P. Bryan

发表

A minimal sequence code for switching protein structure and function

P. Alexander, Yanan He, Yihong Chen, 2009, Proceedings of the National Academy of Sciences.

Engineering the independent folding of the subtilisin BPN' prodomain: analysis of two-state folding versus protein stability.

G L Gilliland, P. Bryan, G. Gilliland, 1997, Biochemistry.

Rapid folding of calcium-free subtilisin by a stabilized pro-domain mutant.

P. Bryan, B. Ruan, J. Hoskins, 1999, Biochemistry.

Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding.

P. Bryan, K. D. Hardman, M. Pantoliano, 1989, Biochemistry.

NMR structures of two designed proteins with high sequence identity but different fold and function

John Orban, Yihong Chen, Yanan He, 2008, Proceedings of the National Academy of Sciences.

The design and characterization of two proteins with 88% sequence identity but different structure and function

John Orban, Yihong Chen, Yanan He, 2007, Proceedings of the National Academy of Sciences.

Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.

G L Gilliland, T Gallagher, P. Alexander, 1994, Biochemistry.

Structural metamorphism and polymorphism in proteins on the brink of thermodynamic stability

John Orban, Yihong Chen, Yanan He, 2018, Protein science : a publication of the Protein Society.

Mutational tipping points for switching protein folds and functions.

John Orban, Yihong Chen, Yanan He, 2012, Structure.

Proteins that switch folds.

John Orban, J. Orban, P. Bryan, 2010, Current opinion in structural biology.

Physical properties of inner histone-DNA complexes.

D. E. Olins, P. Bryan, D. Olins, 1978, Nucleic acids research.

Generation of soluble and active subtilisin and alpha-chymotrypsin in organic solvents via hydrophobic ion pairing.

P. Bryan, M. Manning, J. Matsuura, 2009, International journal of peptide and protein research.

Microsoft Word-Manuscript.docx

K. Rajagopalan, Yanan He, Yihong Chen, 2015 .

Design and characterization of a protein fold switching network

Eun Jung Choi, Yanan He, J. Orban, 2022, bioRxiv.

Energetics of folding subtilisin BPN'.

P. Alexander, P. Bryan, G. Gilliland, 1992, Biochemistry.

Solution Structure of the Mouse Prohormone Convertase 1 Pro-Domain

J. Orban, P. Bryan, M. Tangrea, 2002 .

De novo structure generation using chemical shifts for proteins with high‐sequence identity but different folds

D. Baker, A. Bax, Yanan He, 2010, Protein science : a publication of the Protein Society.

Site-directed mutagenesis to study protein folding and stability.

P. Bryan, 1995, Methods in molecular biology.

The Denatured State Dictates the Topology of Two Proteins with Almost Identical Sequence but Different Native Structure and Function*

Valerie Daggett, Michelle E McCully, M. Brunori, 2010, The Journal of Biological Chemistry.

Prodomains and protein folding catalysis.

P. Bryan, 2002, Chemical reviews.

Crystal structure of calcium‐independent subtilisin BPN′ with restored thermal stability folded without the prodomain

P. Bryan, G. Gilliland, O. Almog, 1998, Proteins.

Enzymes in organic synthesis: use of subtilisin and a highly stable mutant derived from multiple site-specific mutations

P. Bryan, Chi‐Huey Wong, M. Pantoliano, 1990 .

Protein engineering of subtilisin.

P. Bryan, 2000, Biochimica et biophysica acta.

The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case.

T. Poulos, P. Bryan, G. Gilliland, 1988, Biochemistry.

Structural Basis of Thermostability

P. Alexander, P. Bryan, G. Gilliland, 2002, The Journal of Biological Chemistry.

Crystal structure analysis of subtilisin BPN' mutants engineered for studying thermal stability.

P. Alexander, P. Bryan, G. Gilliland, 1996, Advances in experimental medicine and biology.

Engineering thermostability in subtilisin BPN' by in vitro mutagenesis.

P. Bryan, M. Pantoliano, M. Rollence, 1988, Critical reviews in biotechnology.

Protein engineering of subtilisin BPN': enhanced stabilization through the introduction of two cysteines to form a disulfide bond.

T. Poulos, P. Bryan, M. Pantoliano, 1987, Biochemistry.

Engineering subtilisin proteases that specifically degrade active RAS

Eun Jung Choi, David J Weber, Yanan He, 2021, Communications Biology.

Engineering subtilisin proteases that specifically degrade active RAS

Eun Jung Choi, David J Weber, Yanan He, 2021, Communications biology.

Engineering protein-specific proteases: targeting active RAS

Eun Jung Choi, David J Weber, Yanan He, 2020, bioRxiv.

Structure of a Switchable Subtilisin Complexed with a Substrate and with the Activator Azide†

P. Bryan, B. Ruan, T. Gallagher, 2009, Biochemistry.

Engineering substrate preference in subtilisin: structural and kinetic analysis of a specificity mutant.

P. Bryan, Viktoriya London, D. Gallagher, 2008, Biochemistry.

Mechanism of the kinetically-controlled folding reaction of subtilisin.

P. Alexander, P. Bryan, K. Fisher, 2007, Biochemistry.

Using offset recombinant polymerase chain reaction to identify functional determinants in a common family of bacterial albumin binding domains.

P. Alexander, Yanan He, Yihong Chen, 2006, Biochemistry.

Directed coevolution of stability and catalytic activity in calcium-free subtilisin.

P. Alexander, P. Bryan, K. Fisher, 2005, Biochemistry.

Engineering subtilisin into a fluoride-triggered processing protease useful for one-step protein purification.

P. Alexander, P. Bryan, K. Fisher, 2004, Biochemistry.

The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'.

P. Bryan, G. Gilliland, L. Wang, 1995, Structure.

Catalysis of a protein folding reaction: mechanistic implications of the 2.0 A structure of the subtilisin-prodomain complex.

P. Alexander, P. Bryan, G. Gilliland, 1995, Biochemistry.

Directed Evolution of a Subtilisin with Calcium-Independent Stability

P. Alexander, P. Bryan, G. Gilliland, 1995, Bio/Technology.

Enhancer sequences responsible for DNase I hypersensitivity in polyomavirus chromatin

P. Bryan, W. Folk, 1986, Molecular and cellular biology.

Conformational states of chromatin.

D. E. Olins, P. Bryan, R. Harrington, 1978, Cold Spring Harbor symposia on quantitative biology.

Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen*

K. Rajagopalan, Yanan He, Yihong Chen, 2015, The Journal of Biological Chemistry.

Major changes in the 5′ and 3′ chromatin structure of sea urchin histone genes accompany their activation and inactivation in development

P. Bryan, J. Olah, M. Birnstiel, 1983, Cell.

Conformational states of chromatin nu bodies induced by urea.

D. E. Olins, P. Bryan, R. Harrington, 1977, Nucleic acids research.

Engineering a Stable Protease

P. Bryan, K. D. Hardman, M. Pantoliano, 1988 .

G148-GA3: a streptococcal virulence module with atypical thermodynamics of folding optimally binds human serum albumin at physiological temperatures.

J. Orban, P. Bryan, D. Rozak, 2005, Biochimica et biophysica acta.

Stabilizing the subtilisin BPN' pro‐domain by phage display selection: How restrictive is the amino acid code for maximum protein stability?

P. Bryan, B. Ruan, J. Hoskins, 1998, Protein science : a publication of the Protein Society.

Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment.

P. Alexander, P. Bryan, L. Wang, 1993, Biochemistry.

Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G.

P. Alexander, J. Orban, P. Bryan, 1992, Biochemistry.

An engineered disulfide cross-link accelerates the refolding rate of calcium-free subtilisin by 850-fold.

P. Alexander, P. Bryan, G. Gilliland, 1993, Biochemistry.

Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B-domain.

P. Alexander, J. Orban, P. Bryan, 1994, Biochemistry.

Calcium‐independent subtilisin by design

P. Bryan, G. Gilliland, T. Gallagher, 1993, Proteins.

Nucleosome arrangement on tRNA genes of Xenopus laevis

P. Bryan, M. Birnstiel, H. Hofstetter, 1981, Cell.

Bacterial expression and one-step purification of an isotope-labeled heterotrimeric G-protein α-subunit

P. Bryan, T. Ngo, K. Ridge, 2005, Journal of biomolecular NMR.

Engineering the independent folding of the subtilisin BPN' pro-domain: correlation of pro-domain stability with the rate of subtilisin folding.

P. Bryan, S. Ruvinov, L. Wang, 1998, Biochemistry.

Core nucleosomes by digestion of reconstructed histone-DNA complexes.

P. Bryan, D. Olins, E. B. Wright, 1979, Nucleic acids research.

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.

P. Alexander, J. Orban, P. Bryan, 1992, Biochemistry.

Engineering Environmentally-Stable Proteases to Specifically Neutralize Protein Toxins

P. Bryan, 2012 .

Sequence-specific 1H NMR assignments and secondary structure of the streptococcal protein G B2-domain.

P. Alexander, J. Orban, P. Bryan, 1992, Biochemistry.

Reversible switching between two common protein folds in a designed system using only temperature

Yanan He, J. Orban, P. Bryan, 2023, Proceedings of the National Academy of Sciences of the United States of America.

Crystal structure of subtilisin BPN′ folded without the prodomain

P. Bryan, G. Gilliland, D. Gallagher, 1996 .

Prodomain mutations at the subtilisin interface: correlation of binding energy and the rate of catalyzed folding.

P. Bryan, G. Gilliland, D. Gallagher, 1995, Biochemistry.

pKa 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.

M. Gilson, J. Antosiewicz, P. Alexander, 1997, Biochemistry.

Subdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.

Yanan He, Yihong Chen, J. Orban, 2015, Biophysical journal.

Rules for designing protein fold switches and their implications for the folding code

Eun Jung Choi, Yanan He, J. Orban, 2021, bioRxiv.

Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus.

J. Orban, P. Bryan, M. Tangrea, 2002, Journal of molecular biology.

Offset recombinant PCR: a simple but effective method for shuffling compact heterologous domains

P. Bryan, D. Rozak, 2005, Nucleic acids research.

Assessment of stability differences in the protein G B1 and B2 domains from hydrogen-deuterium exchange: comparison with calorimetric data.

P. Alexander, J. Orban, P. Bryan, 1995, Biochemistry.

Engineering substrate preference in subtilisin: structural and kinetic analysis of a specificity mutant.

P. Bryan, Viktoriya London, B. Ruan, 2008, Biochemistry.

Subdomain interactions foster the design of two protein pairs with ∼80% sequence identity but different folds.

Yanan He, Yihong Chen, J. Orban, 2015, Biophysical Journal.

Structure, dynamics, and stability variation in bacterial albumin binding modules: implications for species specificity.

Yanan He, Yihong Chen, J. Orban, 2006, Biochemistry.

Structure and dynamics of an acid-denatured protein G mutant.

J. Orban, P. Bryan, N. Sari, 2000, Biochemistry.