| Year |
Citation |
Score |
| 2021 |
Chen Y, Toth EA, Ruan B, Choi EJ, Simmerman R, Chen Y, He Y, Wang R, Godoy-Ruiz R, King H, Custer G, Travis Gallagher D, Rozak DA, Solomon M, Muro S, ... ... Bryan PN, et al. Engineering subtilisin proteases that specifically degrade active RAS. Communications Biology. 4: 299. PMID 33674772 DOI: 10.1038/s42003-021-01818-7 |
0.635 |
|
| 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 |
0.343 |
|
| 2012 |
He Y, Chen Y, Alexander P, Bryan P, Orban J. Ga98 solution structure Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17839 |
0.328 |
|
| 2011 |
Morrone A, McCully ME, Bryan PN, Brunori M, Daggett V, Gianni S, Travaglini-Allocatelli C. The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function. The Journal of Biological Chemistry. 286: 3863-72. PMID 21118804 DOI: 10.1074/Jbc.M110.155911 |
0.329 |
|
| 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 |
0.308 |
|
| 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 |
0.3 |
|
| 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 |
0.428 |
|
| 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 |
0.322 |
|
| 2008 |
Bryan PN. Protein Folding Catalysis by Pro-domains Protein Folding Handbook. 2: 1032-1058. DOI: 10.1002/9783527619498.ch29 |
0.334 |
|
| 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 |
0.379 |
|
| 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 |
0.73 |
|
| 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 |
0.735 |
|
| 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 |
0.723 |
|
| 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 |
0.719 |
|
| 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 |
0.397 |
|
| 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 |
0.707 |
|
| 2005 |
Rozak DA, Bryan PN. Offset recombinant PCR: a simple but effective method for shuffling compact heterologous domains. Nucleic Acids Research. 33: e82. PMID 15901853 DOI: 10.1093/Nar/Gni081 |
0.657 |
|
| 2004 |
Ruan B, Fisher KE, Alexander PA, Doroshko V, Bryan PN. Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification. Biochemistry. 43: 14539-46. PMID 15544324 DOI: 10.1021/bi048177j |
0.321 |
|
| 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 |
0.371 |
|
| 2002 |
Almog O, Gallagher DT, Ladner JE, Strausberg S, Alexander P, Bryan P, Gilliland GL. Structural basis of thermostability. Analysis of stabilizing mutations in subtilisin BPN'. The Journal of Biological Chemistry. 277: 27553-8. PMID 12011071 DOI: 10.1074/Jbc.M111777200 |
0.357 |
|
| 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 |
0.371 |
|
| 1999 |
Ruan B, Hoskins J, Bryan PN. Rapid folding of calcium-free subtilisin by a stabilized pro-domain mutant Biochemistry. 38: 8562-8571. PMID 10387104 DOI: 10.1021/bi990362n |
0.313 |
|
| 1998 |
Ruan B, Hoskins J, Wang L, Bryan PN. Stabilizing the subtilisin BPN' pro-domain by phage display selection: How restrictive is the amino acid code for maximum protein stability? Protein Science. 7: 2345-2353. PMID 9828000 DOI: 10.1002/PRO.5560071111 |
0.374 |
|
| 1998 |
Almog O, Gallagher T, Tordova M, Hoskins J, Bryan P, Gilliland GL. Crystal structure of calcium-independent subtilisin BPN' with restored thermal stability folded without the prodomain. Proteins. 31: 21-32. PMID 9552156 DOI: 10.1002/(Sici)1097-0134(19980401)31:1<21::Aid-Prot3>3.0.Co;2-K |
0.41 |
|
| 1998 |
Wang L, Ruan B, Ruvinov S, Bryan PN. Engineering the independent folding of the subtilisin BPN' pro-domain: Correlation of pro-domain stability with the rate of subtilisin folding Biochemistry. 37: 3165-3171. PMID 9485470 DOI: 10.1021/bi972741r |
0.35 |
|
| 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 |
0.391 |
|
| 1996 |
Gilliland GL, Gallagher DT, Alexander P, Bryan P. Crystal structure analysis of subtilisin BPN' mutants engineered for studying thermal stability Advances in Experimental Medicine and Biology. 379: 159-169. PMID 8796321 DOI: 10.1007/978-1-4613-0319-0_18 |
0.368 |
|
| 1996 |
Wang L, Ruvinov S, Strausberg S, Gallagher DT, Gilliland G, Bryan PN. Prodomain mutations at the subtilisin interface: correlation of binding energy and the rate of catalyzed folding. Biochemistry. 34: 15415-20. PMID 7492541 DOI: 10.1021/bi00047a004 |
0.368 |
|
| 1995 |
Gallagher T, Gilliland G, Wang L, Bryan P. The prosegment-subtilisin BPN′ complex: crystal structure of a specific 'foldase' Structure. 3: 907-914. PMID 8535784 DOI: 10.1016/S0969-2126(01)00225-8 |
0.452 |
|
| 1995 |
Bryan P, Wang L, Hoskins J, Ruvinov S, Strausberg S, Alexander P, Almog O, Gilliland G, Gallagher T. Catalysis of a protein folding reaction: mechanistic implications of the 2.0 A structure of the subtilisin-prodomain complex. Biochemistry. 34: 10310-8. PMID 7640287 DOI: 10.1021/Bi00032A026 |
0.409 |
|
| 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 |
0.336 |
|
| 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 |
0.446 |
|
| 1994 |
Gallagher T, Alexander P, Bryan P, Gilliland GL. Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry. 33: 4721-4729. DOI: 10.1021/Bi00181A032 |
0.415 |
|
| 1993 |
Strausberg S, Alexander P, Wang L, Gallagher T, Gilliland G, Bryan P. An engineered disulfide cross-link accelerates the refolding rate of calcium-free subtilisin by 850-fold. Biochemistry. 32: 10371-10377. PMID 8399180 DOI: 10.1021/Bi00090A012 |
0.433 |
|
| 1993 |
Bryan P. Catalysis of a protein folding reaction: Thermodynamic and kinetic analysis of subtilisin BPN′ interactions with its propeptide fragment Biochemistry. 32: 8112-8119. PMID 8347611 DOI: 10.1021/Bi00083A009 |
0.372 |
|
| 1993 |
Gallagher T, Bryan P, Gilliland GL. Calcium-independent subtilisin by design Proteins: Structure, Function and Genetics. 16: 205-213. PMID 8332608 DOI: 10.1002/Prot.340160207 |
0.38 |
|
| 1992 |
Bryan P, Alexander P, Strausberg S, Schwarz F, Lan W, Gilliland G, Gallagher DT. Energetics of folding subtilisin BPN'. Biochemistry. 31: 4937-45. PMID 1599918 DOI: 10.1021/bi00136a003 |
0.317 |
|
| 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 |
0.483 |
|
| 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 |
0.41 |
|
| 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 |
0.429 |
|
| 1990 |
Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN. Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding. Biochemistry. 28: 7205-13. PMID 2684274 DOI: 10.1021/bi00444a012 |
0.307 |
|
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