Elisar Barbar - Publications

Affiliations: 
Ohio University, Athens, OH, United States 
Area:
Biochemistry

78 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Estelle AB, George A, Barbar EJ, Zuckerman DM. Quantifying cooperative multisite binding in the hub protein LC8 through Bayesian inference. Plos Computational Biology. 19: e1011059. PMID 37083599 DOI: 10.1371/journal.pcbi.1011059  0.439
2023 Walker DR, Jara KA, Rolland AD, Brooks C, Hare W, Swansiger AK, Reardon PN, Prell JS, Barbar EJ. Linker Length Drives Heterogeneity of Multivalent Complexes of Hub Protein LC8 and Transcription Factor ASCIZ. Biomolecules. 13. PMID 36979339 DOI: 10.3390/biom13030404  0.451
2023 Jara KA, Barbar EJ. NMR Analysis of the Interactions and Conformational Plasticity of Dynein Intermediate Chain. Methods in Molecular Biology (Clifton, N.J.). 2623: 241-256. PMID 36602690 DOI: 10.1007/978-1-0716-2958-1_15  0.396
2022 Jara KA, Loening NM, Reardon PN, Yu Z, Woonnimani P, Brooks C, Vesely CH, Barbar EJ. Multivalency, autoinhibition, and protein disorder in the regulation of interactions of dynein intermediate chain with dynactin and the nuclear distribution protein. Elife. 11. PMID 36416224 DOI: 10.7554/eLife.80217  0.507
2022 Howe J, Weeks A, Reardon P, Barbar E. Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1. Biophysical Journal. 121: 4433-4442. PMID 36335430 DOI: 10.1016/j.bpj.2022.11.006  0.393
2021 Rodriguez Galvan J, Donner B, Veseley CH, Reardon P, Forsythe HM, Howe J, Fujimura G, Barbar E. Human Parainfluenza Virus 3 Phosphoprotein Is a Tetramer and Shares Structural and Interaction Features with Ebola Phosphoprotein VP35. Biomolecules. 11. PMID 34827601 DOI: 10.3390/biom11111603  0.318
2021 Forsythe HM, Barbar E. The role of dancing duplexes in biology and disease. Progress in Molecular Biology and Translational Science. 183: 249-270. PMID 34656330 DOI: 10.1016/bs.pmbts.2021.06.004  0.429
2021 Morgan JL, Yeager A, Estelle AB, Gsponer J, Barbar E. Transient Tertiary Structures of Disordered Dynein Intermediate Chain Regulate its Interactions with Multiple Partners. Journal of Molecular Biology. 433: 167152. PMID 34273400 DOI: 10.1016/j.jmb.2021.167152  0.48
2021 Forsythe HM, Galvan JR, Yu Z, Pinckney S, Reardon P, Cooley RB, Zhu P, Rolland AD, Prell JS, Barbar E. Multivalent binding of the partially disordered SARS-CoV-2 nucleocapsid phosphoprotein dimer to RNA. Biophysical Journal. PMID 33794152 DOI: 10.1016/j.bpj.2021.03.023  0.366
2021 Loening NM, Barbar E. Structural characterization of the self-association domain of swallow. Protein Science : a Publication of the Protein Society. PMID 33641207 DOI: 10.1002/pro.4055  0.388
2020 Loening NM, Saravanan S, Jespersen NE, Jara K, Barbar E. Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes. Biophysical Journal. 119: 950-965. PMID 32814057 DOI: 10.1016/J.Bpj.2020.07.023  0.523
2020 Jespersen N, Barbar E. Emerging Features of Linear Motif-Binding Hub Proteins: (Trends in Biochemical Sciences, 45, 375-3849, 2020). Trends in Biochemical Sciences. PMID 32601043 DOI: 10.1016/J.Tibs.2020.06.002  0.439
2020 Jespersen N, Barbar E. Emerging Features of Linear Motif-Binding Hub Proteins. Trends in Biochemical Sciences. 45: 375-384. PMID 32311332 DOI: 10.1016/J.Tibs.2020.01.004  0.539
2020 Reardon PN, Jara KA, Rolland AD, Smith DA, Hoang HTM, Prell JS, Barbar EJ. The dynein light chain 8 (LC8) binds "in-register" to multivalent intrinsically disordered partners. The Journal of Biological Chemistry. PMID 32139510 DOI: 10.1074/Jbc.Ra119.011653  0.502
2019 Jespersen NE, Leyrat C, Gérard FC, Bourhis JM, Blondel D, Jamin M, Barbar E. The LC8-RavP ensemble structure evinces a role for LC8 in regulating Lyssavirus polymerase functionality. Journal of Molecular Biology. PMID 31634467 DOI: 10.1016/J.Jmb.2019.10.011  0.462
2019 Jespersen N, Estelle A, Waugh N, Davey NE, Blikstad C, Ammon YC, Akhmanova A, Ivarsson Y, Hendrix DA, Barbar E. Systematic identification of recognition motifs for the hub protein LC8. Life Science Alliance. 2. PMID 31266884 DOI: 10.26508/lsa.201900366  0.394
2018 Clark SA, Myers JB, King A, Fiala R, Novacek J, Pearce FG, Heierhorst J, Reichow SL, Barbar EJ. Multivalency regulates activity in an intrinsically disordered transcription factor. Elife. 7. PMID 29714690 DOI: 10.7554/Elife.36258  0.326
2017 Morgan J, Jensen MR, Ozenne V, Blackledge M, Barbar EJ. The LC8 Recognition Motif Preferentially Samples Polyproline II Structure in its Free State. Biochemistry. PMID 28792212 DOI: 10.1021/Acs.Biochem.7B00552  0.604
2017 Jie J, Löhr F, Barbar E. Dynein Binding of Competitive Regulators Dynactin and NudE Involves Novel Interplay between Phosphorylation Site and Disordered Spliced Linkers. Structure (London, England : 1993). PMID 28162951 DOI: 10.1016/J.Str.2017.01.003  0.508
2016 Clark S, Nyarko A, Löhr F, Karplus PA, Barbar E. The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex. Biochemistry. 55: 199-209. PMID 26652654 DOI: 10.1021/Acs.Biochem.5B01099  0.791
2016 Jie J, Barbar E. Regulation of Mammalian Dynein Intermediate Chain Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.1929  0.602
2015 Jie J, Löhr F, Barbar E. Interactions of Yeast Dynein with Dynein Light Chain and Dynactin: GENERAL IMPLICATIONS FOR INTRINSICALLY DISORDERED DUPLEX SCAFFOLDS IN MULTIPROTEIN ASSEMBLIES. The Journal of Biological Chemistry. 290: 23863-74. PMID 26253171 DOI: 10.1074/Jbc.M115.649715  0.611
2015 Clark SA, Jespersen N, Woodward C, Barbar E. Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds. Febs Letters. 589: 2543-51. PMID 26226419 DOI: 10.1016/J.Febslet.2015.07.032  0.58
2015 Baßler J, Paternoga H, Holdermann I, Thoms M, Granneman S, Barrio-Garcia C, Nyarko A, Lee W, Stier G, Clark SA, Schraivogel D, Kallas M, Beckmann R, Tollervey D, Barbar E, et al. A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. The Journal of Cell Biology. 210: 169-70. PMID 26150393 DOI: 10.1083/jcb.20140811106112015c  0.67
2015 Lampi KJ, Murray MR, Peterson MP, Eng BS, Yue E, Clark AR, Barbar E, David LL. Differences in solution dynamics between lens β-crystallin homodimers and heterodimers probed by hydrogen-deuterium exchange and deamidation. Biochimica Et Biophysica Acta. PMID 26145577 DOI: 10.1016/J.Bbagen.2015.06.014  0.375
2015 Gaik M, Flemming D, von Appen A, Kastritis P, Mücke N, Fischer J, Stelter P, Ori A, Bui KH, Baßler J, Barbar E, Beck M, Hurt E. Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold. The Journal of Cell Biology. 208: 283-97. PMID 25646085 DOI: 10.1083/Jcb.201411003  0.38
2015 Barbar E, Nyarko A. Polybivalency and disordered proteins in ordering macromolecular assemblies. Seminars in Cell & Developmental Biology. 37: 20-5. PMID 25263009 DOI: 10.1016/J.Semcdb.2014.09.016  0.794
2015 Jie J, Barbar E. Protein Disorder in Dynein Regulation by Dynactin and NudE Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.2124  0.596
2014 Bassler J, Paternoga H, Holdermann I, Thoms M, Granneman S, Barrio-Garcia C, Nyarko A, Stier G, Clark SA, Schraivogel D, Kallas M, Beckmann R, Tollervey D, Barbar E, Sinning I, et al. A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation. The Journal of Cell Biology. 207: 481-98. PMID 25404745 DOI: 10.1083/Jcb.201408111  0.741
2014 Nyarko A, Singarapu KK, Figueroa M, Manning VA, Pandelova I, Wolpert TJ, Ciuffetti LM, Barbar E. Solution NMR structures of Pyrenophora tritici-repentis ToxB and its inactive homolog reveal potential determinants of toxin activity. The Journal of Biological Chemistry. 289: 25946-56. PMID 25063993 DOI: 10.1074/Jbc.M114.569103  0.729
2014 Barbar E, Nyarko A. NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein. Computational and Structural Biotechnology Journal. 9: e201402003. PMID 24757501 DOI: 10.5936/Csbj.201402003  0.797
2014 Jie J, Barbar E. Structural Basis of Multiple Sequential LC8 Sites: Insights from Interactions of Lc8 with Pac11 Biophysical Journal. 106: 6-8. DOI: 10.1016/J.Bpj.2013.11.3807  0.622
2014 Nyarko A, Song Y, Barbar E. Multiple Recognition Motifs Provide Rigidity to Stabilize LC8 Complexes Biophysical Journal. 106. DOI: 10.1016/J.Bpj.2013.11.3795  0.788
2013 Kidane AI, Song Y, Nyarko A, Hall J, Hare M, Löhr F, Barbar E. Structural features of LC8-induced self-association of swallow. Biochemistry. 52: 6011-20. PMID 23914803 DOI: 10.1021/Bi400642U  0.781
2013 Nyarko A, Song Y, Nováček J, Žídek L, Barbar E. Multiple recognition motifs in nucleoporin Nup159 provide a stable and rigid Nup159-Dyn2 assembly. The Journal of Biological Chemistry. 288: 2614-22. PMID 23223634 DOI: 10.1074/Jbc.M112.432831  0.806
2013 Barbar E. Intrinsic Protein Disorder in the Regulation of Large Molecular Machines Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.052  0.508
2012 Barbar E. Native disorder mediates binding of dynein to NudE and dynactin. Biochemical Society Transactions. 40: 1009-13. PMID 22988856 DOI: 10.1042/Bst20120180  0.481
2012 Nyarko A, Song Y, Barbar E. Intrinsic disorder in dynein intermediate chain modulates its interactions with NudE and dynactin. The Journal of Biological Chemistry. 287: 24884-93. PMID 22669947 DOI: 10.1074/Jbc.M112.376038  0.802
2012 Powell JD, Barbar E, Dreher TW. Turnip yellow mosaic virus forms infectious particles without the native beta-annulus structure and flexible coat protein N-terminus Virology. 422: 165-173. PMID 22078163 DOI: 10.1016/J.Virol.2011.10.019  0.312
2011 Morgan JL, Song Y, Barbar E. Structural dynamics and multiregion interactions in dynein-dynactin recognition. The Journal of Biological Chemistry. 286: 39349-59. PMID 21931160 DOI: 10.1074/Jbc.M111.296277  0.587
2011 Nyarko A, Hall J, Hall A, Hare M, Kremerskothen J, Barbar E. Conformational dynamics promote binding diversity of dynein light chain LC8. Biophysical Chemistry. 159: 41-7. PMID 21621319 DOI: 10.1016/J.Bpc.2011.05.001  0.784
2011 Nyarko A, Barbar E. Light chain-dependent self-association of dynein intermediate chain. The Journal of Biological Chemistry. 286: 1556-66. PMID 20974845 DOI: 10.1074/Jbc.M110.171686  0.794
2010 Hall J, Song Y, Karplus PA, Barbar E. The crystal structure of dynein intermediate chain-light chain roadblock complex gives new insights into dynein assembly. The Journal of Biological Chemistry. 285: 22566-75. PMID 20472935 DOI: 10.1074/Jbc.M110.103861  0.546
2010 Nyarko A, Barbar E. Light Chain-Mediated Self-Association of Intrinsically Disordered Dynein Intermediate Chain Biophysical Journal. 98. DOI: 10.1016/J.Bpj.2009.12.3578  0.807
2009 Benison G, Chiodo M, Karplus PA, Barbar E. Structural, thermodynamic, and kinetic effects of a phosphomimetic mutation in dynein light chain LC8. Biochemistry. 48: 11381-9. PMID 19863079 DOI: 10.1021/Bi901589W  0.494
2009 Hall J, Karplus PA, Barbar E. Multivalency in the assembly of intrinsically disordered Dynein intermediate chain. The Journal of Biological Chemistry. 284: 33115-21. PMID 19759397 DOI: 10.1074/Jbc.M109.048587  0.549
2009 Hall A, Parsonage D, Horita D, Karplus PA, Poole LB, Barbar E. Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds. Biochemistry. 48: 5984-93. PMID 19459661 DOI: 10.1021/Bi900270W  0.362
2009 Benison G, Barbar E. NMR analysis of dynein light chain dimerization and interactions with diverse ligands. Methods in Enzymology. 455: 237-58. PMID 19289209 DOI: 10.1016/S0076-6879(08)04209-2  0.559
2009 Barbar E, Hall J, Benison G, Karplus PA, Nyarko A. Mechanisms Underlying the Binding Diversity of Dynein Light Chain Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.2876  0.818
2008 Benison G, Karplus PA, Barbar E. The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8. Journal of Molecular Biology. 384: 954-66. PMID 18948118 DOI: 10.1016/J.Jmb.2008.09.083  0.545
2008 Hall J, Hall A, Pursifull N, Barbar E. Differences in dynamic structure of LC8 monomer, dimer, and dimer-peptide complexes. Biochemistry. 47: 11940-52. PMID 18942858 DOI: 10.1021/Bi801093K  0.539
2008 Barbar E. Dynein light chain LC8 is a dimerization hub essential in diverse protein networks. Biochemistry. 47: 503-8. PMID 18092820 DOI: 10.1021/Bi701995M  0.444
2007 Benison G, Karplus PA, Barbar E. Structure and dynamics of LC8 complexes with KXTQT-motif peptides: swallow and dynein intermediate chain compete for a common site. Journal of Molecular Biology. 371: 457-68. PMID 17570393 DOI: 10.1016/J.Jmb.2007.05.046  0.601
2007 Song Y, Benison G, Nyarko A, Hays TS, Barbar E. Potential role for phosphorylation in differential regulation of the assembly of dynein light chains. The Journal of Biological Chemistry. 282: 17272-9. PMID 17428790 DOI: 10.1074/Jbc.M610445200  0.791
2006 Benison G, Nyarko A, Barbar E. Heteronuclear NMR identifies a nascent helix in intrinsically disordered dynein intermediate chain: implications for folding and dimerization. Journal of Molecular Biology. 362: 1082-93. PMID 16949604 DOI: 10.1016/J.Jmb.2006.08.006  0.8
2006 Talbott M, Hare M, Nyarko A, Hays TS, Barbar E. Folding is coupled to dimerization of Tctex-1 dynein light chain. Biochemistry. 45: 6793-800. PMID 16734416 DOI: 10.1021/Bi0600345  0.72
2005 Nyarko A, Cochrun L, Norwood S, Pursifull N, Voth A, Barbar E. Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation Biochemistry. 44: 14248-14255. PMID 16245941 DOI: 10.1021/Bi0512694  0.744
2004 Nyarko A, Hare M, Hays TS, Barbar E. The intermediate chain of cytoplasmic dynein is partially disordered and gains structure upon binding to light-chain LC8. Biochemistry. 43: 15595-603. PMID 15581372 DOI: 10.1021/Bi048451+  0.807
2004 Wang L, Hare M, Hays TS, Barbar E. Dynein light chain LC8 promotes assembly of the coiled-coil domain of swallow protein. Biochemistry. 43: 4611-20. PMID 15078108 DOI: 10.1021/Bi036328X  0.498
2004 Barbar E, Hare M. Characterization of the cargo attachment complex of cytoplasmic dynein using NMR and mass spectrometry. Methods in Enzymology. 380: 219-41. PMID 15051340 DOI: 10.1016/S0076-6879(04)80011-9  0.316
2004 Makokha M, Huang YJ, Montelione G, Edison AS, Barbar E. The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila Protein Science. 13: 727-734. PMID 14767079 DOI: 10.1110/Ps.03462204  0.418
2003 Nyarko A, Hare M, Makokha M, Barbar E. Interactions of LC8 with N-terminal segments of the intermediate chain of cytoplasmic dynein. Thescientificworldjournal. 3: 647-54. PMID 12920307 DOI: 10.1100/Tsw.2003.56  0.796
2002 Barbar E, Makokha M, Hare M. Protein Interactions Within the Cytoplasmic Dynein Complex as Probed by Mass Spectrometry and Nmr. Thescientificworldjournal. 2: 95-96. PMID 29973819 DOI: 10.1100/Tsw.2002.45  0.6
2002 Makokha M, Hare M, Li M, Hays T, Barbar E. Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74. Biochemistry. 41: 4302-11. PMID 11914076 DOI: 10.1021/Bi011970H  0.527
2001 Barbar E, Hare M, Makokha M, Barany G, Woodward C. NMR-detected order in core residues of denatured bovine pancreatic trypsin inhibitor. Biochemistry. 40: 9734-42. PMID 11583174 DOI: 10.1021/Bi010483Z  0.385
2001 Woodward C, Barbar E, Carulla N, Battiste J, Barany G. Experimental approaches to protein folding based on the concept of a slow hydrogen exchange core. Journal of Molecular Graphics & Modelling. 19: 94-101. PMID 11381535 DOI: 10.1016/S1093-3263(00)00131-5  0.383
2001 Barbar E, Kleinman B, Imhoff D, Li M, Hays TS, Hare M. Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein Biochemistry. 40: 1596-1605. PMID 11327818 DOI: 10.1021/Bi002278+  0.458
1999 Barbar E. NMR characterization of partially folded and unfolded conformational ensembles of proteins. Biopolymers. 51: 191-207. PMID 10516571 DOI: 10.1002/(Sici)1097-0282(1999)51:3<191::Aid-Bip3>3.0.Co;2-B  0.439
1998 Barbar E, Hare M, Daragan V, Barany G, Woodward C. Dynamics of the conformational ensemble of partially folded bovine pancreatic trypsin inhibitor. Biochemistry. 37: 7822-33. PMID 9601043 DOI: 10.1021/Bi973102J  0.387
1997 Barbar E, Gross CM, Woodward C, Barany G. Chemical synthesis and nuclear magnetic resonance characterization of partially folded proteins. Methods in Enzymology. 289: 587-611. PMID 9353740 DOI: 10.1016/S0076-6879(97)89066-0  0.351
1997 Barbar E, LiCata VJ, Barany G, Woodward C. Local fluctuations and global unfolding of partially folded BPTI detected by NMR. Biophysical Chemistry. 64: 45-57. PMID 9127937 DOI: 10.1016/S0301-4622(96)02210-7  0.375
1996 Barbar E, Barany G, Woodward C. Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink. Folding & Design. 1: 65-76. PMID 9079365 DOI: 10.1016/S1359-0278(96)00013-2  0.39
1996 Barbar E, Martin TM, Brown M, Rittenberg MB, Peyton DH. Binding of phenylphosphocholine-carrier conjugates to the combining site of antibodies maintains a conformation of the hapten Biochemistry. 35: 2958-2967. PMID 8608133 DOI: 10.1021/Bi950823E  0.453
1996 Barany G, Gross CM, Ferrer M, Barbar E, Pan H, Woodward C. Optimized methods for chemical synthesis of bovine pancreatic trypsin inhibitor (BPTI) analogues Techniques in Protein Chemistry. 7: 503-514. DOI: 10.1016/S1080-8914(96)80055-X  0.347
1995 Breslow E, Sardana V, Deeb R, Barbar E, Peyton DH. NMR behavior of the aromatic protons of bovine neurophysin-I and its peptide complexes: Implications for solution structure and for function Biochemistry. 34: 2137-2147. PMID 7857924 DOI: 10.1021/Bi00007A006  0.489
1995 Pan H, Barbar E, Barany G, Woodward C. Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor. Biochemistry. 34: 13974-81. PMID 7577994 DOI: 10.1021/Bi00043A002  0.423
1995 Barbar E, Barany G, Woodward C. Dynamic structure of a highly ordered beta-sheet molten globule: multiple conformations with a stable core. Biochemistry. 34: 11423-434. PMID 7547870 DOI: 10.1021/Bi00036A015  0.388
1992 Bruderer U, Peyton DH, Barbar E, Fellman JH, Rittenberg MB. Hapten conformation in the combining site of antibodies that bind phenylphosphocholine. Biochemistry. 31: 584-9. PMID 1731913 DOI: 10.1021/Bi00117A040  0.409
Show low-probability matches.