Year |
Citation |
Score |
2024 |
Pitman C, Santiago-McRae E, Lohia R, Bassi K, Joseph TT, Hansen MEB, Brannigan G. The blobulator: a webtool for identification and visual exploration of hydrophobic modularity in protein sequences. Biorxiv : the Preprint Server For Biology. PMID 38293114 DOI: 10.1101/2024.01.15.575761 |
0.713 |
|
2022 |
Lohia R, Hansen MEB, Brannigan G. Contiguously hydrophobic sequences are functionally significant throughout the human exome. Proceedings of the National Academy of Sciences of the United States of America. 119: e2116267119. PMID 35294280 DOI: 10.1073/pnas.2116267119 |
0.566 |
|
2022 |
Ahmed SS, Rifat ZT, Lohia R, Campbell AJ, Dunker AK, Rahman MS, Iqbal S. Characterization of intrinsically disordered regions in proteins informed by human genetic diversity. Plos Computational Biology. 18: e1009911. PMID 35275927 DOI: 10.1371/journal.pcbi.1009911 |
0.425 |
|
2020 |
Lohia R, Bassi K, Hansen M, Brannigan G. Disease Associated Mutations in Intrinsically Disordered Proteins Show Evidence of Enrichment in Hydrophobic Blobs Biophysical Journal. 118. DOI: 10.1016/J.Bpj.2019.11.1280 |
0.684 |
|
2019 |
Lohia R, Salari R, Brannigan G. Sequence specificity despite intrinsic disorder: How a disease-associated Val/Met polymorphism rearranges tertiary interactions in a long disordered protein. Plos Computational Biology. 15: e1007390. PMID 31626641 DOI: 10.1371/Journal.Pcbi.1007390 |
0.781 |
|
2019 |
Lohia R, Brannigan G. Conformational Effects of a Disease-Associated Hydrophobic-to-Hydrophobic Substitution and Histidine Protonation State Located at the Midpoint of the Intrinsically Disordered Region of proBDNF Biophysical Journal. 116: 179a. DOI: 10.1016/J.Bpj.2018.11.993 |
0.704 |
|
2018 |
Salari R, Joseph T, Lohia R, Hénin J, Brannigan G. A streamlined, general approach for computing ligand binding free energies and its application to GPCR-bound cholesterol. Journal of Chemical Theory and Computation. PMID 30358394 DOI: 10.1021/Acs.Jctc.8B00447 |
0.667 |
|
2018 |
Lohia R, Brannigan G. Conformational Effects of Various Hydrophobic-to-Hydrophobic Substitution Located at the Midpoint of the Intrinsically Disordered Region of ProBDNF Biophysical Journal. 114: 591a. DOI: 10.1016/J.Bpj.2017.11.3229 |
0.721 |
|
2017 |
Lohia R, Salari R, Brannigan G. Mechanism Underlying Conformational Effects of a Disease-Associated Hydrophobic-to-Hydrophobic Substitution on an Intrinsically Disordered Region Biophysical Journal. 112: 207a. DOI: 10.1016/J.Bpj.2016.11.1145 |
0.782 |
|
2016 |
Lohia R, Salari R, Brannigan G. Effects of a Structured Domain on the Conformational Ensemble of Disordered Regions in Brain-Derived Neurotrophic Factor Biophysical Journal. 110: 559a. DOI: 10.1016/J.Bpj.2015.11.2989 |
0.791 |
|
2015 |
Lohia R, Salari R, Brannigan G. Prediction of the Effects of the Val66Met Polymorphism and Adjacent Structured Domains on the Conformational Ensemble of an Intrinsically Disordered Protein, Brain-Derived Neurotrophic Factor Biophysical Journal. 108: 386a-387a. DOI: 10.1016/J.Bpj.2014.11.2118 |
0.793 |
|
2014 |
Lohia R, Salari R, Brannigan G. Prediction of the Effects of the Val66Met Polymorphism on the Conformational Ensemble of an Intrinsically Disordered Protein, Brain-Derived Neurotrophic Factor Biophysical Journal. 106: 425a. DOI: 10.1016/J.Bpj.2013.11.2397 |
0.795 |
|
Show low-probability matches. |