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 |
0.749 |
|
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 |
0.394 |
|
2017 |
Sun Y, Chakrabartty A. Phase to phase with TDP-43. Biochemistry. PMID 28112502 DOI: 10.1021/Acs.Biochem.6B01088 |
0.401 |
|
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 |
0.347 |
|
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 |
0.347 |
|
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 |
0.737 |
|
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 |
0.329 |
|
2015 |
Hadley KC, Rakhit R, Guo H, Sun Y, Jonkman JE, McLaurin J, Hazrati L, Emili A, Chakrabartty A. Author response: Determining composition of micron-scale protein deposits in neurodegenerative disease by spatially targeted optical microproteomics Elife. DOI: 10.7554/Elife.09579.018 |
0.744 |
|
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 |
0.31 |
|
2014 |
Mompeán M, Buratti E, Guarnaccia C, Brito RM, Chakrabartty A, Baralle FE, Laurents DV. "Structural characterization of the minimal segment of TDP-43 competent for aggregation". Archives of Biochemistry and Biophysics. 545: 53-62. PMID 24440310 DOI: 10.1016/J.Abb.2014.01.007 |
0.38 |
|
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 |
0.333 |
|
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 |
0.336 |
|
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 |
0.685 |
|
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 |
0.368 |
|
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 |
0.344 |
|
2012 |
Errington WJ, Khan MQ, Bueler SA, Rubinstein JL, Chakrabartty A, Privé GG. Adaptor protein self-assembly drives the control of a cullin-RING ubiquitin ligase. Structure (London, England : 1993). 20: 1141-53. PMID 22632832 DOI: 10.1016/J.Str.2012.04.009 |
0.311 |
|
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 |
0.706 |
|
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 |
0.709 |
|
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 |
0.348 |
|
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 |
0.363 |
|
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 |
0.345 |
|
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 |
0.678 |
|
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 |
0.679 |
|
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 |
0.769 |
|
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 |
0.378 |
|
2011 |
Hadley KC, Borrelli MJ, Lepock JR, McLaurin J, Croul SE, Guha A, Chakrabartty A. Erratum to: Multiphoton ANS fluorescence microscopy as an in vivo sensor for protein misfolding stress Cell Stress and Chaperones. 16: 563-563. DOI: 10.1007/S12192-011-0279-1 |
0.735 |
|
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 |
0.681 |
|
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 |
0.316 |
|
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 |
0.393 |
|
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 |
0.72 |
|
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 |
0.319 |
|
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 |
0.383 |
|
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 |
0.683 |
|
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 |
0.379 |
|
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 |
0.366 |
|
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 |
0.339 |
|
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 |
0.332 |
|
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 |
0.375 |
|
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 |
0.315 |
|
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 |
0.322 |
|
2006 |
Eli P, Chakrabartty A. P4-432: Amyloid inhibition via Abeta42 monomerization using semi-random peptides libraries Alzheimer's & Dementia. 2: S645-S645. DOI: 10.1016/J.Jalz.2006.05.2174 |
0.326 |
|
2006 |
Bateman DA, Chakrabartty A. P4-024: Alzheimer amyloid peptides aggregation propensity correlates directly with neuronal cell surface binding Alzheimer's & Dementia. 2: S520-S520. DOI: 10.1016/J.Jalz.2006.05.1762 |
0.342 |
|
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 |
0.329 |
|
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 |
0.314 |
|
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 |
0.367 |
|
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 |
0.375 |
|
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 |
0.3 |
|
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 |
0.356 |
|
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 |
0.348 |
|
2004 |
Gorman P, Guo M, Darabie A, McLaurin J, Chakrabartty A. P1-199 Cytotoxicity of membrane active spheroids formed by Alzheimer amyloid peptides Neurobiology of Aging. 25: S152-S153. DOI: 10.1016/S0197-4580(04)80512-8 |
0.311 |
|
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 |
0.302 |
|
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 |
0.311 |
|
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 |
0.361 |
|
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 |
0.349 |
|
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 |
0.343 |
|
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 |
0.404 |
|
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 |
0.395 |
|
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 |
0.406 |
|
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 |
0.318 |
|
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 |
0.31 |
|
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 |
0.393 |
|
2000 |
Boon CL, Chakrabartty A. Nonpolar contributions to conformational specificity in assemblies of designed short helical peptides Protein Science. 9: 1011-1023. PMID 10850811 DOI: 10.1110/Ps.9.5.1011 |
0.327 |
|
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 |
0.376 |
|
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 |
0.392 |
|
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 |
0.34 |
|
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 |
0.385 |
|
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 |
0.383 |
|
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 DOI: 10.1111/J.1432-1033.1997.T01-2-00355.X |
0.331 |
|
1995 |
Chakrabartty A, Baldwin RL. Stability Of Alpha -Helices Advances in Protein Chemistry. 46: 141-176. DOI: 10.1016/S0065-3233(08)60334-4 |
0.307 |
|
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 |
0.317 |
|
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