S. Burston

发表

Structure and function in GroEL-mediated protein folding.

A. Horwich, W. Fenton, P. Sigler, 1998, Annual review of biochemistry.

Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL

A. Horwich, W. Fenton, P. Sigler, 1997, Nature.

Biochemical and Functional Analysis of the Assembly of Full-length Sup35p and Its Prion-forming Domain*

S. Burston, R. Melki, J. Krzewska, 2007, Journal of Biological Chemistry.

ASSEMBLY AND CHARACTERISATION OF DIELS-ALDERASE POLYMER CONJUGATES FOR INDUSTRIAL BIOCATALYSIS

S. Burston, A. Strauss, 2019 .

Molecular chaperones and folding catalysts

H. Saibil, S. Burston, 1999 .

Molecular chaperones: physical and mechanistic properties.

A. Clarke, S. Burston, 1995, Essays in biochemistry.

Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL.

J. Weissman, A. Horwich, W. Fenton, 1998, Methods in enzymology.

The stability and hydrophobicity of cytosolic and mitochondrial malate dehydrogenases and their relation to chaperonin‐assisted folding

T. Atkinson, A. Clarke, J. Holbrook, 1994, FEBS letters.

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

T. Atkinson, A. Clarke, J. Holbrook, 1993, Biochemistry.

Mapping the road to recovery: the ClpB/Hsp104 molecular chaperone.

S. Burston, Jacqueline J. T. Marshall, S. Hodson, 2012, Journal of structural biology.

Location of a folding protein and shape changes in GroELGroES complexes imaged by cryo-electron microscopy

Neil A. Ranson, Helen R. Saibil, Anthony R. Clarke, 1994, Nature.

Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.

E. Kovács, A. Clarke, S. Burston, 2010, Journal of molecular biology.

The E. coli GroE Chaperone

S. Burston, S. Walter, 2008 .

The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture

V. Higman, S. Burston, D. Frankel, 2020, The Journal of Biological Chemistry.

Distinctactionsof cis and trans ATPwithin thedouble ring of thechaperoninGroEL

A. Horwich, W. Fenton, P. Sigler, 2022 .

Identification of a Major Inter-ring Coupling Step in the GroEL Reaction Cycle*

A. Clarke, S. Burston, D. Poso, 2004, Journal of Biological Chemistry.

A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL.

A. Clarke, S. Burston, N. Hay, 1999, Journal of molecular biology.

Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction.

A. Clarke, S. Burston, N. Ranson, 1997, Journal of molecular biology.

Release of both native and non-native proteins from a cis-only GroEL ternary complex

J. Weissman, G. Farr, W. Fenton, 1996, Nature.

Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds.

A. Clarke, S. Burston, N. Dunster, 1995, Journal of molecular biology.

The origins and consequences of asymmetry in the chaperonin reaction cycle.

A. Clarke, N. Ranson, S. Burston, 1995, Journal of molecular biology.

Anything a ClpA can do, two ClpAs can do better.

Steven G Burston, S. Burston, 2009, Structure.

Protein Folding Handbook: Part II

S. Burston, S. Walter, 2004 .

The energetics and cooperativity of protein folding: a simple experimental analysis based upon the solvation of internal residues.

T. Atkinson, A. Clarke, J. Holbrook, 1993, Biochemistry.

Activation by sub-stoichiometric inhibition.

R. Huber, S. Burston, M. Ehrmann, 2019 .

Toward a detailed description of the pathways of allosteric communication in the GroEL chaperonin through atomistic simulation.

S. Burston, R. Sessions, T. Piggot, 2012, Biochemistry.

Elucidation of Steps in the Capture of a Protein Substrate for Efficient Encapsulation by GroE *

A. Clarke, S. Burston, M. Cliff, 2006, Journal of Biological Chemistry.

Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10.

T. Atkinson, A. Clarke, S. Burston, 1994, The Biochemical journal.

A kinetic analysis of the nucleotide-induced allosteric transitions in a single-ring mutant of GroEL.

A. Clarke, S. Burston, D. Poso, 2004, Journal of molecular biology.

Self-malonylation is an intrinsic property of a chemically synthesized type II polyketide synthase acyl carrier protein.

S. Burston, A. Szafranska, T. J. Simpson, 2005, Biochemistry.

The influence of chaperonins on protein folding. A mechanism for increasing the yield of the native form.

A. Clarke, J. Holbrook, S. Burston, 1992, Annals of the New York Academy of Sciences.

Structure and malonyl CoA-ACP transacylase binding of streptomyces coelicolor fatty acid synthase acyl carrier protein.

Steven G Burston, John Crosby, S. Burston, 2009, ACS chemical biology.

An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein

S. Burston, T. J. Simpson, J. Crosby, 2008, Chembiochem : a European journal of chemical biology.

Domain shuffling of a highly mutable ligand‐binding fold drives adhesin generation across the bacterial kingdom

A. Bateman, S. Burston, J. Potempa, 2023, Proteins.

Activation by substoichiometric inhibition

R. Huber, S. Knapp, S. Burston, 2020, Proceedings of the National Academy of Sciences.

High resolution analysis of proteolytic substrate processing

R. Huber, S. Burston, H. Luecke, 2022, bioRxiv.

Domain behavior during the folding of a thermostable phosphoglycerate kinase.

M. J. Parker, A. Clarke, S. Burston, 1996, Biochemistry.

Characterisation of a GroEL single-ring mutant that supports growth of Escherichia coli and has GroES-dependent ATPase activity.

E. Kovács, A. Clarke, S. Burston, 2010, Journal of molecular biology.