J. Potts

发表

Structural and Functional Analysis of the Tandem β-Zipper Interaction of a Streptococcal Protein with Human Fibronectin*♦

Richard P. O. Jones, N. Norris, R. Bingham, 2011, The Journal of Biological Chemistry.

The tandem β‐zipper: Modular binding of tandem domains and linear motifs

J. Matthews, J. Potts, 2013, FEBS letters.

Defining the remarkable structural malleability of a bacterial surface protein Rib domain implicated in infection

A. Bateman, E. Paci, F. Whelan, 2019, Proceedings of the National Academy of Sciences.

The effect of nitrogen limitation on catabolite repression of amidase, histidase and urocanase in Pseudomonas aeruginosa.

J. Potts, P. H. Clarke, 1976, Journal of general microbiology.

Binding of a peptide from a Streptococcus dysgalactiae MSCRAMM to the N‐terminal F1 module pair of human fibronectin involves both modules

I. Campbell, J. Potts, M. Höök, 2001, FEBS letters.

Furanose-specific Sugar Transport

Richard S. P. Horler, G. Thomas, K. Wilson, 2009, The Journal of Biological Chemistry.

Structure and function of fibronectin modules.

I D Campbell, I. Campbell, J. Potts, 1996, Matrix biology : journal of the International Society for Matrix Biology.

Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs

L. Visai, Nicola A. G. Meenan, M. Humphries, 2016, PloS one.

Divergence of Catalytic Mechanism within a Glycosidase Family Provides Insight into Evolution of Carbohydrate Metabolism by Human Gut Flora

B. Henrissat, J. Turkenburg, J. Potts, 2008, Chemistry & biology.

Staphylococcal biofilm-forming protein has a contiguous rod-like structure

J. Clarke, R. Bingham, A. Leech, 2012, Proceedings of the National Academy of Sciences.

Role of Surface Protein SasG in Biofilm Formation by Staphylococcus aureus

J. Potts, T. Foster, J. O’Gara, 2010, Journal of bacteriology.

Diverse functions for acyltransferase-3 proteins in the modification of bacterial cell surfaces

G. Thomas, M. W. van der Woude, J. Potts, 2022, Microbiology.

The Tandem β-Zipper Model Defines High Affinity Fibronectin-binding Repeats within Staphylococcus aureus FnBPA*

L. Visai, Nicola A. G. Meenan, N. Norris, 2007, Journal of Biological Chemistry.

Anomeric preference of fluoroglucose exchange across human red-cell membranes. 19F-n.m.r. studies.

P. Kuchel, J. Potts, 1992, The Biochemical journal.

The 4-hydroxylation of cinnamic acid by sorghum microsomes and the requirement for cytochrome P-450.

J. Potts, E. Conn, R. Weklych, 1974, The Journal of biological chemistry.

Role of Surface Protein SasG in Bioﬁlm Formation by Staphylococcus aureus (cid:1)

J. Potts, T. Foster, J. O’Gara, 2010 .

Coordinated induction and subsequent activity changes of two groups of metabolically interrelated enzymes. Light-induced synthesis of flavonoid glycosides in cell suspension cultures of Petroselinum hortense.

J. Potts, F. Kreuzaler, K. Hahlbrock, 1976, European journal of biochemistry.

Preparation of isotopically labeled recombinant fragments of fibronectin for functional and structural study by heteronuclear nuclear magnetic resonance spectroscopy.

I. Campbell, J. Potts, J. Bright, 2000, Methods in molecular biology.

Exchange of fluorinated glucose across the red-cell membrane measured by 19F-n.m.r. magnetization transfer.

P. Kuchel, J. Potts, A. Hounslow, 1990, The Biochemical journal.

A Novel Fibronectin Binding Motif in MSCRAMMs Targets F3 Modules

J. Potts, Xiaowen Liang, M. Höök, 2009, PloS one.

Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper.

I. Campbell, J. Briggs, J. Potts, 2003, Nature.

Characterization of the transport of the nonelectrolyte dimethyl methylphosphonate across the red cell membrane

P. Kuchel, J. Potts, K. Kirk, 1989, NMR in biomedicine.

Staphylococcus aureus Keratinocyte Invasion Is Dependent upon Multiple High-Affinity Fibronectin-Binding Repeats within FnBPA

Nicola A. G. Meenan, J. Potts, A. Edwards, 2011, PloS one.

Anion channel blockers inhibit swelling-activated anion, cation, and nonelectrolyte transport in HeLa cells.

K. Kirk, J. Potts, J. Hall, 1996, The American journal of physiology.

Staphylococcus aureus Host Cell Invasion and Virulence in Sepsis Is Facilitated by the Multiple Repeats within FnBPA

J. Potts, A. Edwards, E. Josefsson, 2010, PLoS pathogens.

Sialic Acid Mutarotation Is Catalyzed by the Escherichia coli β-Propeller Protein YjhT*

G. Thomas, K. Wilson, A. Müller, 2008, Journal of Biological Chemistry.

Fibronectin-binding proteins of gram-positive cocci.

Ulrich Schwarz-Linek, J. Potts, M. Höök, 2006, Microbes and infection.

Glucose transport in human erythrocytes measured using 13C NMR spin transfer

P. Kuchel, J. Potts, B. Chapman, 1987, FEBS letters.

High-resolution structural studies of the factor Xllla crosslinking site and the first type 1 module of fibronectin

I. Campbell, J. Potts, I. Phan, 1995, Nature Structural Biology.

Fibronectin structure and assembly.

I. Campbell, J. Potts, 1994, Current opinion in cell biology.

Cooperative Binding and Activation of Fibronectin by a Bacterial Surface Protein*

D. Staunton, J. Potts, R. Hagan, 2010, The Journal of Biological Chemistry.

The Streptococcal Binding Site in the Gelatin-binding Domain of Fibronectin Is Consistent with a Non-linear Arrangement of Modules

I. Campbell, M. Erat, D. Staunton, 2010, The Journal of Biological Chemistry.

Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains

Elspeth F Garman, Ulrich Schwarz-Linek, Nicola A. G. Meenan, 2008, Proceedings of the National Academy of Sciences.

High Affinity Streptococcal Binding to Human Fibronectin Requires Specific Recognition of Sequential F1 Modules*

I. Campbell, J. Potts, M. Höök, 2004, Journal of Biological Chemistry.

The molecular basis of fibronectin‐mediated bacterial adherence to host cells

J. Potts, M. Höök, U. Schwarz-Linek, 2004, Molecular microbiology.

Pathogenic bacteria attach to human fibronectin through a tandem β-zipper

I. Campbell, J. Briggs, J. Potts, 2003, Nature.

Evidence for Steric Regulation of Fibrinogen Binding to Staphylococcus aureus Fibronectin-binding Protein A (FnBPA)

Richard P. O. Jones, A. Leech, J. Turkenburg, 2014, The Journal of Biological Chemistry.

(FnBPA) Fibronectin-binding Protein A aureus Staphylococcus Fibrinogen Binding to Evidence for Steric Regulation of Protein Structure and Folding:

Richard P. O. Jones, A. Leech, J. Turkenburg, 2014 .

DNA recognition for virus assembly through multiple sequence-independent interactions with a helix-turn-helix motif

Huw T Jenkins, Herman K. H. Fung, A. Antson, 2015, Nucleic acids research.

Location of genes for the utilization of acetamide, histidine and proline on the chromosome of Pseudomonas aeruginosa

J. Potts, P. H. Clarke, M. Day, 1975 .

Periscope Proteins are variable-length regulators of bacterial cell surface interactions

A. Bateman, E. Paci, F. Whelan, 2020, Proceedings of the National Academy of Sciences.

Arabidopsis Glutathione Transferases U24 and U25 Exhibit a Range of Detoxification Activities with the Environmental Pollutant and Explosive, 2,4,6-Trinitrotoluene1[C][W][OPEN]

J. Potts, N. Bruce, E. Rylott, 2014, Plant Physiology.

The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core

Konrad Zdanowski, Shabaz Mohammed, Connor Sharp, 2016, Nature Communications.

Acetylation of Surface Carbohydrates in Bacterial Pathogens Requires Coordinated Action of a Two-Domain Membrane-Bound Acyltransferase

A. Bateman, G. Thomas, M. W. van der Woude, 2020, mBio.

Structural insight into binding of Staphylococcus aureus to human fibronectin

I. Campbell, Nicola A. G. Meenan, J. Potts, 2006, FEBS letters.

Borrelia burgdorferi Binds Fibronectin through a Tandem β-Zipper, a Common Mechanism of Fibronectin Binding in Staphylococci, Streptococci, and Spirochetes*

J. Potts, H. Jenkins, M. Höök, 2005, Journal of Biological Chemistry.

Solution structure of a pair of modules from the gelatin-binding domain of fibronectin.

I D Campbell, I. Campbell, J. Potts, 1999, Structure.

Rational design and self-assembly of coiled-coil linked SasG protein fibrils.

Daniel T. Peters, L. Regan, A. Rawlings, 2020, ACS synthetic biology.

Two flavonoid-specific malonyltransferases from cell suspension cultures of Petroselinum hortense: partial purification and some properties of malonyl-coenzyme A: flavone/flavonol-7-O-glycoside malonyltransferase and malonyl-coenzyme A: flavonol-3-O-glucoside malonyltransferase.

J. Potts, U. Matern, K. Hahlbrock, 1981, Archives of biochemistry and biophysics.

The solution and crystal structures of a module pair from the Staphylococcus aureus-binding site of human fibronectin--a tale with a twist.

G. Sheldrick, E. Rudiño-Piñera, R. Ravelli, 2007, Journal of molecular biology.

Solution structure of a PAN module from the apicomplexan parasite Eimeria tenella

I. Campbell, P. Brown, J. Potts, 2004, Journal of Structural and Functional Genomics.

Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein

Herman K. H. Fung, E. Paci, J. Clarke, 2015, Nature Communications.

Borrelia burgdorferi Protein BBK32 Binds to Soluble Fibronectin via the N-terminal 70-kDa Region, Causing Fibronectin to Undergo Conformational Extension*

G. Harris, J. Potts, D. Mosher, 2014, The Journal of Biological Chemistry.

Two repetitive, biofilm-forming proteins from Staphylococci: from disorder to extension.

F. Whelan, J. Potts, 2015, Biochemical Society transactions.

Twinned or not twinned, that is the question: crystallization and preliminary crystallographic analysis of the 2F1(3)F1 module pair of human fibronectin.

E. Rudiño-Piñera, E. Garman, J. Potts, 2004, Acta crystallographica. Section D, Biological crystallography.

Solution structure of the glycosylated second type 2 module of fibronectin.

I D Campbell, I. Campbell, J. Potts, 1998, Journal of molecular biology.

Solution structure of a type 2 module from fibronectin: implications for the structure and function of the gelatin-binding domain.

I. Campbell, J. Potts, I. Phan, 1997, Structure.

Multi-factorial modulation of IGD motogenic potential in MSF (migration stimulating factor).

Nicola A. G. Meenan, D. Staunton, J. Potts, 2010, Experimental cell research.

Staphylococcal Periscope proteins Aap, SasG, and Pls project noncanonical legume-like lectin adhesin domains from the bacterial surface

F. Whelan, G. Harris, J. Turkenburg, 2023, The Journal of biological chemistry.

BBK32, a Fibronectin Binding MSCRAMM from Borrelia burgdorferi, Contains a Disordered Region That Undergoes a Conformational Change on Ligand Binding*

Barbara J. B. Johnson, J. Potts, M. Höök, 2004, Journal of Biological Chemistry.

Investigating the Structural Compaction of Biomolecules Upon Transition to the Gas-Phase Using ESI-TWIMS-MS

S. Radford, F. Whelan, A. Ashcroft, 2017, Journal of The American Society for Mass Spectrometry.

Fibronectin structure: a new piece of the puzzle emerges.

R. Bingham, J. Potts, 2010, Structure.

Intrinsically disordered proteins: administration not executive.

M. Williamson, J. Potts, 2012 .

A different path: Revealing the function of staphylococcal proteins in biofilm formation

G. H. Thomas, J. Potts, S. Macdonald, 2014, FEBS letters.

The phenomenon of separate intra‐ and extracellular resonances of difluorophosphate in 31P and 19F NMR spectra of erythrocytes

P. Kuchel, J. Potts, A. Xu, 1991, Magnetic resonance in medicine.

Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE)

M. Deschamps, I. Campbell, J. Potts, 2005, Journal of biomolecular NMR.

Urea exchange across the human erythrocyte membrane measured using 13C NMR lineshape analysis

P. Kuchel, B. T. Bulliman, J. Potts, 2004, European Biophysics Journal.

Recent Developments in Biomolecular NMR

J. Potts, M. Clore, 2012 .

Role of Surface Protein SasG in Biofilm Formation by Staphylococcus aureus

J. Potts, T. Foster, J. O’Gara, 2010, Journal of bacteriology.

Disorder drives cooperative folding in a multidomain protein

Jane Clarke, Emanuele Paci, E. Paci, 2016, Proceedings of the National Academy of Sciences.

1 Disorder drives cooperative folding in a multi-domain protein

E. Paci, J. Clarke, F. Whelan, 2016 .

Solution structure of the N-terminal F1 module pair from human fibronectin.

I D Campbell, I. Campbell, J. Potts, 1999, Biochemistry.