Avijit Chakrabartty - Publications

Affiliations: 
Medical Biophysics University of Toronto, Toronto, ON, Canada 
Area:
General Biophysics, Biochemistry

96 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
2018 Sun Y, Medina Cruz A, Hadley KC, Galant N, Law R, Vernon R, Morris VK, Robertson J, Chakrabartty A. PHYSIOLOGICALLY IMPORTANT ELECTROLYTES AS REGULATORS OF TDP-43 AGGREGATION AND DROPLET-PHASE BEHAVIOR. Biochemistry. PMID 30489059 DOI: 10.1021/acs.biochem.8b00842  0.6
2017 Sun Y, Ip P, Chakrabartty A. Simple Elimination of Background Fluorescence in Formalin-Fixed Human Brain Tissue for Immunofluorescence Microscopy. Journal of Visualized Experiments : Jove. PMID 28892031 DOI: 10.3791/56188  0.36
2017 Ip P, Sharda PR, Cunningham A, Chakrabartty S, Pande V, Chakrabartty A. Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant. Protein Engineering, Design & Selection : Peds. 1-13. PMID 28475686 DOI: 10.1093/protein/gzx025  0.36
2017 Sun Y, Chakrabartty A. Phase to phase with TDP-43. Biochemistry. PMID 28112502 DOI: 10.1021/acs.biochem.6b01088  0.36
2016 Wan LC, Pillon MC, Thevakumaran N, Sun Y, Chakrabartty A, Guarné A, Kurinov I, Durocher D, Sicheri F. Structural and functional characterization of KEOPS dimerization by Pcc1 and its role in t6A biosynthesis. Nucleic Acids Research. PMID 27302132 DOI: 10.1093/nar/gkw542  0.36
2016 Galant NJ, Bugyei-Twum A, Rakhit R, Walsh P, Sharpe S, Arslan PE, Westermark P, Higaki JN, Torres R, Tapia J, Chakrabartty A. Corrigendum: Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses. Scientific Reports. 6: 27679. PMID 27282221 DOI: 10.1038/srep27679  0.52
2016 Galant NJ, Bugyei-Twum A, Rakhit R, Walsh P, Sharpe S, Arslan PE, Westermark P, Higaki JN, Torres R, Tapia J, Chakrabartty A. Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses. Scientific Reports. 6: 25080. PMID 27122057 DOI: 10.1038/srep25080  0.52
2016 Mompeán M, Chakrabartty A, Buratti E, Laurents DV. Electrostatic Repulsion Governs TDP-43 C-terminal Domain Aggregation. Plos Biology. 14: e1002447. PMID 27096426 DOI: 10.1371/journal.pbio.1002447  0.76
2016 Higaki JN, Chakrabartty A, Galant NJ, Hadley KC, Hammerson B, Nijjar T, Torres R, Tapia JR, Salmans J, Barbour R, Tam SJ, Flanagan K, Zago W, Kinney GG. Novel conformation-specific monoclonal antibodies against amyloidogenic forms of transthyretin. Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis. 1-12. PMID 26981744 DOI: 10.3109/13506129.2016.1148025  0.6
2015 Hadley KC, Rakhit R, Guo H, Sun Y, Jonkman JE, McLaurin J, Hazrati LN, Emili A, Chakrabartty A. Determining composition of micron-scale protein deposits in neurodegenerative disease by spatially targeted optical microproteomics. Elife. 4. PMID 26418743 DOI: 10.7554/eLife.09579  0.76
2015 Xiao S, Sanelli T, Chiang H, Sun Y, Chakrabartty A, Keith J, Rogaeva E, Zinman L, Robertson J. Low molecular weight species of TDP-43 generated by abnormal splicing form inclusions in amyotrophic lateral sclerosis and result in motor neuron death. Acta Neuropathologica. 130: 49-61. PMID 25788357 DOI: 10.1007/s00401-015-1412-5  0.76
2014 Sun Y, Arslan PE, Won A, Yip CM, Chakrabartty A. Binding of TDP-43 to the 3'UTR of its cognate mRNA enhances its solubility. Biochemistry. 53: 5885-94. PMID 25171271 DOI: 10.1021/bi500617x  0.52
2014 Weichert A, Besemer AS, Liebl M, Hellmann N, Koziollek-Drechsler I, Ip P, Decker H, Robertson J, Chakrabartty A, Behl C, Clement AM. Wild-type Cu/Zn superoxide dismutase stabilizes mutant variants by heterodimerization. Neurobiology of Disease. 62: 479-88. PMID 24200866 DOI: 10.1016/j.nbd.2013.10.027  0.76
2014 Kerman A, Chakrabartty A. Protein misfolding and toxicity in amyotrophic lateral sclerosis Non-Fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases. 257-288. DOI: 10.1007/978-94-007-2774-8_8  0.76
2013 Diez-García F, Pantoja-Uceda D, Jiménez MÁ, Chakrabartty A, Laurents DV. Structure of a simplified β-hairpin and its ATP complex. Archives of Biochemistry and Biophysics. 537: 62-71. PMID 23811197 DOI: 10.1016/j.abb.2013.06.009  0.76
2013 Sweeting B, Brown E, Khan MQ, Chakrabartty A, Pai EF. N-terminal helix-cap in α-helix 2 modulates β-state misfolding in rabbit and hamster prion proteins. Plos One. 8: e63047. PMID 23675452 DOI: 10.1371/journal.pone.0063047  0.76
2013 Mulligan VK, Chakrabartty A. Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis. Proteins. 81: 1285-303. PMID 23508986 DOI: 10.1002/prot.24285  0.76
2012 Diez-García F, Chakrabartty A, González C, Laurents DV. An Arg-rich putative prebiotic protein is as stable as its Lys-rich variant. Archives of Biochemistry and Biophysics. 528: 118-26. PMID 23022061 DOI: 10.1016/j.abb.2012.09.006  0.76
2012 Liu HN, Tjostheim S, Dasilva K, Taylor D, Zhao B, Rakhit R, Brown M, Chakrabartty A, McLaurin J, Robertson J. Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 32: 8791-9. PMID 22745481 DOI: 10.1523/JNEUROSCI.5053-11.2012  0.76
2012 Mulligan VK, Kerman A, Laister RC, Sharda PR, Arslan PE, Chakrabartty A. Early steps in oxidation-induced SOD1 misfolding: implications for non-amyloid protein aggregation in familial ALS. Journal of Molecular Biology. 421: 631-52. PMID 22542526 DOI: 10.1016/j.jmb.2012.04.016  0.76
2012 Mulligan VK, Hadley KC, Chakrabartty A. Analyzing complicated protein folding kinetics rapidly by analytical Laplace inversion using a Tikhonov regularization variant. Analytical Biochemistry. 421: 181-90. PMID 22119751 DOI: 10.1016/j.ab.2011.10.050  0.76
2012 Diez-García F, Gómez-Pinto I, Chakrabartty A, González C, Laurents DV. Conformation specificity and arene binding in a peptide composed only of Lys, Ile, Ala and Gly. European Biophysics Journal : Ebj. 41: 63-72. PMID 22038076 DOI: 10.1007/s00249-011-0758-4  0.76
2011 Julien O, Chatterjee S, Bjorndahl TC, Sweeting B, Acharya S, Semenchenko V, Chakrabartty A, Pai EF, Wishart DS, Sykes BD, Cashman NR. Relative and regional stabilities of the hamster, mouse, rabbit, and bovine prion proteins toward urea unfolding assessed by nuclear magnetic resonance and circular dichroism spectroscopies. Biochemistry. 50: 7536-45. PMID 21800884 DOI: 10.1021/bi200731e  0.76
2011 Yanagisawa K, Fantini J, Chakrabartty A, Eckert A. Aβ behavior on neuronal membranes: aggregation and toxicities. International Journal of Alzheimer's Disease. 2011: 286536. PMID 21760987 DOI: 10.4061/2011/286536  0.76
2011 Ceccarelli DF, Laister RC, Mulligan VK, Kean MJ, Goudreault M, Scott IC, Derry WB, Chakrabartty A, Gingras AC, Sicheri F. CCM3/PDCD10 heterodimerizes with germinal center kinase III (GCKIII) proteins using a mechanism analogous to CCM3 homodimerization. The Journal of Biological Chemistry. 286: 25056-64. PMID 21561863 DOI: 10.1074/jbc.M110.213777  0.76
2011 Ip P, Mulligan VK, Chakrabartty A. ALS-causing SOD1 mutations promote production of copper-deficient misfolded species. Journal of Molecular Biology. 409: 839-52. PMID 21549128 DOI: 10.1016/j.jmb.2011.04.027  0.76
2011 Hadley KC, Borrelli MJ, Lepock JR, McLaurin J, Croul SE, Guha A, Chakrabartty A. Multiphoton ANS fluorescence microscopy as an in vivo sensor for protein misfolding stress. Cell Stress & Chaperones. 16: 549-61. PMID 21484286 DOI: 10.1007/s12192-011-0266-6  0.76
2011 Bateman DA, Chakrabartty A. Cell surface binding and internalization of aβ modulated by degree of aggregation. International Journal of Alzheimer's Disease. 2011: 962352. PMID 21331340 DOI: 10.4061/2011/962352  0.76
2011 Bateman DA, Chakrabartty A. Interaction of Alzheimer Amyloid Peptide with Cell Surfaces and Artificial Membranes Lipids and Cellular Membranes in Amyloid Diseases. 231-243. DOI: 10.1002/9783527634323.ch11  0.76
2010 Khan MQ, Sweeting B, Mulligan VK, Arslan PE, Cashman NR, Pai EF, Chakrabartty A. Prion disease susceptibility is affected by beta-structure folding propensity and local side-chain interactions in PrP. Proceedings of the National Academy of Sciences of the United States of America. 107: 19808-13. PMID 21041683 DOI: 10.1073/pnas.1005267107  0.76
2010 Sweeting B, Khan MQ, Chakrabartty A, Pai EF. Structural factors underlying the species barrier and susceptibility to infection in prion disease. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 88: 195-202. PMID 20453922 DOI: 10.1139/o09-172  0.76
2010 López-Alonso JP, Pardo-Cea MA, Gómez-Pinto I, Fernández I, Chakrabartty A, Pedroso E, González C, Laurents DV. Putative one-pot prebiotic polypeptides with ribonucleolytic activity. Chemistry (Weinheim An Der Bergstrasse, Germany). 16: 5314-23. PMID 20232309 DOI: 10.1002/chem.200903207  0.76
2010 Kerman A, Liu HN, Croul S, Bilbao J, Rogaeva E, Zinman L, Robertson J, Chakrabartty A. Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form Acta Neuropathologica. 119: 335-344. PMID 20111867 DOI: 10.1007/s00401-010-0646-5  0.76
2010 Arslan PE, Mulligan VK, Ho S, Chakrabartty A. Conversion of Abeta42 into a folded soluble native-like protein using a semi-random library of amphipathic helices. Journal of Molecular Biology. 396: 1284-94. PMID 20026077 DOI: 10.1016/j.jmb.2009.12.019  0.76
2009 Arslan PE, Chakrabartty A. Probing Alzheimer amyloid peptide aggregation using a cell-free fluorescent protein refolding method. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 87: 631-9. PMID 19767826 DOI: 10.1139/o09-038  0.76
2009 Bateman DA, Chakrabartty A. Two distinct conformations of Abeta aggregates on the surface of living PC12 cells. Biophysical Journal. 96: 4260-7. PMID 19450496 DOI: 10.1016/j.bpj.2009.01.056  0.76
2008 Mulligan VK, Kerman A, Ho S, Chakrabartty A. Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis. Journal of Molecular Biology. 383: 424-36. PMID 18761352 DOI: 10.1016/j.jmb.2008.08.024  0.76
2008 Gorman PM, Kim S, Guo M, Melnyk RA, McLaurin J, Fraser PE, Bowie JU, Chakrabartty A. Dimerization of the transmembrane domain of amyloid precursor proteins and familial Alzheimer's disease mutants. Bmc Neuroscience. 9: 17. PMID 18234110 DOI: 10.1186/1471-2202-9-17  0.76
2007 Li L, Coulthart MB, Balachandran A, Chakrabartty A, Cashman NR. Species barriers for chronic wasting disease by in vitro conversion of prion protein. Biochemical and Biophysical Research Communications. 364: 796-800. PMID 17964288 DOI: 10.1016/j.bbrc.2007.10.087  0.76
2007 Scotter AJ, Guo M, Tomczak MM, Daley ME, Campbell RL, Oko RJ, Bateman DA, Chakrabartty A, Sykes BD, Davies PL. Metal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides. Bmc Structural Biology. 7: 63. PMID 17908326 DOI: 10.1186/1472-6807-7-63  0.76
2007 López de la Osa J, Bateman DA, Ho S, González C, Chakrabartty A, Laurents DV. Getting specificity from simplicity in putative proteins from the prebiotic earth. Proceedings of the National Academy of Sciences of the United States of America. 104: 14941-6. PMID 17855563 DOI: 10.1073/pnas.0706876104  0.76
2007 Rakhit R, Robertson J, Vande Velde C, Horne P, Ruth DM, Griffin J, Cleveland DW, Cashman NR, Chakrabartty A. An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS. Nature Medicine. 13: 754-9. PMID 17486090 DOI: 10.1038/nm1559  0.76
2007 Bateman DA, McLaurin J, Chakrabartty A. Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding. Bmc Neuroscience. 8: 29. PMID 17475015 DOI: 10.1186/1471-2202-8-29  0.76
2006 Eli P, Chakrabartty A. Variants of DsRed fluorescent protein: Development of a copper sensor. Protein Science : a Publication of the Protein Society. 15: 2442-7. PMID 17008724 DOI: 10.1110/ps.062239206  0.76
2006 Rakhit R, Chakrabartty A. Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis. Biochimica Et Biophysica Acta. 1762: 1025-37. PMID 16814528 DOI: 10.1016/j.bbadis.2006.05.004  0.76
2006 Gombos Z, Yap KL, Ikura M, Chakrabartty A. NMR-driven secondary and tertiary structure model of Ca2+-loaded calexcitin. Biochemical and Biophysical Research Communications. 343: 520-4. PMID 16546129 DOI: 10.1016/j.bbrc.2006.02.182  0.76
2005 Guo M, Gorman PM, Rico M, Chakrabartty A, Laurents DV. Charge substitution shows that repulsive electrostatic interactions impede the oligomerization of Alzheimer amyloid peptides. Febs Letters. 579: 3574-8. PMID 15964569 DOI: 10.1016/j.febslet.2005.05.036  0.76
2005 Marshall CB, Chakrabartty A, Davies PL. Hyperactive antifreeze protein from winter flounder is a very long rod-like dimer of alpha-helices. The Journal of Biological Chemistry. 280: 17920-9. PMID 15716269 DOI: 10.1074/jbc.M500622200  0.76
2005 Frost DW, Yip CM, Chakrabartty A. Reversible assembly of helical filaments by de novo designed minimalist peptides. Biopolymers. 80: 26-33. PMID 15612048 DOI: 10.1002/bip.20188  0.76
2005 Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? Journal of Molecular Biology. 345: 275-87. PMID 15571721 DOI: 10.1016/j.jmb.2004.10.045  0.76
2005 Laurents DV, Gorman PM, Guo M, Rico M, Chakrabartty A, Bruix M. Alzheimer's Abeta40 studied by NMR at low pH reveals that sodium 4,4-dimethyl-4-silapentane-1-sulfonate (DSS) binds and promotes beta-ball oligomerization. The Journal of Biological Chemistry. 280: 3675-85. PMID 15557279 DOI: 10.1074/jbc.M409507200  0.76
2004 Fung J, Frost D, Chakrabartty A, McLaurin J. Interaction of human and mouse Abeta peptides. Journal of Neurochemistry. 91: 1398-403. PMID 15584916 DOI: 10.1111/j.1471-4159.2004.02828.x  0.76
2004 Boon CL, Frost D, Chakrabartty A. Identification of stable helical bundles from a combinatorial library of amphipathic peptides. Biopolymers. 76: 244-57. PMID 15148684 DOI: 10.1002/bip.20074  0.76
2004 Bateman DA, Chakrabartty A. Interactions of Alzheimer amyloid peptides with cultured cells and brain tissue, and their biological consequences. Biopolymers. 76: 4-14. PMID 14997469 DOI: 10.1002/bip.10561  0.76
2004 Rakhit R, Crow JP, Lepock JR, Kondejewski LH, Cashman NR, Chakrabartty A. Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 279: 15499-504. PMID 14734542 DOI: 10.1074/jbc.M313295200  0.76
2004 Gorochov G, Deslys JP, Paramithiotis E, Pinard M, Lawton T, LaBoissiere S, Leathers VL, Zou WQ, Estey LA, Lamontagne J, Lehto MT, Kondejewski LH, Francoeur GP, Papadopoulos M, Haghighat A, ... ... Chakrabartty A, et al. Properties of a disease-specific prion probe [1] (multiple letters) Nature Medicine. 10: 11-12. PMID 14702617  0.76
2003 Paramithiotis E, Pinard M, Lawton T, LaBoissiere S, Leathers VL, Zou WQ, Estey LA, Lamontagne J, Lehto MT, Kondejewski LH, Francoeur GP, Papadopoulos M, Haghighat A, Spatz SJ, Head M, ... ... Chakrabartty A, et al. A prion protein epitope selective for the pathologically misfolded conformation. Nature Medicine. 9: 893-9. PMID 12778138 DOI: 10.1038/nm883  0.76
2003 Gombos Z, Durussel I, Ikura M, Rose DR, Cox JA, Chakrabartty A. Conformational coupling of Mg2+ and Ca2+ on the three-state folding of calexcitin B. Biochemistry. 42: 5531-9. PMID 12731896 DOI: 10.1021/bi034047j  0.76
2003 Chan PM, Ilangumaran S, La Rose J, Chakrabartty A, Rottapel R. Autoinhibition of the kit receptor tyrosine kinase by the cytosolic juxtamembrane region. Molecular and Cellular Biology. 23: 3067-78. PMID 12697809 DOI: 10.1128/MCB.23.9.3067-3078.2003  0.76
2003 Frost D, Gorman PM, Yip CM, Chakrabartty A. Co-incorporation of A beta 40 and A beta 42 to form mixed pre-fibrillar aggregates. European Journal of Biochemistry / Febs. 270: 654-63. PMID 12581205 DOI: 10.1046/j.1432-1033.2003.03415.x  0.76
2003 Gorman PM, Yip CM, Fraser PE, Chakrabartty A. Alternate aggregation pathways of the Alzheimer beta-amyloid peptide: Abeta association kinetics at endosomal pH. Journal of Molecular Biology. 325: 743-57. PMID 12507477 DOI: 10.1016/S0022-2836(02)01279-2  0.76
2003 Qin K, Coomaraswamy J, Mastrangelo P, Yang Y, Lugowski S, Petromilli C, Prusiner SB, Fraser PE, Goldberg JM, Chakrabartty A, Westaway D. The PrP-like protein Doppel binds copper. The Journal of Biological Chemistry. 278: 8888-96. PMID 12482851 DOI: 10.1074/jbc.M210875200  0.76
2002 Rakhit R, Cunningham P, Furtos-Matei A, Dahan S, Qi XF, Crow JP, Cashman NR, Kondejewski LH, Chakrabartty A. Oxidation-induced misfolding and aggregation of superoxide dismutase and its implications for amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 277: 47551-6. PMID 12356748 DOI: 10.1074/jbc.M207356200  0.76
2001 Gorman PM, Chakrabartty A. Alzheimer β-amyloid peptides: Structures of amyloid fibrils and alternate aggregation products Biopolymers - Peptide Science Section. 60: 381-394. PMID 12115148 DOI: 10.1002/1097-0282(2001)60:5<381::AID-BIP10173>3.0.CO;2-U  0.76
2001 Chakrabartty A. Progress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis Proceedings of the National Academy of Sciences of the United States of America. 98: 14757-14759. PMID 11752419 DOI: 10.1073/pnas.261596398  0.76
2001 Zou WQ, Yang DS, Fraser PE, Cashman NR, Chakrabartty A. All or none fibrillogenesis of a prion peptide. European Journal of Biochemistry / Febs. 268: 4885-91. PMID 11559357 DOI: 10.1046/j.1432-1327.2001.02415.x  0.76
2001 Qi XF, Bagby S, Gombos Z, Ikura M, Chakrabartty A. Alternate routes to conformational specificity in a Greek key β barrel protein European Journal of Biochemistry. 268: 4653-4663. PMID 11532002 DOI: 10.1046/j.1432-1327.2001.02388.x  0.76
2001 Wróblewski K, Muhandiram R, Chakrabartty A, Bennick A. The molecular interaction of human salivary histatins with polyphenolic compounds European Journal of Biochemistry. 268: 4384-4397. PMID 11502198 DOI: 10.1046/j.1432-1327.2001.02350.x  0.76
2001 Schimmer AD, Hedley DW, Chow S, Pham NA, Chakrabartty A, Bouchard D, Mak TW, Trus MR, Minden MD. The BH3 domain of BAD fused to the Antennapedia peptide induces apoptosis via its alpha helical structure and independent of Bcl-2 Cell Death and Differentiation. 8: 725-733. PMID 11464217 DOI: 10.1038/sj.cdd.4400870  0.76
2001 Gombos Z, Jeromin A, Mal TK, Chakrabartty A, Ikura M. Calexcitin B Is a New Member of the Sarcoplasmic Calcium-binding Protein Family Journal of Biological Chemistry. 276: 22529-22536. PMID 11306567 DOI: 10.1074/jbc.M010508200  0.76
2000 Huang TH, Yang DS, Fraser PE, Chakrabartty A. Alternate aggregation pathways of the Alzheimer beta-amyloid peptide. An in vitro model of preamyloid. The Journal of Biological Chemistry. 275: 36436-40. PMID 10961999 DOI: 10.1074/jbc.M005698200  0.76
2000 Boon CL, Chakrabartty A. Nonpolar contributions to conformational specificity in assemblies of designed short helical peptides Protein Science. 9: 1011-1023. PMID 10850811  0.76
2000 Huang TH, Yang DS, Plaskos NP, Go S, Yip CM, Fraser PE, Chakrabartty A. Structural studies of soluble oligomers of the Alzheimer beta-amyloid peptide. Journal of Molecular Biology. 297: 73-87. PMID 10704308 DOI: 10.1006/jmbi.2000.3559  0.76
1999 Yang DS, Yip CM, Huang TH, Chakrabartty A, Fraser PE. Manipulating the amyloid-beta aggregation pathway with chemical chaperones. The Journal of Biological Chemistry. 274: 32970-4. PMID 10551864 DOI: 10.1074/jbc.274.46.32970  0.76
1999 Botuyan MV, Koth CM, Mer G, Chakrabartty A, Conaway JW, Conaway RC, Edwards AM, Arrowsmith CH, Chazin WJ. Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C Proceedings of the National Academy of Sciences of the United States of America. 96: 9033-9038. PMID 10430890 DOI: 10.1073/pnas.96.16.9033  0.76
1998 McLaurin J, Franklin T, Chakrabartty A, Fraser PE. Phosphatidylinositol and inositol involvement in Alzheimer amyloid-beta fibril growth and arrest. Journal of Molecular Biology. 278: 183-94. PMID 9571042 DOI: 10.1006/jmbi.1998.1677  0.76
1998 Bagby S, Go S, Inouye S, Ikura M, Chakrabartty A. Equilibrium folding intermediates of a Greek key β-barrel protein Journal of Molecular Biology. 276: 669-681. PMID 9551104 DOI: 10.1006/jmbi.1997.1563  0.76
1998 McLaurin J, Franklin T, Fraser PE, Chakrabartty A. Structural transitions associated with the interaction of Alzheimer beta-amyloid peptides with gangliosides. The Journal of Biological Chemistry. 273: 4506-15. PMID 9468505 DOI: 10.1074/jbc.273.8.4506  0.76
1997 Yanagisawa K, McLaurin J, Michikawa M, Chakrabartty A, Ihara Y. Amyloid β-protein (Aβ) associated with lipid molecules: Immunoreactivity distinct from that of soluble Aβ Febs Letters. 420: 43-46. PMID 9450547 DOI: 10.1016/S0014-5793(97)01484-1  0.76
1997 Huang TH, Fraser PE, Chakrabartty A. Fibrillogenesis of Alzheimer Abeta peptides studied by fluorescence energy transfer. Journal of Molecular Biology. 269: 214-24. PMID 9191066 DOI: 10.1006/jmbi.1997.1050  0.76
1997 McLaurin J, Chakrabartty A. Characterization of the interactions of Alzheimer β-amyloid peptides with phospholipid membranes European Journal of Biochemistry. 245: 355-363. PMID 9151964  0.76
1996 Rohl CA, Chakrabartty A, Baldwin RL. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Science : a Publication of the Protein Society. 5: 2623-37. PMID 8976571 DOI: 10.1002/pro.5560051225  0.76
1996 McLaurin J, Chakrabartty A. Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides. Implications for neurotoxicity Journal of Biological Chemistry. 271: 26482-26489. PMID 8900116 DOI: 10.1074/jbc.271.43.26482  0.76
1995 Chakrabartty A, Baldwin RL. Stability of α-helices Advances in Protein Chemistry. 46: 141-176. PMID 7771317  0.76
1994 Doig AJ, Chakrabartty A, Klingler TM, Baldwin RL. Determination of free energies of N-capping in α-helices by modification of the Lifson-Roig helix-coil theory to include N- and C-capping Biochemistry. 33: 3396-3403. PMID 8136377  0.76
1994 Chakrabartty A, Kortemme T, Baldwin RL. Helix propensities of the amino acids measured in alanine-based peptides without helix-stabilizing side-chain interactions. Protein Science : a Publication of the Protein Society. 3: 843-52. PMID 8061613 DOI: 10.1002/pro.5560030514  0.76
1993 Chakrabartty A, Kortemme T, Padmanabhan S, Baldwin RL. Aromatic side-chain contribution to far-ultraviolet circular dichroism of helical peptides and its effect on measurement of helix propensities. Biochemistry. 32: 5560-5. PMID 8504077  0.76
1993 Chakrabartty A, Doig AJ, Baldwin RL. Helix capping propensities in peptides parallel those in proteins Proceedings of the National Academy of Sciences of the United States of America. 90: 11332-11336. PMID 8248248  0.76
1991 Chakrabartty A, Schellman JA, Baldwin RL. Large differences in the helix propensities of alanine and glycine. Nature. 351: 586-8. PMID 2046766 DOI: 10.1038/351586a0  0.76
1991 Chakrabartty A, Hew CL. The effect of enhanced α-helicity on the activity of a winter flounder antifreeze polypeptide European Journal of Biochemistry. 202: 1057-1063. PMID 1765066  0.76
1989 Chakrabartty A, Yang DS, Hew CL. Structure-function relationship in a winter flounder antifreeze polypeptide. II. Alteration of the component growth rates of ice by synthetic antifreeze polypeptides Journal of Biological Chemistry. 264: 11313-11316. PMID 2738068  0.76
1989 Chakrabartty A, Ananthanarayanan VS, Hew CL. Structure-function relationships in a winter flounder antifreeze polypeptide. I. Stabilization of an alpha-helical antifreeze polypeptide by charged-group and hydrophobic interactions Journal of Biological Chemistry. 264: 11307-11312. PMID 2738067  0.76
1988 Yang DSC, Sax M, Chakrabartty A, Hew CL. Crystal structure of an antifreeze polypeptide and its mechanistic implications Nature. 333: 232-237. PMID 3368002  0.76
1988 Yang DSC, Sax M, Chakrabartty A, Hew CL. Antifreeze polypeptides come out of the cold [8] Nature. 335: 503.  0.76
1985 Chakrabartty A, Stinson RA. Tetrameric alkaline phosphatase in human liver plasma membranes Biochemical and Biophysical Research Communications. 131: 328-335. PMID 4038299 DOI: 10.1016/0006-291X(85)91806-6  0.76
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