C. Vaughan

发表

Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex

L. Pearl, P. Piper, S. Roe, 2006, Nature.

A common conformationally coupled ATPase mechanism for yeast and human cytoplasmic HSP90s

L. Pearl, P. Piper, C. Prodromou, 2009, The FEBS journal.

β-Amylase–Like Proteins Function as Transcription Factors in Arabidopsis, Controlling Shoot Growth and Development[C][W][OA]

S. Zeeman, C. Hostettler, Sebastian Soyk, 2011, Plant Cell.

The Mechanism of Hsp90 Regulation by the Protein Kinase-Specific Cochaperone p50cdc37

L. Pearl, P. Piper, S. Roe, 2004, Cell.

Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions.

Chrisostomos Prodromou, Bin Hu, Philippe Meyer, 2003, Molecular cell.

Edinburgh Research Explorer Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts upstream of three active beta-amylases in Arabidopsis chloroplasts

K. Halliday, Alison M. Smith, S. Zeeman, 2008 .

X-linked primary ciliary dyskinesia due to mutations in the cytoplasmic axonemal dynein assembly factor PIH1D3

Shane A. McCarthy, Richard D Emes, Klaudia Walter, 2017, Nature Communications.

3.7 Å cryo-EM structure of the core Centromere Binding Factor 3 complex

C. Vaughan, Wenjuan Zhang, N. Lukoynova, 2017, bioRxiv.

Edinburgh Research Explorer Beta-AMYLASE4, a noncatalytic protein required for starch breakdown, acts upstream of three active beta-amylases in Arabidopsis chloroplasts

K. Halliday, Alison M. Smith, S. Eicke, 2008 .

b -Amylase–Like Proteins Function as Transcription Factors in Arabidopsis , Controlling Shoot Growth and Development

Sebastian Soyk, C. Vaughan, H. Reinhold, 2011 .

Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37

L. Pearl, P. Piper, L. Neckers, 2008, Molecular cell.

The Enzyme-Like Domain of Arabidopsis Nuclear b -Amylases Is Critical for DNA Sequence Recognition and Transcriptional Activation

Luise H. Brand, D. Wanke, Sebastian Soyk, 2014 .

Distinct Functional Contributions by the Conserved Domains of the Malaria Parasite Alveolin IMC1h

C. Vaughan, J. Dessens, Annie Z. Tremp, 2019, Front. Cell. Infect. Microbiol..

Hsp90 Picks PIKKs via R2TP and Tel2

C. Vaughan, 2014, Structure.

Crystal structure of a human VH: requirements for maintaining a monomeric fragment.

T. Dottorini, M. Walsh, C. Vaughan, 2004, Biochemistry.

Structural Studies of the Hsp 90-Cdc 37 Complex Using EPR Spectroscopy

C. Vaughan, 2017 .

Chaperone ligand-discrimination by the TPR-domain protein Tah1

L. Pearl, P. Piper, C. Prodromou, 2008, The Biochemical journal.

The Enzyme-Like Domain of Arabidopsis Nuclear β-Amylases Is Critical for DNA Sequence Recognition and Transcriptional Activation[C][W][OPEN]

Luise H. Brand, D. Wanke, S. Zeeman, 2014, Plant Cell.

Measurement of protein-ligand complex formation.

C. Vaughan, T. Daviter, P. N. Lowe, 2013, Methods in molecular biology.

Phosphorylation and Ubiquitination Regulate Protein Phosphatase 5 Activity and Its Prosurvival Role in Kidney Cancer.

Andrew W. Truman, Timothy A. J. Haystead, Mehdi Mollapour, 2017, Cell reports.

Structure of an Hsp90-Cdc37-Cdk4 complex.

L. Pearl, C. Robinson, H. Saibil, 2006, Molecular cell.

Structure of an Hsp 90-Cdc 37-Cdk 4 complex

L. Pearl, C. Robinson, H. Saibil, 2017 .

Structural response to mutation at a protein-protein interface.

A. Fersht, A. Buckle, C. Vaughan, 1998, Journal of molecular biology.

Insights into Centromere DNA Bending Revealed by the Cryo-EM Structure of the Core Centromere Binding Factor 3 with Ndc10

C. Vaughan, Cara K. Vaughan, Wenjuan Zhang, 2018, Cell reports.

3.7 Å cryo-EM structure of the core Centromere Binding Factor 3 complex

C. Vaughan, Wenjuan Zhang, N. Lukoynova, 2017, bioRxiv.

Understanding of the Hsp90 molecular chaperone reaches new heights

P. Piper, L. Neckers, C. Vaughan, 2010, Nature Structural &Molecular Biology.

The crystal structure of the Sgt1-Skp1 complex: the link between Hsp90 and both SCF E3 ubiquitin ligases and kinetochores

K. Thalassinos, C. Vaughan, T. Daviter, 2017, Scientific Reports.

DNA-PK and the TRF2 iDDR inhibit MRN-initiated resection at leading-end telomeres

T. Paull, Kaori Takai, Peng Wu, 2023, bioRxiv.

The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis

Stephen W. Wilson, Thomas A. Hawkins, W. Talbot, 2008, Development.

A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.

A. Fersht, A. Buckle, C. Vaughan, 2002, Acta crystallographica. Section D, Biological crystallography.

Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery

L. Pearl, P. Piper, C. Liao, 2004, The EMBO journal.

Structural and functional basis of protein phosphatase 5 substrate specificity

D. Bourboulia, D. Dunn, M. Mollapour, 2016, Proceedings of the National Academy of Sciences.

Structural and Functional Basis of PP 5 Ser / Thr Phosphatase Substrate Specificity

Dimitra, D. Dunn, M. Mollapour, 2016 .

Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity.

L. Pearl, P. Piper, L. Neckers, 2011, Molecular cell.

Structural and Functional Analysis of the Middle Segment of Hsp 90 : Implications for ATP Hydrolysis and Client

L. Pearl, P. Piper, S. Roe, 2003 .

β-AMYLASE4, a Noncatalytic Protein Required for Starch Breakdown, Acts Upstream of Three Active β-Amylases in Arabidopsis Chloroplasts[W][OA]

K. Halliday, Alison M. Smith, S. Zeeman, 2008, The Plant Cell Online.