. Nitrosative stress mediated misfolded protein aggregation mitigated by Na-D-β-hydroxybutyrate intervention. Biochemical and Biophysical Research Communications. 426: 438-44. PMID 22974977 DOI: 10.1016/J.Bbrc.2012.08.121 |
0.739 |
|
2012 |
Narayan M. Disulfide bonds: protein folding and subcellular protein trafficking. The Febs Journal. 279: 2272-82. PMID 22594874 DOI: 10.1111/J.1742-4658.2012.08636.X |
0.441 |
|
2012 |
Sirimulla S, Pal R, Raparla M, Bailey JB, Duran R, Altamirano AM, Herndon WC, Narayan M. Identification of novel nitrosative stress inhibitors through virtual screening and experimental evaluation Molecular Informatics. 31: 167-172. DOI: 10.1002/minf.201100044 |
0.435 |
|
2011 |
Pal R, Miranda M, Narayan M. Nitrosative stress-induced Parkinsonian Lewy-like aggregates prevented through polyphenolic phytochemical analog intervention. Biochemical and Biophysical Research Communications. 404: 324-9. PMID 21130735 DOI: 10.1016/J.Bbrc.2010.11.117 |
0.586 |
|
2011 |
Jessica GJ, Laura RL, Pal R, Gardea-Torresdey JL, Narayan M. From folklore to molecular pharmacophores: Cultivating STEM students among young, first-generation female Mexican-Americans Journal of Chemical Education. 88: 41-43. DOI: 10.1021/Ed100557U |
0.47 |
|
2011 |
Pinales LA, Chianelli RR, Durrer WG, Pal R, Narayan M, Manciu FS. Spectroscopic study of inhibition of calcium oxalate calculi growth by Larrea tridentata Journal of Raman Spectroscopy. 42: 259-264. DOI: 10.1002/Jrs.2742 |
0.498 |
|
2010 |
Gonzalez V, Pal R, Narayan M. The oxidoreductase behavior of protein disulfide isomerase impedes fold maturation of endoplasmic reticulum-processed proteins in the pivotal structure-coupled step of oxidative folding: implications for subcellular protein trafficking. Biochemistry. 49: 6282-9. PMID 20568731 DOI: 10.1021/Bi100753S |
0.634 |
|
2010 |
Pal R, Cristan EA, Schnittker K, Narayan M. Rescue of ER oxidoreductase function through polyphenolic phytochemical intervention: implications for subcellular traffic and neurodegenerative disorders. Biochemical and Biophysical Research Communications. 392: 567-71. PMID 20097158 DOI: 10.1016/J.Bbrc.2010.01.071 |
0.628 |
|
2010 |
Pal R, Gonzalez V, Narayan M. Reshuffling activity of protein disulfide isomerase reduces refolding yield in the structure-forming step of the oxidative protein folding reaction Chemistry Letters. 39: 263-265. DOI: 10.1246/Cl.2010.263 |
0.634 |
|
2008 |
Narayan M, Welker E, Zhai H, Han X, Xu G, McLafferty FW, Scheraga HA. Detecting native folds in mixtures of proteins that contain disulfide bonds. Nature Biotechnology. 26: 427-9. PMID 18278035 DOI: 10.1038/Nbt1380 |
0.506 |
|
2008 |
Gahl RF, Narayan M, Xu G, Scheraga HA. Dissimilarity in the oxidative folding of onconase and ribonuclease A, two structural homologues. Protein Engineering, Design & Selection : Peds. 21: 223-31. PMID 18245105 DOI: 10.1093/Protein/Gzm093 |
0.532 |
|
2008 |
Wang YH, Narayan M. pH dependence of the isomerase activity of protein disulfide isomerase: insights into its functional relevance. The Protein Journal. 27: 181-5. PMID 18074210 DOI: 10.1007/S10930-007-9121-0 |
0.377 |
|
2008 |
Fink M, Nieves P, Chang S, Narayan M. Non-redox-active small-molecules can accelerate oxidative protein folding by novel mechanisms. Biophysical Chemistry. 132: 104-9. PMID 18045767 DOI: 10.1016/J.Bpc.2007.10.014 |
0.461 |
|
2007 |
Gomez G, Mansouraty G, Gardea J, Narayan M. Acceleration of oxidative protein folding by curcumin through novel non-redox chemistry. Biochemical and Biophysical Research Communications. 364: 561-6. PMID 17959149 DOI: 10.1016/J.Bbrc.2007.10.024 |
0.496 |
|
2007 |
Welker E, Hathaway L, Xu G, Narayan M, Pradeep L, Shin HC, Scheraga HA. Oxidative folding and N-terminal cyclization of onconase. Biochemistry. 46: 5485-93. PMID 17439243 DOI: 10.1021/Bi602495A |
0.552 |
|
2006 |
Xu G, Narayan M, Kurinov I, Ripoll DR, Welker E, Khalili M, Ealick SE, Scheraga HA. A localized specific interaction alters the unfolding pathways of structural homologues. Journal of the American Chemical Society. 128: 1204-13. PMID 16433537 DOI: 10.1021/Ja055313E |
0.508 |
|
2005 |
Xu G, Narayan M, Scheraga HA. The oxidative folding rate of bovine pancreatic ribonuclease is enhanced by a covalently attached oligosaccharide. Biochemistry. 44: 9817-23. PMID 16008366 DOI: 10.1021/Bi0506932 |
0.471 |
|
2005 |
Leung HJ, Xu G, Narayan M, Scheraga HA. Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins. The Journal of Peptide Research : Official Journal of the American Peptide Society. 65: 47-54. PMID 15686534 DOI: 10.1111/J.1399-3011.2004.00189.X |
0.55 |
|
2004 |
Gahl RF, Narayan M, Xu G, Scheraga HA. Trimethylamine-N-oxide modulates the reductive unfolding of onconase. Biochemical and Biophysical Research Communications. 325: 707-10. PMID 15541346 DOI: 10.1016/J.Bbrc.2004.10.088 |
0.538 |
|
2004 |
Xu G, Zhai H, Narayan M, McLafferty FW, Scheraga HA. Simultaneous characterization of the reductive unfolding pathways of RNase B isoforms by top-down mass spectrometry. Chemistry & Biology. 11: 517-24. PMID 15123246 DOI: 10.1016/J.Chembiol.2004.03.020 |
0.503 |
|
2004 |
Chaudhuri D, Narayan M, Berliner LJ. Conformation-dependent interaction of alpha-lactalbumin with model and biological membranes: a spin-label ESR study. The Protein Journal. 23: 95-101. PMID 15115187 DOI: 10.1023/B:Jopc.0000016263.50484.E1 |
0.526 |
|
2004 |
Narayan M, Xu G, Ripoll DR, Zhai H, Breuker K, Wanjalla C, Leung HJ, Navon A, Welker E, McLafferty FW, Scheraga HA. Dissimilarity in the reductive unfolding pathways of two ribonuclease homologues. Journal of Molecular Biology. 338: 795-809. PMID 15099746 DOI: 10.1016/J.Jmb.2004.03.014 |
0.461 |
|
2004 |
Xu G, Narayan M, Welker E, Scheraga HA. Characterization of the fast-forming intermediate, des [30-75], in the reductive unfolding of onconase. Biochemistry. 43: 3246-54. PMID 15023075 DOI: 10.1021/Bi036215D |
0.489 |
|
2003 |
Narayan M, Xu G, Schultz SK, Scheraga HA. Assessing the magnitude of folding forces along the oxidative folding pathway of multi-disulfide-containing proteins. Journal of the American Chemical Society. 125: 16184-5. PMID 14692748 DOI: 10.1021/Ja0305398 |
0.545 |
|
2003 |
Xu G, Narayan M, Welker E, Scheraga HA. A novel method to determine thermal transition curves of disulfide-containing proteins and their structured folding intermediates. Biochemical and Biophysical Research Communications. 311: 514-7. PMID 14592446 DOI: 10.1016/J.Bbrc.2003.10.039 |
0.476 |
|
2003 |
Shin HC, Narayan M, Song MC, Scheraga HA. Role of the [65-72] disulfide bond in oxidative folding of bovine pancreatic ribonuclease A. Biochemistry. 42: 11514-9. PMID 14516203 DOI: 10.1021/Bi030152H |
0.478 |
|
2003 |
Narayan M, Welker E, Wanjalla C, Xu G, Scheraga HA. Shifting the competition between the intramolecular Reshuffling reaction and the direct oxidation reaction during the oxidative folding of kinetically trapped disulfide-insecure intermediates. Biochemistry. 42: 10783-9. PMID 12962503 DOI: 10.1021/Bi030141O |
0.545 |
|
2003 |
Narayan M, Welker E, Scheraga HA. Characterizing the unstructured intermediates in oxidative folding. Biochemistry. 42: 6947-55. PMID 12795589 DOI: 10.1021/Bi030054W |
0.548 |
|
2003 |
Narayan M, Welker E, Scheraga HA. Native conformational tendencies in unfolded polypeptides: development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins. Journal of the American Chemical Society. 125: 2036-7. PMID 12590517 DOI: 10.1021/Ja021252Y |
0.529 |
|
2002 |
English BP, Welker E, Narayan M, Scheraga HA. Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: implications for the mechanism of oxidative folding of RNase A. Journal of the American Chemical Society. 124: 4995-9. PMID 11982363 DOI: 10.1021/Ja012634R |
0.54 |
|
2001 |
Welker E, Wedemeyer WJ, Narayan M, Scheraga HA. Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins. Biochemistry. 40: 9059-64. PMID 11478871 DOI: 10.1021/Bi010409G |
0.51 |
|
2001 |
Narayan M, Welker E, Scheraga HA. Development of a novel method to study the rate-determining step during protein regeneration: application to the oxidative folding of RNase A at low temperature reveals BPTI-like kinetic traps. Journal of the American Chemical Society. 123: 2909-10. PMID 11456989 DOI: 10.1021/Ja003934W |
0.494 |
|
2001 |
Welker E, Narayan M, Wedemeyer WJ, Scheraga HA. Structural determinants of oxidative folding in proteins. Proceedings of the National Academy of Sciences of the United States of America. 98: 2312-6. PMID 11226236 DOI: 10.1073/Pnas.041615798 |
0.509 |
|
2001 |
Narayan M, Welker E, Wedemeyer WJ, Scheraga HA. ChemInform Abstract: Oxidative Folding of Proteins Cheminform. 32: no-no. DOI: 10.1002/chin.200106255 |
0.465 |
|
2000 |
Narayan M, Welker E, Wedemeyer WJ, Scheraga HA. Oxidative folding of proteins. Accounts of Chemical Research. 33: 805-12. PMID 11087317 DOI: 10.1021/Ar000063M |
0.553 |
|
2000 |
Wedemeyer WJ, Welker E, Narayan M, Scheraga HA. Disulfide bonds and protein folding Biochemistry. 39: 7032. PMID 10841785 |
0.433 |
|
2000 |
Low LK, Shin HC, Narayan M, Wedemeyer WJ, Scheraga HA. Acceleration of oxidative folding of bovine pancreatic ribonuclease A by anion-induced stabilization and formation of structured native-like intermediates. Febs Letters. 472: 67-72. PMID 10781807 DOI: 10.1016/S0014-5793(00)01432-0 |
0.53 |
|
2000 |
Wedemeyer WJ, Welker E, Narayan M, Scheraga HA. Disulfide bonds and protein folding. Biochemistry. 39: 4207-16. PMID 10757967 DOI: 10.1021/Bi992922O |
0.548 |
|
1999 |
Welker E, Narayan M, Volles MJ, Scheraga HA. Two new structured intermediates in the oxidative folding of RNase A. Febs Letters. 460: 477-9. PMID 10556520 DOI: 10.1016/S0014-5793(99)01391-5 |
0.511 |
|
1999 |
Veprintsev DB, Narayan M, Permyakov SE, Uversky VN, Brooks CL, Cherskaya AM, Permyakov EA, Berliner LJ. Fine tuning the N-terminus of a calcium binding protein: alpha-lactalbumin. Proteins. 37: 65-72. PMID 10451551 DOI: 10.1002/(Sici)1097-0134(19991001)37:1<65::Aid-Prot7>3.0.Co;2-2 |
0.563 |
|
1998 |
Narayan M, Berliner LJ. Mapping fatty acid binding to beta-lactoglobulin: Ligand binding is restricted by modification of Cys 121. Protein Science : a Publication of the Protein Society. 7: 150-7. PMID 9514270 DOI: 10.1002/Pro.5560070116 |
0.541 |
|
1997 |
Cawthern KM, Narayan M, Chaudhuri D, Permyakov EA, Berliner LJ. Interactions of alpha-lactalbumin with fatty acids and spin label analogs. The Journal of Biological Chemistry. 272: 30812-6. PMID 9388223 DOI: 10.1074/Jbc.272.49.30812 |
0.547 |
|
1997 |
Narayan M, Berliner LJ, Merola AJ, Diaz PT, Clanton TL. Biological reactions of peroxynitrite: evidence for an alternative pathway of salicylate hydroxylation. Free Radical Research. 27: 63-72. PMID 9269581 DOI: 10.3109/10715769709097839 |
0.533 |
|
1997 |
Narayan M, Berliner LJ. Fatty acids and retinoids bind independently and simultaneously to beta-lactoglobulin. Biochemistry. 36: 1906-11. PMID 9048577 DOI: 10.1021/Bi9621526 |
0.522 |
|
1997 |
Narayan M, Wright VP, Berliner LJ, Diaz PT, Merola AJ, Clanton TL. Do nitric oxide and peroxynitrite contribute to hydroxylation reactions in fatigued diaphragm? Faseb Journal. 11: A13. |
0.501 |
|
Show low-probability matches. |