Year |
Citation |
Score |
2022 |
Morck MM, Bhowmik D, Pathak D, Dawood A, Spudich J, Ruppel KM. Hypertrophic cardiomyopathy mutations in the pliant and light chain-binding regions of the lever arm of human β-cardiac myosin have divergent effects on myosin function. Elife. 11. PMID 35767336 DOI: 10.7554/eLife.76805 |
0.466 |
|
2022 |
Gupta A, Dey S, Bhowmik D, Maiti S. Coexisting Ordered and Disordered Membrane Phases Have Distinct Modes of Interaction with Disease-Associated Oligomers. The Journal of Physical Chemistry. B. PMID 35104126 DOI: 10.1021/acs.jpcb.1c09421 |
0.434 |
|
2020 |
Bhowmik D, Nandwani N, Ruppel K, Liu C, Spudich JA. Study of Hcm Causing β-Cardiac Myosin Mutations Located at Different Structurally Significant Regions of the Myosin-Head Biophysical Journal. 118: 435a. DOI: 10.1016/J.Bpj.2019.11.2441 |
0.575 |
|
2019 |
Bhowmik D, Culver KSB, Liu T, Odom TW. Resolving Single-Nanoconstruct Dynamics during Targeting and Nontargeting Live-Cell Membrane Interactions. Acs Nano. PMID 31398007 DOI: 10.1021/Acsnano.9B03144 |
0.476 |
|
2019 |
Hu J, Wang D, Bhowmik D, Liu T, Deng S, Knudson MP, Ao X, Odom TW. Lattice-Resonance Metalenses for Fully Reconfigurable Imaging. Acs Nano. PMID 30896920 DOI: 10.1021/Acsnano.9B00651 |
0.719 |
|
2018 |
Choo P, Hryn AJ, Culver KS, Bhowmik D, Hu J, Odom TW. Wavelength-Dependent Differential Interference Contrast Inversion of Anisotropic Gold Nanoparticles. The Journal of Physical Chemistry. C, Nanomaterials and Interfaces. 122: 27024-27031. PMID 30627302 DOI: 10.1021/Acs.Jpcc.8B08995 |
0.479 |
|
2017 |
Chandra B, Bhowmik D, Maity BK, Mote KR, Dhara D, Venkatramani R, Maiti S, Madhu PK. Major Reaction Coordinates Linking Transient Amyloid-β Oligomers to Fibrils Measured at Atomic Level. Biophysical Journal. 113: 805-816. PMID 28834717 DOI: 10.1016/J.Bpj.2017.06.068 |
0.768 |
|
2017 |
Chandra B, Mithu VS, Bhowmik D, Das AK, Sahoo B, Maiti S, Madhu PK. Curcumin Dictates Divergent Fates for the Central Salt Bridges in Amyloid-β40 and Amyloid-β42. Biophysical Journal. 112: 1597-1608. PMID 28445751 DOI: 10.1016/J.Bpj.2017.02.043 |
0.813 |
|
2017 |
Chandra B, Bhowmik D, Kumar Maity B, Mote KR, Dhara D, Bera K, Das A, Venkatramani R, Maiti S, Madhu PK. Secondary Structure Flipping Connected to Salt-Bridge Formation Converts Toxic Amyloid-β 40 Oligomers to Fibrils Biophysical Journal. 112: 362a-363a. DOI: 10.1016/J.Bpj.2016.11.1966 |
0.796 |
|
2016 |
Adler J, Baumann M, Voigt B, Scheidt H, Bhowmik D, Häupl T, Abel B, Madhu PK, Balbach J, Maiti S, Huster D. A Detailed Analysis of the Morphology of Fibrils of Selectively Mutated Amyloid beta (1-40). Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. PMID 27224205 DOI: 10.1002/Cphc.201600413 |
0.804 |
|
2016 |
Rawat A, Bhowmik D, Kumar Maity B, Maiti S. Amyloid Aggregation of Amylin: Gain of Function along Aggregation Pathway? Biophysical Journal. 110: 554a-555a. DOI: 10.1016/J.Bpj.2015.11.2965 |
0.646 |
|
2016 |
Chandra B, Bhowmik D, Maity BK, Dhara D, Mote K, Venkatramani R, Madhu PK, Maiti S. A Hidden Structural Transition Accompanies the Progression of Amyloid-Beta Oligomers to Mature Fibrils Biophysical Journal. 110: 357a. DOI: 10.1016/J.Bpj.2015.11.1928 |
0.74 |
|
2016 |
Adler J, Baumann M, Voigt B, Scheidt HA, Bhowmik D, Häupl T, Abel B, Madhu PK, Balbach J, Maiti S, Huster D. Inside Back Cover: A Detailed Analysis of the Morphology of Fibrils of Selectively Mutated Amyloid β (1–40) (ChemPhysChem 17/2016) Chemphyschem. 17: 2773. DOI: 10.1002/Cphc.201600880 |
0.76 |
|
2015 |
Chandrakesan M, Bhowmik D, Sarkar B, Abhyankar R, Singh H, Kallianpur M, Dandekar SP, Madhu PK, Maiti S, Mithu VS. Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β18-35 and Makes it Soluble. The Journal of Biological Chemistry. PMID 26487720 DOI: 10.1074/Jbc.M115.674135 |
0.833 |
|
2015 |
Bhowmik D, Mote KR, MacLaughlin CM, Biswas N, Chandra B, Basu JK, Walker GC, Madhu PK, Maiti S. Cell-Membrane-Mimicking Lipid-Coated Nanoparticles Confer Raman Enhancement to Membrane Proteins and Reveal Membrane-Attached Amyloid-β Conformation. Acs Nano. 9: 9070-7. PMID 26391443 DOI: 10.1021/Acsnano.5B03175 |
0.766 |
|
2015 |
Das AK, Rawat A, Bhowmik D, Pandit R, Huster D, Maiti S. An Early Folding Contact between Phe19 and Leu34 is Critical for Amyloid-β Oligomer Toxicity. Acs Chemical Neuroscience. PMID 25951510 DOI: 10.1021/Acschemneuro.5B00074 |
0.776 |
|
2015 |
Bhowmik D, Das AK, Maiti S. Rapid, cell-free assay for membrane-active forms of amyloid-β. Langmuir : the Acs Journal of Surfaces and Colloids. 31: 4049-53. PMID 25310376 DOI: 10.1021/La502679T |
0.655 |
|
2015 |
Bhowmik D, Maiti S, Mote K, Chandra B, Madhu P. Amyloid-β Oligomers: Now for the Structure in the Membrane Biophysical Journal. 108: 65a. DOI: 10.1016/J.Bpj.2014.11.387 |
0.759 |
|
2014 |
Sarkar B, Mithu VS, Chandra B, Mandal A, Chandrakesan M, Bhowmik D, Madhu PK, Maiti S. Significant structural differences between transient amyloid-β oligomers and less-toxic fibrils in regions known to harbor familial Alzheimer's mutations. Angewandte Chemie (International Ed. in English). 53: 6888-92. PMID 24756858 DOI: 10.1002/Anie.201402636 |
0.83 |
|
2014 |
Mithu VS, Sarkar B, Bhowmik D, Das AK, Chandrakesan M, Maiti S, Madhu PK. Curcumin alters the salt bridge-containing turn region in amyloid β(1-42) aggregates. The Journal of Biological Chemistry. 289: 11122-31. PMID 24599958 DOI: 10.1074/Jbc.M113.519447 |
0.817 |
|
2014 |
Bhowmik D, MacLaughlin CM, Chandrakesan M, Ramesh P, Venkatramani R, Walker GC, Maiti S. pH changes the aggregation propensity of amyloid-β without altering the monomer conformation. Physical Chemistry Chemical Physics : Pccp. 16: 885-9. PMID 24292856 DOI: 10.1039/C3Cp54151G |
0.725 |
|
2014 |
Bhowmik D, MacLaughlin C, Walker GC, Maiti S. Decoupling Conformation, Aggregation and Function of Amyloid-β Monomers and Oligomers: An Fcs, Sers and Afm Study Biophysical Journal. 106: 269a-270a. DOI: 10.1016/J.Bpj.2013.11.1580 |
0.759 |
|
2014 |
Sarkar B, Mithu VS, Chandra B, Mandal A, Chandrakesan M, Bhowmik D, Madhu PK, Maiti S. Inside Cover: Significant Structural Differences between Transient Amyloid-β Oligomers and Less-Toxic Fibrils in Regions Known To Harbor Familial Alzheimer′s Mutations (Angew. Chem. Int. Ed. 27/2014) Angewandte Chemie International Edition. 53: 6830-6830. DOI: 10.1002/Anie.201405438 |
0.798 |
|
2013 |
Nag S, Sarkar B, Chandrakesan M, Abhyanakar R, Bhowmik D, Kombrabail M, Dandekar S, Lerner E, Haas E, Maiti S. A folding transition underlies the emergence of membrane affinity in amyloid-β. Physical Chemistry Chemical Physics : Pccp. 15: 19129-33. PMID 24121316 DOI: 10.1039/C3Cp52732H |
0.769 |
|
2013 |
Chandrakesan M, Sarkar B, Mithu VS, Abhyankar R, Bhowmik D, Nag S, Sahoo B, Shah R, Gurav S, Banerjee R, Dandekar S, Jose JC, Sengupta N, Madhu PK, Maiti S. The basic structural motif and major biophysical properties of Amyloid-β are encoded in the fragment 18-35 Chemical Physics. 422: 80-87. DOI: 10.1016/J.Chemphys.2013.01.010 |
0.827 |
|
2012 |
Abhyankar R, Sahoo B, Singh NK, Meijer LM, Sarkar B, Das AK, Nag S, Chandrakesan M, Bhowmik D, Dandekar S, Maiti S. Amyloid diagnostics: Probing protein aggregation and conformation with ultrasensitive fluorescence detection Progress in Biomedical Optics and Imaging - Proceedings of Spie. 8233. DOI: 10.1117/12.909829 |
0.788 |
|
2012 |
Nag S, Sarkar B, Muralidharan C, Bhowmik D, Das AK, Kombrabail M, Maiti S. Amyloid Beta Misfolds and Increases its Affinity for Cell Membranes at the Initial Step of Aggregation Biophysical Journal. 102: 44a. DOI: 10.1016/J.Bpj.2011.11.273 |
0.803 |
|
2011 |
Mithu VS, Sarkar B, Bhowmik D, Chandrakesan M, Maiti S, Madhu PK. Zn(++) binding disrupts the Asp(23)-Lys(28) salt bridge without altering the hairpin-shaped cross-β Structure of Aβ(42) amyloid aggregates. Biophysical Journal. 101: 2825-32. PMID 22261072 DOI: 10.1016/J.Bpj.2011.10.023 |
0.803 |
|
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