J. Waltho

发表

Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1

Timothy D. Craggs, Ian A. Bennet, L. Finger, 2018, Nucleic acids research.

Peptide structure from NMR

J. Waltho, M. Williamson, 1992 .

Atomic details of near-transition state conformers for enzyme phosphoryl transfer revealed by MgF 3 - rather than by phosphoranes

N. J. Baxter, A. Hounslow, J. Waltho, 2010, Proceedings of the National Academy of Sciences.

Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis.

Matthew W Bowler, N. J. Baxter, A. Hounslow, 2010, Journal of the American Chemical Society.

β1 integrin is a sensor of blood flow direction

P. Evans, M. Humphries, J. Waltho, 2019, Journal of Cell Science.

Calcium-induced structural changes and domain autonomy in calmodulin

Eva Thulin, Bryan E. Finn, Sture Forsén, 1995, Nature Structural Biology.

Improved experiments for the assignment of crowded peptide spectra

J. Waltho, M. Williamson, Nicola J. Murray, 1992 .

Complexes formed between calmodulin and the antagonists J-8 and TFP in solution.

J. Waltho, E. Thulin, G. Blackburn, 1996, Biochemistry.

Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration.

M. Blackledge, J. Nissink, M. R. Jensen, 2019, Structure.

Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate

C. E. Webster, N. J. Baxter, A. Hounslow, 2012, Proceedings of the National Academy of Sciences.

Evidence supporting a cis-enediol-based mechanism for Pyrococcus furiosus phosphoglucose isomerase.

Stan J. J. Brouns, Jasper Akerboom, D. Rice, 2006, Journal of molecular biology.

Real-time pure shift 15N HSQC of proteins: a real improvement in resolution and sensitivity

M. Foroozandeh, M. Nilsson, G. Morris, 2015, Journal of Biomolecular NMR.

Simultaneously Enhancing Spectral Resolution and Sensitivity in Heteronuclear Correlation NMR Spectroscopy

M. Foroozandeh, M. Nilsson, G. Morris, 2013, Angewandte Chemie.

Nonequivalence of Second Sphere “Noncatalytic” Residues in Pentaerythritol Tetranitrate Reductase in Relation to Local Dynamics Linked to H-Transfer in Reactions with NADH and NADPH Coenzymes

N. Scrutton, N. J. Baxter, J. Waltho, 2018, ACS catalysis.

Fast protein motions are coupled to enzyme H-transfer reactions.

N. Scrutton, L. Johannissen, N. J. Baxter, 2013, Journal of the American Chemical Society.

Cystatin forms a tetramer through structural rearrangement of domain-swapped dimers prior to amyloidogenesis.

M. J. Conroy, A. Hounslow, J. Waltho, 2004, Journal of molecular biology.

Semiselective two-dimensional NMR experiments

J. Keeler, J. Waltho, J. Cavanagh, 1987 .

The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L.

J. Waltho, N. Hill, C. Craven, 1998, Biochemistry.

Versatile low-molecular-weight hydrogelators: achieving multiresponsiveness through a modular design.

C. Hunter, J. Waltho, Salvador Tomas, 2011, Chemistry.

A reassessment of copper(II) binding in the full-length prion protein.

J. Collinge, A. Clarke, G. Jackson, 2006, The Biochemical journal.

Deconvolution of conformational exchange from Raman spectra of aqueous RNA nucleosides

A. Doig, C. Outeiral, P. Popelier, 2020, Communications Chemistry.

Practical aspects of recording multidimensional NMR spectra in water with flat baselines

J. Waltho, J. Cavanagh, 1993 .

Aspects of molecular recognition: solvent exclusion and dimerization of the antibiotic ristocetin when bound to a model bacterial cell-wall precursor

Dudley H. Williams, J. Waltho, 1989 .

Structure and Dynamics of Coxsackievirus B4 2A Proteinase, an Enyzme Involved in the Etiology of Heart Disease

N. J. Baxter, A. Hounslow, J. Waltho, 2006, Journal of Virology.

Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4.

J. Collinge, A. Clarke, G. Jackson, 2006, The Biochemical journal.

Molecular basis of the activity of antibiotics of the vancomycin group

D. Williams, J. Waltho, 1989, Biochemical pharmacology.

Function of the amino sugar and N-terminal amino acid of the antibiotic vancomycin in its complexation with cell wall peptides

Dudley H. Williams, J. Waltho, N. Skelton, 1988 .

Peptide structure from NMR

J. Waltho, M. Williamson, 1993 .

The three-dimensional solution structure of human stefin A.

J. Waltho, V. Turk, C. Craven, 1995, Journal of molecular biology.

Loss of the first β-strand of human prion protein generates an aggregation-competent partially “open” form

J. Collinge, D. Sangar, M. Batchelor, 2022, bioRxiv.

Prioritization of charge over geometry in transition state analogues of a dual specificity protein kinase.

N. J. Baxter, A. Hounslow, J. Waltho, 2011, Journal of the American Chemical Society.

α-Fluorophosphonates reveal how a phosphomutase conserves transition state conformation over hexose recognition in its two-step reaction

N. J. Baxter, J. Waltho, M. Bowler, 2014, Proceedings of the National Academy of Sciences.

A pulse--radiolysis approach to fast reductive cleavage of a disulfide bond to uncage enzyme activity.

C. Hunter, J. Waltho, Salvador Tomas, 2008, Free radical biology & medicine.

Enzymatic production of β-glucose 1,6-bisphosphate through manipulation of catalytic magnesium coordination

C. R. Trevitt, N. J. Baxter, A. Hounslow, 2020, Green Chemistry.

Aspects of molecular recognition: solvent exclusion and dimerization of the antibiotic ristocetin when bound to a model bacterial cell-wall precursor

Dudley H. Williams, J. Waltho, 1989 .

Structure elucidation of the glycopeptide antibiotic complex A40926

Dudley H. Williams, J. Waltho, P. Ferrari, 1987 .

Amplification of bifunctional ligands for calmodulin from a dynamic combinatorial library.

C. Hunter, J. Waltho, S. Sedelnikova, 2006, Chemistry.

Location and properties of metal-binding sites on the human prion protein

J. Collinge, A. Clarke, G. Jackson, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1alpha, MIP-1beta, and RANTES. Characterization of active disaggregated chemokine variants.

V. Appay, L. Czaplewski, J. Waltho, 1999, The Journal of biological chemistry.

Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate state.

J. Waltho, V. Turk, E. Žerovnik, 2001, Biochemical Society transactions.

Differences in the effects of TFE on the folding pathways of human stefins A and B

J. Waltho, V. Turk, R. Jerala, 1999, Proteins.

On the mechanism of human stefin B folding: I. Comparison to homologous stefin A. Influence of pH and trifluoroethanol on the fast and slow folding phases

J. Waltho, V. Turk, R. Jerala, 1998, Proteins.

Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin.

P E Wright, R. Lerner, H. Dyson, 1992, Journal of molecular biology.

Enhanced ligand affinity for receptors in which components of the binding site are independently mobile.

C. Hunter, J. Perkins, A. Annila, 2005, Chemistry & biology.

Why did Nature select phosphate for its dominant roles in biology

J. Waltho, M. Bowler, M. Cliff, 2010 .

Cryogenic and Laser Photoexcitation Studies Identify Multiple Roles for Active Site Residues in the Light-driven Enzyme Protochlorophyllide Oxidoreductase*

N. Scrutton, J. Waltho, D. Heyes, 2009, The Journal of Biological Chemistry.

Reflections on biocatalysis involving phosphorus

J. Waltho, M. Bowler, G. Blackburn, 2012, Biochemistry (Moscow).

Characterization of the Elk-1 ETS DNA-binding Domain (*)

A. Sharrocks, J. Waltho, J. Lakey, 1995, The Journal of Biological Chemistry.

Metal Fluorides as Analogues for Studies on Phosphoryl Transfer Enzymes.

N. Richards, J. Waltho, G. Blackburn, 2017, Angewandte Chemie.

19F NMR and DFT Analysis Reveal Structural and Electronic Transition State Features for RhoA‐Catalyzed GTP Hydrolysis

N. Richards, J. Waltho, G. Blackburn, 2016, Angewandte Chemie.

Structure of TCTP reveals unexpected relationship with guanine nucleotide-free chaperones

N. J. Baxter, A. Hounslow, J. Waltho, 2001, Nature Structural Biology.

Obligate heterodimerization of the archaeal Alba2 protein with Alba1 provides a mechanism for control of DNA packaging.

M. F. White, G. Taylor, M. J. Conroy, 2005, Structure.

Allomorphy as a mechanism of post-translational control of enzyme activity

C. R. Trevitt, N. J. Baxter, A. Hounslow, 2020, Nature Communications.

Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations.

J Collinge, J. Collinge, A. Hill, 1999, Science.

Mechanism-based inhibition of C5-cytosine DNA methyltransferases by 2-H pyrimidinone.

N. C. Price, D. Hornby, J. Waltho, 1999, Journal of molecular biology.

Determinants of DNA-binding specificity of ETS-domain transcription factors

A. Sharrocks, J. Waltho, R. Davis, 1996, Molecular and cellular biology.

Multiple folding pathways for heterologously expressed human prion protein.

J. Collinge, A. Hill, A. Clarke, 1999, Biochimica et biophysica acta.

Structural mobility of the human prion protein probed by backbone hydrogen exchange

J. Collinge, A. Clarke, G. Jackson, 1999, Nature Structural Biology.

Structural effects of the highly protective V127 polymorphism on human prion protein

J. Collinge, G. Jackson, D. Sangar, 2020, Communications Biology.

Structural effects of the highly protective V127 polymorphism on human prion protein

J. Collinge, G. Jackson, D. Sangar, 2020, Communications Biology.

The Residue 129 Polymorphism in Human Prion Protein Does Not Confer Susceptibility to Creutzfeldt-Jakob Disease by Altering the Structure or Global Stability of PrPC*

J. Collinge, A. Clarke, C. R. Trevitt, 2004, Journal of Biological Chemistry.

Folding kinetics of the human prion protein probed by temperature jump

John Collinge, J. Collinge, A. Clarke, 2009, Proceedings of the National Academy of Sciences.

Comparison of backbone dynamics of monomeric and domain‐swapped stefin A

J. Waltho, R. Jerala, B. Japelj, 2004, Proteins.

Double and triple resonance NMR methods for protein assignment.

J. Waltho, C. Craven, B. Whitehead, 1997, Methods in molecular biology.

Isotopically labeled flavoenzymes and their uses in probing reaction mechanisms.

N. Scrutton, J. Waltho, M. Cliff, 2019, Methods in enzymology.

Myc phosphorylation in its basic helix–loop–helix region destabilizes transient α-helical structures, disrupting Max and DNA binding

J. Nissink, J. Waltho, M. Cliff, 2018, The Journal of Biological Chemistry.

Characterisation of low free-energy excited states of folded proteins.

N. J. Baxter, J. Waltho, M. Williamson, 1998, Journal of molecular biology.

Conformation of a T cell stimulating peptide in aqueous solution

R. Lerner, P. Wright, J. Waltho, 1989, FEBS letters.

High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin

C. R. Trevitt, A. Hounslow, J. Waltho, 2021, Magnetic Resonance.

High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin

C. Hunter, C. R. Trevitt, A. Hounslow, 2021, Magnetic resonance.

Determinants of the endosomal localization of sorting nexin 1.

A. Hounslow, J. Waltho, G. Gill, 2005, Molecular biology of the cell.

Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.

A. Hounslow, J. Waltho, Karl Syson, 2005, Structure.

Letter to the Editor: Backbone NMR assignment of the 19 kDa translationally controlled tumor-associated protein p23 fyp from Schizosaccharomyces pombe

N. J. Baxter, J. Waltho, S. Sedelnikova, 2000 .

The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone.

C. Hunter, J. Waltho, G. Beddard, 2015, Physical chemistry chemical physics : PCCP.

Structural Analysis of Bacillus subtilis SPP1 Phage Helicase Loader Protein G39P*

J. Rafferty, J. Alonso, J. Waltho, 2003, The Journal of Biological Chemistry.

An Enzyme with High Catalytic Proficiency Utilizes Distal Site Substrate Binding Energy to Stabilize the Closed State but at the Expense of Substrate Inhibition

N. J. Baxter, A. Hounslow, J. Waltho, 2022, ACS catalysis.

Topology, sequence evolution and folding dynamics of an immunoglobulin domain

M. J. Parker, A. Clarke, J. Waltho, 1998, Nature Structural Biology.

Three‐dimensional domain swapping in the folded and molten‐globule states of cystatins, an amyloid‐forming structural superfamily

M. J. Conroy, A. Hounslow, J. Waltho, 2001, The EMBO journal.

On the mechanism of human stefin B folding: II. Folding from GuHCl unfolded, TFE denatured, acid denatured, and acid intermediate states

J. Waltho, V. Turk, R. Jerala, 1998, Proteins.

Pharmacological chaperone for the structured domain of human prion protein

J. Collinge, A. Clarke, C. R. Trevitt, 2010, Proceedings of the National Academy of Sciences.

A bacteriophage capsid protein provides a general amyloid interaction motif (GAIM) that binds and remodels misfolded protein assemblies.

D. Kirschner, A. Hounslow, J. Waltho, 2014, Journal of molecular biology.

β1 integrin is a sensor of blood flow direction

P. Evans, M. Humphries, J. Waltho, 2019, Journal of Cell Science.

Structural tightening and interdomain communication in the catalytic cycle of phosphoglycerate kinase.

M. Reed, A. Hounslow, J. Waltho, 2010, Journal of molecular biology.

Conformational Properties of β-PrP*

J. Collinge, A. Clarke, C. R. Trevitt, 2009, The Journal of Biological Chemistry.

Charge-balanced metal fluoride complexes for protein kinase A with adenosine diphosphate and substrate peptide SP20.

N. J. Baxter, A. Hounslow, J. Waltho, 2012, Angewandte Chemie.

Effects of domain dissection on the folding and stability of the 43 kDa protein PGK probed by NMR.

M. Reed, A. Clarke, A. Hounslow, 2003, Journal of molecular biology.

Structure elucidation of two triterpenoid tetrasaccharides from Androsace saxifragifolia

Dudley H. Williams, J. Waltho, S. Mahato, 1986 .

Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-O-methyltransferase

N. Scrutton, L. Johannissen, N. J. Baxter, 2019, ACS catalysis.

Essential role of proline isomerization in stefin B tetramer formation.

D. Turk, J. Waltho, G. Guncar, 2007, Journal of molecular biology.

Quaternary structure built from subunits combining NMR and small-angle x-ray scattering data.

A. Annila, J. Waltho, R. Serimaa, 2002, Biophysical journal.

The denatured state under native conditions: a non-native-like collapsed state of N-PGK.

M. Reed, A. Clarke, A. Hounslow, 2006, Journal of molecular biology.

Definable equilibrium states in the folding of human prion protein.

J. Collinge, A. Clarke, G. Jackson, 2005, Biochemistry.

Kinetic analysis of beta-phosphoglucomutase and its inhibition by magnesium fluoride.

F. Hollfelder, N. J. Baxter, J. Waltho, 2009, Journal of the American Chemical Society.

A Trojan horse transition state analogue generated by MgF3− formation in an enzyme active site

F. Hollfelder, N. J. Baxter, A. Hounslow, 2006, Proceedings of the National Academy of Sciences.

Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin.

P E Wright, H. Dyson, P. Wright, 1993, Biochemistry.

1H, 15N and 13C backbone resonance assignments of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2

N. Scrutton, N. J. Baxter, J. Waltho, 2017, Biomolecular NMR assignments.

Limited Proteolysis Reveals That Amyloids from the 3D Domain-Swapping Cystatin B Have a Non-Native β-Sheet Topology.

J. Waltho, P. Davis, D. Holmes, 2015, Journal of molecular biology.

Assessing the Influence of Mutation on GTPase Transition States by Using X‐ray Crystallography, 19F NMR, and DFT Approaches

N. Richards, J. Waltho, M. Bowler, 2017, Angewandte Chemie.

1H, 15N and 13C backbone resonance assignments of the P146A variant of β-phosphoglucomutase from Lactococcus lactis in its substrate-free form

N. J. Baxter, A. Hounslow, J. Waltho, 2019, Biomolecular NMR Assignments.

Intramolecular determinants of conformation and mobility within the antibiotic vancomycin

Dudley H. Williams, J. Waltho, N. Skelton, 1988 .

Protein folding pathways and intermediates

A. Clarke, J. Waltho, 1997 .

Peptide models of protein folding initiation sites. 3. The G-H helical hairpin of myoglobin.

H. Dyson, P. Wright, J. Waltho, 1993, Biochemistry.

Structural characterisation of human stefin A in solution and implications for binding to cysteine proteinases.

J. Waltho, V. Turk, R. Jerala, 1994, European journal of biochemistry.

Beyond the EX1 limit: probing the structure of high-energy states in protein unfolding.

A. Clarke, R. Sessions, J. Waltho, 2004, Journal of molecular biology.

Measurement of energy landscape roughness of folded and unfolded proteins

C. Hunter, D. Shaw, J. Waltho, 2012, Proceedings of the National Academy of Sciences.

Metal Ion-dependent Heavy Chain Transfer Activity of TSG-6 Mediates Assembly of the Cumulus-Oocyte Matrix*

Marilyn S. Rugg, J. Enghild, J. Waltho, 2015, The Journal of Biological Chemistry.

N-terminal Domain of Prion Protein Directs Its Oligomeric Association*

J. Collinge, H. Saibil, A. Clarke, 2014, The Journal of Biological Chemistry.

Mapping local structural perturbations in the native state of stefin B (cystatin B) under amyloid forming conditions

A. Hounslow, J. Waltho, M. Cliff, 2012, Front. Mol. Neurosci..

The mechanism of amyloid‐fibril formation by stefin B: Temperature and protein concentration dependence of the rates

D. Turk, J. Waltho, V. Turk, 2009, Proteins.

Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein.

A. Hounslow, J. Waltho, V. Turk, 2008, Journal of molecular biology.

Folding and amyloid‐fibril formation for a series of human stefins' chimeras: Any correlation?

F. Avbelj, D. Turk, J. Waltho, 2005, Proteins.

The major transition state in folding need not involve the immobilization of side chains.

A. Clarke, J. Waltho, E. Žerovnik, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Loss of residues 119 – 136, including the first β-strand of human prion protein, generates an aggregation-competent partially “open” form

J. Collinge, D. Sangar, M. Batchelor, 2023, Journal of Molecular Biology.

Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes.

F. Hollfelder, D. Wemmer, N. J. Baxter, 2008, Journal of the American Chemical Society.

How to name atoms in phosphates, polyphosphates, their derivatives and mimics, and transition state analogues for enzyme-catalysed phosphoryl transfer reactions (IUPAC Recommendations 2016)

G. P. Moss, J. Cherfils, A. Wittinghofer, 2017 .

The H187R mutation of the human prion protein induces conversion of recombinant prion protein to the PrP(Sc)-like form.

J. Collinge, A. Clarke, C. R. Trevitt, 2010, Biochemistry.

Folding of Peptide Fragments of Proteins in Aqueous Solution

D. Case, R. Lerner, H. Dyson, 1990 .

Metal Ion-dependent Heavy Chain Transfer Activity of TSG-6 Mediates Assembly of the Cumulus-Oocyte Matrix*

Marilyn S. Rugg, J. Enghild, J. Waltho, 2015, The Journal of Biological Chemistry.

Assessing the Influence of Mutation on GTPase Transition States by Using X‐ray Crystallography, 19F NMR, and DFT Approaches

N. Richards, J. Waltho, M. Bowler, 2017, Angewandte Chemie.

Identification of Amino Acid Residues Critical for Aggregation of Human CC Chemokines Macrophage Inflammatory Protein (MIP)-1α, MIP-1β, and RANTES

J. Waltho, S. Cribbes, E. Randle, 1999, The Journal of Biological Chemistry.

J. Waltho, S. Cribbes, E. Randle, 1999, The Journal of biological chemistry.

Peptide models of protein folding initiation sites. 2. The G-H turn region of myoglobin acts as a helix stop signal.

H. Dyson, P. Wright, J. Waltho, 1993, Biochemistry.

A thiol labelling competition experiment as a probe for sidechain packing in the kinetic folding intermediate of N-PGK.

J. Waltho, Tooba Alizadeh, M. Cliff, 2006, Journal of molecular biology.

1H, 15N, 13C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-l-methionine and 3,5-dinitrocatechol

N. Scrutton, N. J. Baxter, J. Waltho, 2016, Biomolecular NMR Assignments.

Conformational Properties of β-PrP*

J. Collinge, A. Clarke, C. R. Trevitt, 2009, The Journal of Biological Chemistry.

Metal Fluorides as Analogues for Studies on Phosphoryl Transfer Enzymes.

J. Waltho, Yi Jin, Nigel G. Richards, 2017, Angewandte Chemie.

The Relationship between Enzyme Conformational Change, Proton Transfer, and Phosphoryl Transfer in β-Phosphoglucomutase

P. Popelier, J. Waltho, M. Cliff, 2021, ACS Catalysis.

van der Waals Contact between Nucleophile and Transferring Phosphorus Is Insufficient To Achieve Enzyme Transition-State Architecture

L. A. Johnson, C. R. Trevitt, N. J. Baxter, 2018, ACS Catalysis.

1H, 15N, 13C backbone resonance assignments of human phosphoglycerate kinase in a transition state analogue complex with ADP, 3-phosphoglycerate and magnesium trifluoride

N. J. Baxter, J. Waltho, M. Cliff, 2017, Biomolecular NMR Assignments.

Transition state analogue structures of human phosphoglycerate kinase establish the importance of charge balance in catalysis.

N. J. Baxter, A. Hounslow, J. Waltho, 2010, Journal of the American Chemical Society.

MgF(3)(-) and alpha-galactose 1-phosphate in the active site of beta-phosphoglucomutase form a transition state analogue of phosphoryl transfer.

N. J. Baxter, A. Hounslow, J. Waltho, 2009, Journal of the American Chemical Society.

Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes.

F. Hollfelder, N. J. Baxter, A. Hounslow, 2008, Journal of the American Chemical Society.

Kinetic analysis of beta-phosphoglucomutase and its inhibition by magnesium fluoride.

F. Hollfelder, N. J. Baxter, J. Waltho, 2009, Journal of the American Chemical Society.

Deposited in DRO : 15 October 2015 Version of attached le : Published Version Peer-review status of attached le : Peer-reviewed Citation for published item :

M. Foroozandeh, M. Nilsson, J. Waltho, 2014 .

A pulse--radiolysis approach to fast reductive cleavage of a disulfide bond to uncage enzyme activity.

C. Hunter, J. Waltho, Salvador Tomas, 2008, Free radical biology & medicine.

Modulation of contact order effects in the two-state folding of stefins A and B.

D. Turk, J. Waltho, D. Clarke, 2011, Biophysical journal.

Fast protein motions are coupled to enzyme H-transfer reactions.

N. Scrutton, L. Johannissen, N. J. Baxter, 2013, Journal of the American Chemical Society.

Domain behavior during the folding of a thermostable phosphoglycerate kinase.

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

25 – THE H-HELIX OF MYOGLOBIN AS A POTENTIAL INDEPENDENT PROTEIN FOLDING DOMAIN

P. Wright, J. Waltho, V. Feher, 1990 .

ASYMMETRY IN THE STRUCTURE OF GLYCOPEPTIDE ANTIBIOTIC DIMERS : NMR STUDIESOF THE RISTOCETIN A COMPLEX WITH A BACTERIAL CELL WALL ANALOGUE

Dudley H. Williams, J. Waltho, M. Searle, 1995 .