| Year |
Citation |
Score |
| 2018 |
Kulkarni P, Solomon T, He Y, Chen Y, Bryan PN, Orban J. Structural metamorphism and polymorphism in proteins on the brink of thermodynamic stability. Protein Science : a Publication of the Protein Society. PMID 30144197 DOI: 10.1002/Pro.3458 |
0.369 |
|
| 2018 |
Rangarajan S, He Y, Chen Y, Kerzic MC, Ma B, Gowthaman R, Pierce BG, Nussinov R, Mariuzza RA, Orban J. Peptide-MHC (pMHC) binding to a human antiviral T cell receptor induces long-range allosteric communication between pMHC- and CD3-binding sites. The Journal of Biological Chemistry. PMID 30135211 DOI: 10.1074/Jbc.Ra118.003832 |
0.306 |
|
| 2018 |
Lin X, Roy S, Jolly MK, Bocci F, Schafer NP, Tsai MY, Chen Y, He Y, Grishaev A, Weninger K, Orban J, Kulkarni P, Rangarajan G, Levine H, Onuchic JN. PAGE4 and Conformational Switching: Insights from Molecular Dynamics Simulations and Implications for Prostate Cancer. Journal of Molecular Biology. PMID 29758263 DOI: 10.1016/J.Jmb.2018.05.011 |
0.313 |
|
| 2017 |
Kulkarni P, Jolly MK, Jia D, Mooney SM, Bhargava A, Kagohara LT, Chen Y, Hao P, He Y, Veltri RW, Grishaev A, Weninger K, Levine H, Orban J. Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity. Proceedings of the National Academy of Sciences of the United States of America. PMID 28289210 DOI: 10.1073/Pnas.1700082114 |
0.314 |
|
| 2015 |
He Y, Chen Y, Mooney SM, Rajagopalan K, Bhargava A, Sacho E, Weninger K, Bryan PN, Kulkarni P, Orban J. Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen. The Journal of Biological Chemistry. 290: 25090-102. PMID 26242913 DOI: 10.1074/Jbc.M115.658583 |
0.355 |
|
| 2015 |
Porter LL, He Y, Chen Y, Orban J, Bryan PN. Subdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds. Biophysical Journal. 108: 154-62. PMID 25564862 DOI: 10.1016/J.Bpj.2014.10.073 |
0.372 |
|
| 2015 |
Porter LL, He Y, Chen Y, Orban J, Bryan PN. Protein Evolution across Fold Classes: A 3-α-Helix Bundle can Switch to β, α/β, and α+β Folds by Stepwise Mutation Biophysical Journal. 108: 203a-204a. DOI: 10.1016/J.Bpj.2014.11.1125 |
0.304 |
|
| 2013 |
Klein SL, Neilson KM, Orban J, Yaklichkin S, Hoffbauer J, Mood K, Daar IO, Moody SA. Conserved structural domains in FoxD4L1, a neural forkhead box transcription factor, are required to repress or activate target genes. Plos One. 8: e61845. PMID 23610594 DOI: 10.1371/Journal.Pone.0061845 |
0.402 |
|
| 2013 |
Bryan PN, Orban J. Implications of protein fold switching. Current Opinion in Structural Biology. 23: 314-6. PMID 23518177 DOI: 10.1016/J.Sbi.2013.03.001 |
0.312 |
|
| 2012 |
He Y, Chen Y, Oganesyan N, Ruan B, O'Brochta D, Bryan PN, Orban J. Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum. Proteins. 80: 2810-7. PMID 23011838 DOI: 10.1002/Prot.24187 |
0.397 |
|
| 2012 |
He Y, Chen Y, Alexander PA, Bryan PN, Orban J. Mutational tipping points for switching protein folds and functions. Structure (London, England : 1993). 20: 283-91. PMID 22325777 DOI: 10.1016/J.Str.2011.11.018 |
0.35 |
|
| 2012 |
He Y, Chen Y, Alexander P, Bryan P, Orban J. GB98 solution structure Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Lhd/Pdb |
0.301 |
|
| 2011 |
Chen Y, Apolinario E, Brachova L, Kelman Z, Li Z, Nikolau BJ, Showman L, Sowers K, Orban J. A nuclear magnetic resonance based approach to accurate functional annotation of putative enzymes in the methanogen Methanosarcina acetivorans. Bmc Genomics. 12: S7. PMID 21810209 DOI: 10.1186/1471-2164-12-S1-S7 |
0.336 |
|
| 2011 |
Zeng Y, He Y, Yang F, Mooney SM, Getzenberg RH, Orban J, Kulkarni P. The cancer/testis antigen prostate-associated gene 4 (PAGE4) is a highly intrinsically disordered protein. The Journal of Biological Chemistry. 286: 13985-94. PMID 21357425 DOI: 10.1074/Jbc.M110.210765 |
0.337 |
|
| 2010 |
Bryan PN, Orban J. Proteins that switch folds. Current Opinion in Structural Biology. 20: 482-8. PMID 20591649 DOI: 10.1016/J.Sbi.2010.06.002 |
0.377 |
|
| 2010 |
Shen Y, Bryan PN, He Y, Orban J, Baker D, Bax A. De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds. Protein Science : a Publication of the Protein Society. 19: 349-56. PMID 19998407 DOI: 10.1002/Pro.303 |
0.437 |
|
| 2009 |
Alexander PA, He Y, Chen Y, Orban J, Bryan PN. A minimal sequence code for switching protein structure and function. Proceedings of the National Academy of Sciences of the United States of America. 106: 21149-54. PMID 19923431 DOI: 10.1073/Pnas.0906408106 |
0.418 |
|
| 2009 |
He Y, Alexander P, Chen Y, Bryan P, Orban J. NMR structures of GA95 and GB95, two designed proteins with 95% sequence identity but different folds and functions Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb2Kdl/Pdb |
0.382 |
|
| 2008 |
He Y, Chen Y, Alexander P, Bryan PN, Orban J. NMR structures of two designed proteins with high sequence identity but different fold and function. Proceedings of the National Academy of Sciences of the United States of America. 105: 14412-7. PMID 18796611 DOI: 10.1073/Pnas.0805857105 |
0.431 |
|
| 2007 |
Sari N, Fisher KE, Bryan PN, Orban J. Main chain NMR assignments of subtilisin Sbt70 in its prodomain-bound state. Biomolecular Nmr Assignments. 1: 209-11. PMID 19636867 DOI: 10.1007/S12104-007-9058-4 |
0.337 |
|
| 2007 |
Alexander PA, He Y, Chen Y, Orban J, Bryan PN. The design and characterization of two proteins with 88% sequence identity but different structure and function. Proceedings of the National Academy of Sciences of the United States of America. 104: 11963-8. PMID 17609385 DOI: 10.1073/Pnas.0700922104 |
0.469 |
|
| 2007 |
He Y, Chen Y, Rozak DA, Bryan PN, Orban J. An artificially evolved albumin binding module facilitates chemical shift epitope mapping of GA domain interactions with phylogenetically diverse albumins. Protein Science : a Publication of the Protein Society. 16: 1490-4. PMID 17567743 DOI: 10.1110/Ps.072799507 |
0.394 |
|
| 2007 |
Sari N, He Y, Doseeva V, Surabian K, Ramprakash J, Schwarz F, Herzberg O, Orban J. Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae. Protein Science : a Publication of the Protein Society. 16: 977-82. PMID 17400915 DOI: 10.1110/Ps.072820907 |
0.512 |
|
| 2007 |
Sari N, Ruan B, Fisher KE, Alexander PA, Orban J, Bryan PN. Hydrogen-deuterium exchange in free and prodomain-complexed subtilisin. Biochemistry. 46: 652-8. PMID 17223687 DOI: 10.1021/Bi061601R |
0.403 |
|
| 2006 |
He Y, Rozak DA, Sari N, Chen Y, Bryan P, Orban J. Structure, dynamics, and stability variation in bacterial albumin binding modules: implications for species specificity. Biochemistry. 45: 10102-9. PMID 16906768 DOI: 10.1021/Bi060409M |
0.391 |
|
| 2006 |
Rozak DA, Alexander PA, He Y, Chen Y, Orban J, Bryan PN. Using offset recombinant polymerase chain reaction to identify functional determinants in a common family of bacterial albumin binding domains. Biochemistry. 45: 3263-71. PMID 16519521 DOI: 10.1021/Bi051926S |
0.361 |
|
| 2006 |
Parsons LM, Lin F, Orban J. Peptidoglycan recognition by Pal, an outer membrane lipoprotein. Biochemistry. 45: 2122-8. PMID 16475801 DOI: 10.1021/Bi052227I |
0.604 |
|
| 2005 |
Sari N, Yeh DC, Doseeva V, Surabian K, Herzberg O, Orban J. NMR assignment of HI1506, a novel two-domain protein from Haemophilus influenzae. Journal of Biomolecular Nmr. 33: 281. PMID 16341755 DOI: 10.1007/S10858-005-3869-3 |
0.402 |
|
| 2005 |
Rozak DA, Orban J, Bryan PN. G148-GA3: a streptococcal virulence module with atypical thermodynamics of folding optimally binds human serum albumin at physiological temperatures. Biochimica Et Biophysica Acta. 1753: 226-33. PMID 16290081 DOI: 10.1016/J.Bbapap.2005.10.005 |
0.377 |
|
| 2005 |
He Y, Yeh DC, Alexander P, Bryan PN, Orban J. Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds. Biochemistry. 44: 14055-61. PMID 16245921 DOI: 10.1021/Bi051232J |
0.456 |
|
| 2005 |
Alexander PA, Rozak DA, Orban J, Bryan PN. Directed evolution of highly homologous proteins with different folds by phage display: implications for the protein folding code. Biochemistry. 44: 14045-54. PMID 16245920 DOI: 10.1021/Bi051231R |
0.456 |
|
| 2005 |
Parsons LM, Orban J. NMR assignment of the periplasmic domain of peptidoglycan-associated lipoprotein (Pal) from Haemophilus influenzae. Journal of Biomolecular Nmr. 32: 93. PMID 16041489 DOI: 10.1007/S10858-005-3676-X |
0.581 |
|
| 2005 |
Parsons LM, Liu F, Orban J. HU-alpha binds to the putative double-stranded DNA mimic HI1450 from Haemophilus influenzae. Protein Science : a Publication of the Protein Society. 14: 1684-7. PMID 15883182 DOI: 10.1110/Ps.041275705 |
0.628 |
|
| 2005 |
Yeh DC, Parsons LM, Parsons JF, Liu F, Eisenstein E, Orban J. NMR structure of HI0004, a putative essential gene product from Haemophilus influenzae, and comparison with the X-ray structure of an Aquifex aeolicus homolog. Protein Science : a Publication of the Protein Society. 14: 424-30. PMID 15632286 DOI: 10.1110/Ps.041096705 |
0.625 |
|
| 2004 |
Cheon Yeh D, Parsons JF, Parsons LM, Liu F, Eisenstein E, Orban J. NMR assignment of the hypothetical protein HI0004 from Haemophilus influenzae--a putative essential gene product. Journal of Biomolecular Nmr. 29: 101-2. PMID 15017148 DOI: 10.1023/B:Jnmr.0000019469.77977.72 |
0.57 |
|
| 2004 |
Parsons L, Orban J. Structural genomics and the metabolome: combining computational and NMR methods to identify target ligands. Current Opinion in Drug Discovery & Development. 7: 62-8. PMID 14982149 |
0.586 |
|
| 2004 |
Parsons LM, Yeh DC, Orban J. Solution structure of the highly acidic protein HI1450 from Haemophilus influenzae, a putative double-stranded DNA mimic. Proteins. 54: 375-83. PMID 14747986 DOI: 10.1002/Prot.10607 |
0.603 |
|
| 2004 |
Yeh D, Orban J. 1H, 13C, 15N resonance assignment of hypothetical protein hi1723 from Haemophilus Influenzae Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5963 |
0.312 |
|
| 2004 |
Parsons L, Liu F, Yeh DC, Sari N, Orban J. Integrating structural and functional genomics Australian Journal of Chemistry. 57: 619-623. DOI: 10.1071/Ch04024 |
0.605 |
|
| 2003 |
Parsons L, Bonander N, Eisenstein E, Gilson M, Kairys V, Orban J. Solution structure and functional ligand screening of HI0719, a highly conserved protein from bacteria to humans in the YjgF/YER057c/UK114 family. Biochemistry. 42: 80-9. PMID 12515541 DOI: 10.1021/Bi020541W |
0.634 |
|
| 2003 |
Parsons L, Orban J. 1H 13C and 15N chemical shift assignments for HI0719 Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr5606 |
0.529 |
|
| 2002 |
Gilliland GL, Teplyakov A, Obmolova G, Tordova M, Thanki N, Ladner J, Herzberg O, Lim K, Zhang H, Huang K, Li Z, Tempczyk A, Krajewski W, Parsons L, Yeh DC, ... Orban J, et al. Assisting functional assignment for hypothetical Heamophilus influenzae gene products through structural genomics Current Drug Targets - Infectious Disorders. 2: 339-353. PMID 12570740 DOI: 10.2174/1568005023342281 |
0.613 |
|
| 2002 |
Tangrea MA, Bryan PN, Sari N, Orban J. Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus. Journal of Molecular Biology. 320: 801-12. PMID 12095256 DOI: 10.1016/S0022-2836(02)00543-0 |
0.696 |
|
| 2001 |
Parsons L, Eisenstein E, Orban J. Solution structure of HI0257, a bacterial ribosome binding protein. Biochemistry. 40: 10979-86. PMID 11551193 DOI: 10.1021/Bi011077I |
0.64 |
|
| 2001 |
Tangrea MA, Alexander P, Bryan PN, Eisenstein E, Toedt J, Orban J. Stability and global fold of the mouse prohormone convertase 1 pro-domain. Biochemistry. 40: 5488-95. PMID 11331013 DOI: 10.1021/Bi0026472 |
0.689 |
|
| 2000 |
Sari N, Alexander P, Bryan PN, Orban J. Structure and dynamics of an acid-denatured protein G mutant. Biochemistry. 39: 965-77. PMID 10653640 DOI: 10.1021/Bi9920230 |
0.389 |
|
| 1999 |
Khare D, Alexander P, Orban J. Hydrogen bonding and equilibrium protium-deuterium fractionation factors in the immunoglobulin G binding domain of protein G. Biochemistry. 38: 3918-25. PMID 10194303 DOI: 10.1021/Bi9827114 |
0.323 |
|
| 1997 |
Khare D, Alexander P, Antosiewicz J, Bryan P, Gilson M, Orban J. pK(a) measurements from nuclear magnetic resonance for the B1 and B2 immunoglobulin G-binding domains of protein G: Comparison with calculated values for nuclear magnetic resonance and x-ray structures Biochemistry. 36: 3580-3589. PMID 9132009 DOI: 10.1021/Bi9630927 |
0.387 |
|
| 1995 |
Orban J, Alexander P, Bryan P, Khare D. Assessment of stability differences in the protein G B1 and B2 domains from hydrogen-deuterium exchange: Comparison with calorimetric data Biochemistry. 34: 15291-15300. PMID 7578145 DOI: 10.1021/Bi00046A038 |
0.308 |
|
| 1994 |
Orban J, Alexander P, Bryan P. Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B-domain Biochemistry. 33: 5702-5710. PMID 8180196 DOI: 10.1021/Bi00185A006 |
0.35 |
|
| 1992 |
Alexander P, Fahnestock S, Lee T, Orban J, Bryan P. Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures Biochemistry®. 31: 3597-3603. PMID 1567818 DOI: 10.1021/Bi00129A007 |
0.383 |
|
| 1992 |
Alexander P, Orban J, Bryan P. Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G. Biochemistry. 31: 7243-8. PMID 1510916 DOI: 10.1021/Bi00147A006 |
0.348 |
|
| 1992 |
Orban J, Alexander P, Bryan P. Sequence-specific 1H NMR assignments and secondary structure of the streptococcal protein G B2-domain Biochemistry®. 31: 3604-3611. PMID 1314644 DOI: 10.1021/Bi00129A008 |
0.417 |
|
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