S. Freund

发表

Quaternary structures of tumor suppressor p53 and a specific p53–DNA complex

A. Fersht, M. Valle, D. Svergun, 2007, Proceedings of the National Academy of Sciences.

Domain–domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy

Michal Bista, A. Fersht, S. Freund, 2012, Proceedings of the National Academy of Sciences.

Effects of Oncogenic Mutations and DNA Response Elements on the Binding of p53 to p53-binding Protein 2 (53BP2)*

Henning Tidow, A. Fersht, D. Veprintsev, 2006, Journal of Biological Chemistry.

Core domain interactions in full-length p53 in solution

Antonina Andreeva, Alan R. Fersht, Dmitry B. Veprintsev, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Interaction of the p53 DNA-Binding Domain with Its N-Terminal Extension Modulates the Stability of the p53 Tetramer

Alan R. Fersht, Carol V. Robinson, Andreas C. Joerger, 2011, Journal of molecular biology.

Solution structure of p53 core domain: Structural basis for its instability

Alan R. Fersht, Henning Tidow, A. Fersht, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Characterization of the p53-rescue drug CP-31398 in vitro and in living cells

Galina Selivanova, A. Fersht, K. Wiman, 2002, Oncogene.

A peptide that binds and stabilizes p53 core domain: Chaperone strategy for rescue of oncogenic mutants

A. Fersht, M. Proctor, D. Veprintsev, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Two sequence motifs from HIF-1α bind to the DNA-binding site of p53

A. Fersht, S. Freund, S. Rüdiger, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Hot-spot mutants of p53 core domain evince characteristic local structural changes.

M Bycroft, A. Fersht, M. Bycroft, 1999, Proceedings of the National Academy of Sciences of the United States of America.

An ensemble view of thrombin allostery

S. Freund, B. C. Lechtenberg, J. Huntington, 2012, Biological chemistry.

Molecular mechanism of the interaction between MDM2 and p53.

A. Fersht, M. Bycroft, S. Freund, 2002, Journal of molecular biology.

Biophysical characterizations of human mitochondrial transcription factor A and its binding to tumor suppressor p53

A. Fersht, S. Freund, T. Rutherford, 2009, Nucleic acids research.

Biophysical characterization of elongin C from Saccharomyces cerevisiae.

A. Fersht, M. Bycroft, M. Proctor, 2000, Biochemistry.

The complete folding pathway of a protein from nanoseconds to microseconds

Valerie Daggett, Alan R. Fersht, J. Günter Grossmann, 2003, Nature.

Deconvoluting Protein (Un)folding Structural Ensembles Using X-Ray Scattering, Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulation

A. Menzel, A. Fersht, D. van der Spoel, 2015, PloS one.

Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding.

C. J. Bond, A. Fersht, V. Daggett, 2000, Journal of molecular biology.

NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation

S. Freund, B. C. Lechtenberg, J. Huntington, 2010, Proceedings of the National Academy of Sciences.

The Solution Structure of the S1 RNA Binding Domain: A Member of an Ancient Nucleic Acid–Binding Fold

Mark Proctor, T. Hubbard, A. Murzin, 1997, Cell.

Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne

P. R. Elliott, H. Ovaa, J. Burke, 2016, Nature.

OTU Deubiquitinases Reveal Mechanisms of Linkage Specificity and Enable Ubiquitin Chain Restriction Analysis

P. R. Elliott, H. Ovaa, S. Freund, 2013, Cell.

Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne

David Komander, S. Freund, D. Komander, 2010, Nature Structural &Molecular Biology.

Lys 11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase

S. Freund, D. Komander, Anja Bremm, 2010 .

Role of Conformational Heterogeneity in Domain Swapping and Adapter Function of the Cks Proteins*

M. Karplus, M. Bycroft, L. Itzhaki, 2005, Journal of Biological Chemistry.

Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis

M. Bycroft, A. Buckle, S. Freund, 2015, Protein engineering, design & selection : PEDS.

The ligand-binding loops in the tunicate C-type lectin TC14 are rigid.

M. Bycroft, M. Howard, S. Freund, 2001, Biochemistry.

Crystal Structures of Engrailed Homeodomain Mutants

A. Fersht, L. Federici, S. Lovell, 2003, Journal of Biological Chemistry.

Features critical for membrane binding revealed by DivIVA crystal structure

T. Leonard, J. Löwe, L. Hamoen, 2010, The EMBO journal.

Thermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core protein

N. Ferguson, S. Freund, Crispin G. Alexander, 2013, Proceedings of the National Academy of Sciences.

Mechanism of completion of peptidyltransferase centre assembly in eukaryotes

Florian Stengel, S. Freund, A. Andreeva, 2019, eLife.

Molecular mechanism of Mad1 kinetochore targeting by phosphorylated Bub1

D. Barford, S. Freund, A. Wagner, 2021, EMBO reports.

Uncoupling of GTP hydrolysis from eIF6 release on the ribosome causes Shwachman-Diamond syndrome.

Charles Boone, M. Costanzo, S. Freund, 2011, Genes & development.

Assembly and Specific Recognition of K29- and K33-Linked Polyubiquitin

P. R. Elliott, J. Pruneda, S. Freund, 2015, Molecular cell.

CCDC61/VFL3 Is a Paralog of SAS6 and Promotes Ciliary Functions

T. Blundell, Christopher M Johnson, S. Jackson, 2020, Structure.

Juxtaposition of Bub1 and Cdc20 on phosphorylated Mad1 during catalytic mitotic checkpoint complex assembly

D. Barford, A. Heck, S. Freund, 2022, bioRxiv.

Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly

Christopher M Johnson, C. Robinson, L. Pelletier, 2018, Nature Communications.

SPATA2 Links CYLD to LUBAC, Activates CYLD, and Controls LUBAC Signaling

P. R. Elliott, S. Freund, D. Komander, 2016, Molecular cell.

An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1

J. Pruneda, S. Freund, D. Komander, 2017, The EMBO journal.

The native structure of the assembled matrix protein 1 of influenza A virus

J. Briggs, X. Xiong, W. Wan, 2020, Nature.

Distinct USP25 and USP28 Oligomerization States Regulate Deubiquitinating Activity

B. Graves, S. Freund, D. Komander, 2019, Molecular cell.

Disease-Associated Mutations in CEP120 Destabilize the Protein and Impair Ciliogenesis

Christopher M Johnson, F. Gergely, S. Freund, 2018, Cell reports.

Crystal Structures and Nuclear Magnetic Resonance Studies of the Apo Form of the c-MYC:MAX bHLHZip Complex Reveal a Helical Basic Region in the Absence of DNA

M. Bycroft, S. Freund, M. Allen, 2019, Biochemistry.

Molecular Basis and Regulation of OTULIN-LUBAC Interaction

P. R. Elliott, S. V. Nielsen, N. Mailand, 2014, Molecular cell.

The topology, structure and PE interaction of LITAF underpin a Charcot-Marie-Tooth disease type 1C

E. Garman, S. Freund, R. Roberts, 2016, BMC Biology.

A molecular mechanism for membrane chaperoning by a late embryogenesis abundant protein

D. Green, M. Babu, Christopher M Johnson, 2022, bioRxiv.

The SWI/SNF Subunit INI1 Contains an N-Terminal Winged Helix DNA Binding Domain that Is a Target for Mutations in Schwannomatosis

M. Bycroft, S. Freund, M. Allen, 2015, Structure.

Bacterial divisome protein FtsA forms curved antiparallel double filaments upon binding FtsN

J. Chin, J. Löwe, S. Freund, 2022, Nature Microbiology.

The native structure of assembled influenza A virus M1 matrix protein

Calder, X. Xiong, W. Wan, 2020 .

The UBAP1 Subunit of ESCRT-I Interacts with Ubiquitin via a SOUBA Domain

M. Bycroft, Roger L. Williams, K. Hofmann, 2012, Structure.

An intrinsically labile α-helix abutting the BCL9-binding site of β-catenin is required for its inhibition by carnosic acid

M. Bienz, D. Veprintsev, S. Freund, 2012, Nature Communications.

Moving towards high-resolution descriptions of the molecular interactions and structural rearrangements of the human hepatitis B core protein.

N. Ferguson, S. Freund, Christopher M. Johnson, 2008, Journal of molecular biology.

Comparative Biophysical Characterization of p53 with the Pro-apoptotic BAK and the Anti-apoptotic BCL-xL*

A. Fersht, S. Freund, B. Sot, 2007, Journal of Biological Chemistry.

LC3C, Bound Selectively by a Noncanonical LIR Motif in NDP52, Is Required for Antibacterial Autophagy

S. Bloor, S. Freund, T. Rutherford, 2012, Molecular cell.

Characterisation of the BRCT domains of the breast cancer susceptibility gene product BRCA1.

L. Itzhaki, H. Wilkinson, J. Schymkowitz, 2002, Journal of molecular biology.

Solution structure of the nonmethyl‐CpG‐binding CXXC domain of the leukaemia‐associated MLL histone methyltransferase

M. Bycroft, S. Freund, M. Allen, 2006, The EMBO journal.

Interaction of the p 53 DNA-Binding Domain with Its N-Terminal Extension Modulates the Stability of the p 53 Tetramer

A. Fersht, C. Robinson, A. Joerger, 2011 .

Structure and stability of an immunoglobulin superfamily domain from twitchin, a muscle protein of the nematode Caenorhabditis elegans.

C. Chothia, M. Bycroft, J. Clarke, 1996, Journal of molecular biology.

Periphilin self-association underpins epigenetic silencing by the HUSH complex

Y. Modis, P. Lehner, S. Freund, 2019, bioRxiv.

Molecular basis of the interactions between the p73 N terminus and p300: Effects on transactivation and modulation by phosphorylation

Sarah W. Burge, A. Fersht, M. Bycroft, 2009, Proceedings of the National Academy of Sciences.

Solution structure of the BRK domains from CHD7.

M. Bycroft, S. Freund, M. Allen, 2007, Journal of molecular biology.

Molecular basis of histone H3K36me3 recognition by the PWWP domain of Brpf1

Berthold Göttgens, B. Göttgens, M. Bycroft, 2010, Nature Structural &Molecular Biology.

The FtsK γ domain directs oriented DNA translocation by interacting with KOPS

M. Bycroft, D. Sherratt, J. Löwe, 2006, Nature Structural &Molecular Biology.

Solution structure of the FCS zinc finger domain of the human polycomb group protein L(3)mbt‐like 2

M. Bycroft, S. Freund, T. Rutherford, 2009, Protein science : a publication of the Protein Society.

Bipartite binding and partial inhibition links DEPTOR and mTOR in a mutually antagonistic embrace

Roger L. Williams, G. Murshudov, S. Freund, 2021, bioRxiv.

Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core

A. Fersht, A. Joerger, S. Freund, 2009, Protein engineering, design & selection : PEDS.

FtsA forms actin‐like protofilaments

J. Löwe, S. Freund, P. Szwedziak, 2012, The EMBO journal.

The FtsK gamma domain directs oriented DNA translocation by interacting with KOPS.

M. Bycroft, D. Sherratt, J. Löwe, 2006, Nature structural & molecular biology.

The V86M mutation in HIV-1 capsid confers resistance to TRIM5α by abrogation of cyclophilin A-dependent restriction and enhancement of viral nuclear import

L. James, S. Freund, L. Berthoux, 2013, Retrovirology.

Diverse HIV viruses are targeted by a conformationally dynamic antiviral

L. James, S. Freund, G. Towers, 2012, Nature Structural &Molecular Biology.

HIV-1 capsid undergoes coupled binding and isomerization by the nuclear pore protein NUP358

L. James, T. Schaller, S. Freund, 2013, Retrovirology.

Structure of PINK1 in complex with its substrate ubiquitin

E. Pardon, J. Steyaert, S. Freund, 2017, Nature.

The dependence of chemical exchange on boundary selection in a fibronectin type III domain from human tenascin.

V. Arcus, J. Clarke, S. Freund, 1998, Journal of molecular biology.

The central region of HDM2 provides a second binding site for p53

A. Fersht, D. Veprintsev, S. Freund, 2006, Proceedings of the National Academy of Sciences of the United States of America.

A Role for the ESCRT System in Cell Division in Archaea

Roger L. Williams, S. Bell, S. Freund, 2008, Science.

TASOR is a pseudo-PARP that directs HUSH complex assembly and epigenetic transposon control

Anna V. Protasio, Y. Modis, P. Lehner, 2020, Nature Communications.

High-resolution NMR structures of the domains of Saccharomyces cerevisiae Tho1

M. Bycroft, S. Freund, M. Allen, 2014, Acta crystallographica. Section F, Structural biology communications.

Modulation of binding of DNA to the C-terminal domain of p53 by acetylation.

A. Fersht, D. Veprintsev, S. Freund, 2005, Structure.

CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90

A. Fersht, D. Veprintsev, S. Freund, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53

A. Fersht, M. Bycroft, S. Freund, 2007, Proceedings of the National Academy of Sciences.

Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding.

A. Fersht, D. Veprintsev, S. Freund, 2002, Journal of molecular biology.

Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions.

S. Freund, P D Barker, P. Barker, 1996, Biochemistry.

Conversion of cytochrome b562 to c-type cytochromes.

S. Freund, I. Fearnley, P D Barker, 1995, Biochemistry.

Molecular Basis for Modulation of the p53 Target Selectivity by KLF4

D. Veprintsev, S. Freund, T. Brandt, 2012, PloS one.

Physical and functional interactions between human mitochondrial single-stranded DNA-binding protein and tumour suppressor p53

A. Fersht, S. Freund, Miriana Petrovich, 2008, Nucleic acids research.

Physical and functional interactions between human mitochondrial single-stranded DNA-binding protein and tumour suppressor p 53

A. Fersht, S. Freund, Miriana Petrovich, 2009 .

Regulation of DNA binding of p53 by its C-terminal domain.

A. Fersht, M. Bycroft, R. Weinberg, 2004, Journal of molecular biology.

Assembly, analysis and architecture of atypical ubiquitin chains

S. Freund, D. Komander, M. Hospenthal, 2013, Nature Structural &Molecular Biology.

The hepatitis B virus preS1 domain hijacks host trafficking proteins by motif mimicry.

Neil Ferguson, N. Ferguson, Christopher M Johnson, 2013, Nature chemical biology.

Binding of p53-derived ligands to MDM2 induces a variety of long range conformational changes.

A. Fersht, S. Freund, A. Friedler, 2004, Journal of molecular biology.

Dynamics in Fip1 regulate eukaryotic mRNA 3′ end processing

L. Passmore, S. Freund, Juan B. Rodríguez-Molina, 2021, bioRxiv.

Assignment of the backbone 1H,15N, 13C NMR resonances and secondary structure of a double‐stranded RNA binding domain from the Drosophila protein staufen

M. Bycroft, M. Proctor, D. Johnston, 1995, FEBS letters.

Separating the contributions to 15N transverse relaxation in a fibronectin type III domain

S. Freund, A. E. Meekhof, Alison E. Meekhof, 1999, Journal of biomolecular NMR.

Probing residual structure and backbone dynamics on the milli- to picosecond timescale in a urea-denatured fibronectin type III domain.

S. Freund, A. E. Meekhof, 1999, Journal of molecular biology.

NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.

A. Fersht, S. Freund, K. B. Wong, 1997, Journal of molecular biology.

The native structure of the full-length, assembled influenza A virus matrix protein, M1

J. Briggs, X. Xiong, W. Wan, 2020, bioRxiv.

Regulation of CYLD activity and specificity by phosphorylation and ubiquitin-binding CAP-Gly domains

P. R. Elliott, S. Freund, D. Komander, 2021, Cell reports.

The denatured state of Engrailed Homeodomain under denaturing and native conditions.

A. Fersht, S. Freund, U. Mayor, 2003, Journal of molecular biology.

Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy.

A. Fersht, M. Bycroft, S. Freund, 1994, Biochemistry.

NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.

A. Fersht, S. Freund, N. Kobayashi, 1999, Journal of molecular biology.

RNA recognition by a Staufen double‐stranded RNA‐binding domain

Gabriele Varani, Andres Ramos, Stefan Freund, 2000, The EMBO journal.

A low-complexity region in the YTH domain protein Mmi1 enhances RNA binding

L. Passmore, S. Freund, Minmin Yu, 2018, The Journal of Biological Chemistry.

Structural basis of p63α SAM domain mutants involved in AEC syndrome

M. Bycroft, S. Freund, M. Allen, 2011, The FEBS journal.

The bacterial actin-like cell division protein FtsA forms curved antiparallel double filaments upon binding of FtsN

J. Chin, J. Löwe, S. Freund, 2021, bioRxiv.

Interaction between the Transactivation Domain of p53 and PC4 Exemplifies Acidic Activation Domains as Single-stranded DNA Mimics

A. Fersht, S. Freund, A. Andreeva, 2009, The Journal of Biological Chemistry.

Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis

David Komander, Christopher M Johnson, J. Pruneda, 2014, The EMBO journal.

ANXA11 biomolecular condensates facilitate protein-lipid phase coupling on lysosomal membranes

Michael S. Fernandopulle, E. Derivery, M. Vendruscolo, 2023, bioRxiv.

An ‘invisible’ ubiquitin conformation is required for efficient phosphorylation by PINK1

J. Pruneda, S. Freund, D. Komander, 2017, bioRxiv.

The native structure of the assembled matrix protein 1 of influenza A virus

J. Briggs, X. Xiong, W. Wan, 2020, Nature.

A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding.

V L Arcus, M Bycroft, A. Fersht, 1995, Journal of molecular biology.

Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state.

A. Fersht, M. Bycroft, V. Arcus, 1994, Proceedings of the National Academy of Sciences of the United States of America.

Solution structure of a protein denatured state and folding intermediate

A. R. Fersht, U. Mayor, A. Fersht, 2005, Nature.

The topology, structure and PE interaction of LITAF underpin a Charcot-Marie-Tooth disease type 1C

E. Garman, S. Freund, R. Roberts, 2016, BMC Biology.

GpIbα Interacts Exclusively with Exosite II of Thrombin☆

S. Freund, B. C. Lechtenberg, J. Huntington, 2014, Journal of molecular biology.

Binding of EMSY to HP1β: implications for recruitment of HP1β and BS69

L. Itzhaki, T. Kouzarides, C. Ekblad, 2005 .

Binding of EMSY to HP1beta: implications for recruitment of HP1beta and BS69.

L. Itzhaki, T. Kouzarides, C. Ekblad, 2005, EMBO reports.

Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: implications for "mutant conformation".

A. Fersht, B. DeDecker, S. Freund, 2004, Journal of molecular biology.

Self-correcting mismatches during high-fidelity DNA replication

Sjors H W Scheres, M. Lamers, S. Scheres, 2017, Nature Structural &Molecular Biology.

Regulation of Dishevelled DEP domain swapping by conserved phosphorylation sites

H. Pelham, M. Gammons, M. Bienz, 2021, Proceedings of the National Academy of Sciences.

Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution

Valerie Daggett, Alan R. Fersht, A. Fersht, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Characterisation of urea-denatured states of an immunoglobulin superfamily domain by heteronuclear NMR.

M. Bycroft, J. Clarke, S. Freund, 1998, Journal of molecular biology.

Initiation sites of protein folding by NMR analysis.

A. Fersht, S. Freund, K. B. Wong, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.

A. Fersht, S. Freund, K. B. Wong, 1996, Journal of molecular biology.

Disease-specific tau filaments assemble via polymorphic intermediates

A. Murzin, M. Goedert, S. Scheres, 2023, bioRxiv.

SWI/SNF subunit BAF155 N-terminus structure informs the impact of cancer-associated mutations and reveals a potential drug binding site

M. Bycroft, S. Freund, M. Allen, 2021, Communications biology.

An essential role for the ATG8 ortholog LC3C in antibacterial autophagy

S. Bloor, S. Freund, T. Rutherford, 2013, Autophagy.

The malignant brain tumor repeats of human SCML2 bind to peptides containing monomethylated lysine.

M. Bycroft, S. Freund, M. Allen, 2008, Journal of molecular biology.

Structure of PINK1 in complex with its substrate ubiquitin

E. Pardon, J. Steyaert, S. Freund, 2017, Nature.

Real‐time nmr studies on a transient folding intermediate of barstar

A. Fersht, S. Freund, T. Killick, 1999, Protein science : a publication of the Protein Society.

Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly

C. Robinson, L. Pelletier, B. Raught, 2018, Nature Communications.

Structural basis of p63α SAM domain mutants involved in AEC syndrome

M. Bycroft, S. Freund, M. Allen, 2011, The FEBS journal.