| Year |
Citation |
Score |
| 2022 |
Rudden LSP, Hijazi M, Barth P. Deep learning approaches for conformational flexibility and switching properties in protein design. Frontiers in Molecular Biosciences. 9: 928534. PMID 36032687 DOI: 10.3389/fmolb.2022.928534 |
0.33 |
|
| 2020 |
Yin J, Chen KM, Clark MJ, Hijazi M, Kumari P, Bai XC, Sunahara RK, Barth P, Rosenbaum DM. Structure of a D2 dopamine receptor-G-protein complex in a lipid membrane. Nature. PMID 32528175 DOI: 10.1038/S41586-020-2379-5 |
0.305 |
|
| 2020 |
Leman JK, Weitzner BD, Lewis SM, Adolf-Bryfogle J, Alam N, Alford RF, Aprahamian M, Baker D, Barlow KA, Barth P, Basanta B, Bender BJ, Blacklock K, Bonet J, Boyken SE, et al. Macromolecular modeling and design in Rosetta: recent methods and frameworks. Nature Methods. PMID 32483333 DOI: 10.1038/S41592-020-0848-2 |
0.318 |
|
| 2020 |
Chen KM, Keri D, Barth P. Computational design of G Protein-Coupled Receptor allosteric signal transductions. Nature Chemical Biology. 16: 77-86. PMID 31792443 DOI: 10.1038/S41589-019-0407-2 |
0.353 |
|
| 2018 |
Keri D, Barth P. Reprogramming G protein coupled receptor structure and function. Current Opinion in Structural Biology. 51: 187-194. PMID 30055347 DOI: 10.1016/J.Sbi.2018.07.008 |
0.333 |
|
| 2018 |
Young M, Dahoun T, Sokrat B, Arber C, Chen KM, Bouvier M, Barth P. Computational design of orthogonal membrane receptor-effector switches for rewiring signaling pathways. Proceedings of the National Academy of Sciences of the United States of America. PMID 29915030 DOI: 10.1073/Pnas.1718489115 |
0.334 |
|
| 2017 |
Lai JK, Ambia J, Wang Y, Barth P. Enhancing Structure Prediction and Design of Soluble and Membrane Proteins with Explicit Solvent-Protein Interactions. Structure (London, England : 1993). PMID 28966016 DOI: 10.1016/J.Str.2017.09.002 |
0.385 |
|
| 2017 |
Arber C, Young M, Barth P. Reprogramming cellular functions with engineered membrane proteins. Current Opinion in Biotechnology. 47: 92-101. PMID 28709113 DOI: 10.1016/J.Copbio.2017.06.009 |
0.365 |
|
| 2017 |
Feng X, Ambia J, Chen KM, Young M, Barth P. Computational design of ligand-binding membrane receptors with high selectivity. Nature Chemical Biology. PMID 28459439 DOI: 10.1038/Nchembio.2371 |
0.355 |
|
| 2016 |
Barth P, Senes A. Toward high-resolution computational design of the structure and function of helical membrane proteins. Nature Structural & Molecular Biology. 23: 475-80. PMID 27273630 DOI: 10.1038/Nsmb.3231 |
0.393 |
|
| 2016 |
Basanta B, Chan KK, Barth P, King T, Hinshaw JR, Sosnick TR, Liu G, Everett J, Xiao R, Montelione GT, Baker D. Introduction of a polar core into the de novo designed protein Top7. Protein Science : a Publication of the Protein Society. PMID 26873166 DOI: 10.1002/Pro.2899 |
0.461 |
|
| 2016 |
Feng X, Barth P. A topological and conformational stability alphabet for multipass membrane proteins. Nature Chemical Biology. PMID 26780406 DOI: 10.1038/Nchembio.2001 |
0.321 |
|
| 2016 |
Barth P. Uncovering and Reprogramming G Protein Coupled Receptor Signaling Biophysical Journal. 110: 21a. DOI: 10.1016/J.Bpj.2015.11.175 |
0.349 |
|
| 2015 |
Wang Y, Barth P. Evolutionary-guided de novo structure prediction of self-associated transmembrane helical proteins with near-atomic accuracy. Nature Communications. 6: 7196. PMID 25995083 DOI: 10.1038/Ncomms8196 |
0.366 |
|
| 2014 |
Chen KY, Sun J, Salvo JS, Baker D, Barth P. High-resolution modeling of transmembrane helical protein structures from distant homologues. Plos Computational Biology. 10: e1003636. PMID 24854015 DOI: 10.1371/Journal.Pcbi.1003636 |
0.517 |
|
| 2012 |
Chen KY, Zhou F, Fryszczyn BG, Barth P. Naturally evolved G protein-coupled receptors adopt metastable conformations. Proceedings of the National Academy of Sciences of the United States of America. 109: 13284-9. PMID 22847407 DOI: 10.1073/Pnas.1205512109 |
0.333 |
|
| 2009 |
Zhu J, Luo BH, Barth P, Schonbrun J, Baker D, Springer TA. The structure of a receptor with two associating transmembrane domains on the cell surface: integrin alphaIIbbeta3. Molecular Cell. 34: 234-49. PMID 19394300 DOI: 10.1016/J.Molcel.2009.02.022 |
0.383 |
|
| 2009 |
Barth P, Wallner B, Baker D. Prediction of membrane protein structures with complex topologies using limited constraints. Proceedings of the National Academy of Sciences of the United States of America. 106: 1409-14. PMID 19190187 DOI: 10.1073/Pnas.0808323106 |
0.6 |
|
| 2008 |
Barth P, Schoeffler A, Alber T. Targeting metastable coiled-coil domains by computational design. Journal of the American Chemical Society. 130: 12038-44. PMID 18698842 DOI: 10.1021/Ja802447E |
0.422 |
|
| 2007 |
Barth P, Schonbrun J, Baker D. Toward high-resolution prediction and design of transmembrane helical protein structures. Proceedings of the National Academy of Sciences of the United States of America. 104: 15682-7. PMID 17905872 DOI: 10.1073/Pnas.0702515104 |
0.491 |
|
| 2007 |
Barth P. Modulating membrane protein stability and association by design. Current Opinion in Structural Biology. 17: 460-6. PMID 17870471 DOI: 10.1016/J.Sbi.2007.08.006 |
0.369 |
|
| 2007 |
Barth P, Alber T, Harbury PB. Accurate, conformation-dependent predictions of solvent effects on protein ionization constants. Proceedings of the National Academy of Sciences of the United States of America. 104: 4898-903. PMID 17360348 DOI: 10.1073/Pnas.0700188104 |
0.322 |
|
| 2004 |
Howard EI, Sanishvili R, Cachau RE, Mitschler A, Chevrier B, Barth P, Lamour V, Van Zandt M, Sibley E, Bon C, Moras D, Schneider TR, Joachimiak A, Podjarny A. Ultrahigh resolution drug design I: details of interactions in human aldose reductase-inhibitor complex at 0.66 A. Proteins. 55: 792-804. PMID 15146478 DOI: 10.1002/Prot.20015 |
0.334 |
|
| 1999 |
Rogniaux H, Van Dorsselaer A, Barth P, Biellmann JF, Barbanton J, van Zandt M, Chevrier B, Howard E, Mitschler A, Potier N, Urzhumtseva L, Moras D, Podjarny A. Binding of aldose reductase inhibitors: Correlation of crystallographic and mass spectrometric studies Journal of the American Society For Mass Spectrometry. 10: 635-647. PMID 10384727 DOI: 10.1016/S1044-0305(99)00030-6 |
0.306 |
|
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