Year |
Citation |
Score |
2019 |
Langan RA, Boyken SE, Ng AH, Samson JA, Dods G, Westbrook AM, Nguyen TH, Lajoie MJ, Chen Z, Berger S, Mulligan VK, Dueber JE, Novak WRP, El-Samad H, Baker D. De novo design of bioactive protein switches. Nature. PMID 31341284 DOI: 10.1038/S41586-019-1432-8 |
0.348 |
|
2019 |
Chen Z, Boyken SE, Jia M, Busch F, Flores-Solis D, Bick MJ, Lu P, VanAernum ZL, Sahasrabuddhe A, Langan RA, Bermeo S, Brunette TJ, Mulligan VK, Carter LP, DiMaio F, et al. Programmable design of orthogonal protein heterodimers. Nature. 565: 106-111. PMID 30568301 DOI: 10.1038/s41586-018-0802-y |
0.31 |
|
2018 |
Lu P, Min D, DiMaio F, Wei KY, Vahey MD, Boyken SE, Chen Z, Fallas JA, Ueda G, Sheffler W, Mulligan VK, Xu W, Bowie JU, Baker D. Accurate computational design of multipass transmembrane proteins. Science (New York, N.Y.). 359: 1042-1046. PMID 29496880 DOI: 10.1126/Science.Aaq1739 |
0.31 |
|
2017 |
Blacklock K, Yang L, Mulligan VK, Khare SD. A Computational Method for the Design of Nested Proteins by Loop-Directed Domain Insertion. Proteins. PMID 29250820 DOI: 10.1002/Prot.25445 |
0.321 |
|
2017 |
Hosseinzadeh P, Bhardwaj G, Mulligan VK, Shortridge MD, Craven TW, Pardo-Avila F, Rettie SA, Kim DE, Silva DA, Ibrahim YM, Webb IK, Cort JR, Adkins JN, Varani G, Baker D. Comprehensive computational design of ordered peptide macrocycles. Science (New York, N.Y.). 358: 1461-1466. PMID 29242347 DOI: 10.1126/Science.Aap7577 |
0.31 |
|
2017 |
Dang B, Wu H, Mulligan VK, Mravic M, Wu Y, Lemmin T, Ford A, Silva DA, Baker D, DeGrado WF. De novo design of covalently constrained mesosize protein scaffolds with unique tertiary structures. Proceedings of the National Academy of Sciences of the United States of America. PMID 28973862 DOI: 10.1073/Pnas.1710695114 |
0.382 |
|
2017 |
Rocklin GJ, Chidyausiku TM, Goreshnik I, Ford A, Houliston S, Lemak A, Carter L, Ravichandran R, Mulligan VK, Chevalier A, Arrowsmith CH, Baker D. Global analysis of protein folding using massively parallel design, synthesis, and testing. Science (New York, N.Y.). 357: 168-175. PMID 28706065 DOI: 10.1126/Science.Aan0693 |
0.379 |
|
2017 |
Alford RF, Leaver-Fay A, Jeliazkov JR, O'Meara MJ, DiMaio FP, Park H, Shapovalov MV, Renfrew PD, Mulligan VK, Kappel K, Labonte JW, Pacella MS, Bonneau R, Bradley P, Dunbrack RL, et al. The Rosetta all-atom energy function for macromolecular modeling and design. Journal of Chemical Theory and Computation. PMID 28430426 DOI: 10.1021/Acs.Jctc.7B00125 |
0.317 |
|
2016 |
Park H, Bradley P, Greisen P, Liu Y, Mulligan VK, Kim DE, Baker D, DiMaio F. Simultaneous optimization of biomolecular energy function on features from small molecules and macromolecules. Journal of Chemical Theory and Computation. PMID 27766851 DOI: 10.1021/Acs.Jctc.6B00819 |
0.319 |
|
2013 |
Mills JH, Khare SD, Bolduc JM, Forouhar F, Mulligan VK, Lew S, Seetharaman J, Tong L, Stoddard BL, Baker D. Computational design of an unnatural amino acid dependent metalloprotein with atomic level accuracy. Journal of the American Chemical Society. 135: 13393-9. PMID 23924187 DOI: 10.1021/Ja403503M |
0.318 |
|
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 |
0.572 |
|
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 |
0.589 |
|
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 |
0.598 |
|
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 |
0.568 |
|
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 |
0.577 |
|
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 |
0.568 |
|
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 |
0.577 |
|
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 |
0.583 |
|
Show low-probability matches. |