J. Lott

发表

The TB Structural Genomics Consortium: a decade of progress.

D. Eisenberg, M. James, J. Sacchettini, 2011, Tuberculosis.

A highly conserved transcriptional repressor controls a large regulon involved in lipid degradation in Mycobacterium smegmatis and Mycobacterium tuberculosis

Ben Sidders, Gurdyal S Besra, G. Besra, 2007, Molecular microbiology.

Cholesterol utilization in mycobacteria is controlled by two TetR-type transcriptional regulators: kstR and kstR2

Sharon L. Kendall, Neil G. Stoker, J. Lott, 2010, Microbiology.

A single WW domain is the predominant mediator of the interaction between the human ubiquitin-protein ligase Nedd4 and the human epithelial sodium channel.

Fiona J. McDonald, P. Teesdale-Spittle, J. Lott, 2002 .

The cloning, expression and crystallisation of a thermostable arginase

E. Baker, M. Bewley, J. Lott, 1996, FEBS letters.

Prediction of the substrate for nonribosomal peptide synthetase (NRPS) adenylation domains by virtual screening

V. Arcus, J. Lott, Richard D. Johnson, 2015, Proteins.

Combining cross-crystal averaging and MRSAD to phase a 4354-amino-acid structure.

J. Lott, S. Panjikar, J. Busby, 2016, Acta crystallographica. Section D, Structural biology.

Teneurin Structures Are Composed of Ancient Bacterial Protein Domains

J. Lott, E. Seiradake, B. Janssen, 2019, Front. Neurosci..

Anthranilate phosphoribosyltransferase: Binding determinants for 5'-phospho-alpha-d-ribosyl-1'-pyrophosphate (PRPP) and the implications for inhibitor design.

E. Baker, E. Parker, J. Lott, 2018, Biochimica et biophysica acta. Proteins and proteomics.

Repurposing the Chemical Scaffold of the Anti‐Arthritic Drug Lobenzarit to Target Tryptophan Biosynthesis in Mycobacterium tuberculosis

S. Gamage, W. Denny, E. Baker, 2014, Chembiochem : a European journal of chemical biology.

Using secretion to solve a solubility problem: high-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGase F.

J. Lott, G. Norris, M. L. Patchett, 2002, Protein expression and purification.

The structure and unusual protein chemistry of hypoxic response protein 1, a latency antigen and highly expressed member of the DosR regulon in Mycobacterium tuberculosis.

E. Baker, J. Lott, Chen Gao, 2008, Journal of molecular biology.

Making sense of a missense mutation: characterization of MutT2, a Nudix hydrolase from Mycobacterium tuberculosis, and the G58R mutant encoded in W-Beijing strains of M. tuberculosis.

E. Baker, J. Lott, C. Charlier, 2009, Biochemistry.

Structure of a Eukaryotic Nonribosomal Peptide Synthetase Adenylation Domain That Activates a Large Hydroxamate Amino Acid in Siderophore Biosynthesis*

V. Arcus, J. Lott, A. Koulman, 2009, The Journal of Biological Chemistry.

Identification of extracellular siderophores and a related peptide from the endophytic fungus Epichloë festucae in culture and endophyte-infected Lolium perenne

V. Arcus, K. Fraser, S. Rasmussen, 2012, Phytochemistry.

Synthesis and evaluation of M. tuberculosis salicylate synthase (MbtI) inhibitors designed to probe plasticity in the active site.

E. Baker, E. M. Bulloch, R. Payne, 2012, Organic & biomolecular chemistry.

High throughput crystallography of TB drug targets.

D. Eisenberg, J. Berger, M. James, 2007, Infectious disorders drug targets.

Membrane trafficking pathways regulating the epithelial sodium channel, ENaC.

J. Lott, F. McDonald, A. Ware, 2019, American journal of physiology. Renal physiology.

Making the most of two crystals: structural analysis of a conserved hypothetical protein using native gel screening and SAD phasing.

E. Baker, J. Lott, M. Banfield, 2003, Acta crystallographica. Section D, Biological crystallography.

Interaction of Serum- and Glucocorticoid Regulated Kinase 1 (SGK1) with the WW-Domains of Nedd4-2 Is Required for Epithelial Sodium Channel Regulation

P. Teesdale-Spittle, J. Lott, P. Snyder, 2010, PloS one.

Purification, crystallization and preliminary X-ray studies of MbtN (Rv1346) from Mycobacterium tuberculosis.

E. Baker, J. Johnston, E. M. Bulloch, 2013, Acta crystallographica. Section F, Structural biology and crystallization communications.

Synthesis of DOHNAA, a Mycobacterium tuberculosis Cholesterol CD Ring Catabolite and FadD3 Substrate

J. Lott, M. Brimble, S. Dawes, 2015 .

Mechanism of Fluorinated Anthranilate-Induced Growth Inhibition in Mycobacterium tuberculosis.

J. Lott, Santosh Kumar, D. Crick, 2019, ACS infectious diseases.

Expression and purification of high sulfur and high glycine-tyrosine keratin-associated proteins (KAPs) for biochemical and biophysical characterization.

J. Lott, J. Plowman, D. Harland, 2018, Protein expression and purification.

The TB structural genomics consortium: a resource for Mycobacterium tuberculosis biology.

A W Munro, M Wilmanns, E N Baker, 2003, Tuberculosis.

Transport in Mycobacterium smegmatis Transcriptional Regulator of Phosphate Crystal Structure of PhnF, a GntR-Family

J. Lott, G. Fritz, G. Cook, 2014 .

Structure and dynamics of human Nedd4-1 WW3 in complex with the αENaC PY motif.

J. Lott, M. Brimble, F. McDonald, 2013, Biochimica et biophysica acta.

RNase HI Depletion Strongly Potentiates Cell Killing by Rifampicin in Mycobacteria

V. Mizrahi, J. Lott, G. Cook, 2021, bioRxiv.

Structural analysis of Chi1 Chitinase from Yen-Tc: the multisubunit insecticidal ABC toxin complex of Yersinia entomophaga.

J. Lott, B. Hankamer, R. Simpson, 2012, Journal of molecular biology.

3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity

Rosalba Rothnagel, Ben Hankamer, Michael J Landsberg, 2011, Proceedings of the National Academy of Sciences.

Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation.

G. Sprenger, H. Baker, E. Baker, 2000, Journal of molecular biology.

Cryo-EM structures of the pore-forming A subunit from the Yersinia entomophaga ABC toxin

L. Hartley-Tassell, H. Stahlberg, J. Lott, 2019, Nature Communications.

The tryptophan biosynthetic pathway is essential for Mycobacterium tuberculosis to cause disease

J. Lott, 2020, Biochemical Society transactions.

The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device

J. Lott, S. Panjikar, M. Hurst, 2013, Nature.

A single WW domain is the predominant mediator of the interaction between the human ubiquitin-protein ligase Nedd4 and the human epithelial sodium channel.

J. Lott, S. J. Coddington-Lawson, F. McDonald, 2002, The Biochemical journal.

The ordered visual transduction complex of the squid photoreceptor membrane

J. Lott, J. Findlay, J. Wilde, 1999, Molecular Neurobiology.

The γ‐subunit of the principal G‐protein from squid (Loligo forbesi) photoreceptors contains a novel N‐terminal sequence

N. Ryba, J. Lott, J. Findlay, 1992, FEBS letters.

A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis, reveals an unusual acyl-binding pocket.

E. Baker, J. Johnston, E. M. Bulloch, 2015, Acta crystallographica. Section D, Biological crystallography.

The Structure of MbtI from Mycobacterium tuberculosis, the First Enzyme in the Biosynthesis of the Siderophore Mycobactin, Reveals It To Be a Salicylate Synthase

E. Baker, J. Lott, Minmin Yu, 2006, Journal of bacteriology.

Mycobacterial MenJ: An Oxidoreductase Involved in Menaquinone Biosynthesis.

J. Lott, A. Upadhyay, Santosh Kumar, 2018, ACS chemical biology.

Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation

E. Baker, C. Day, J. Lott, 2014, Molecular microbiology.

Crystal Structure of PhnF, a GntR-Family Transcriptional Regulator of Phosphate Transport in Mycobacterium smegmatis

E. Baker, J. Lott, G. Fritz, 2014, Journal of bacteriology.

The structure of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Mycobacterium tuberculosis reveals a common catalytic scaffold and ancestry for type I and type II enzymes.

H. Baker, E. Baker, E. Parker, 2005, Journal of molecular biology.

Crystallization and preliminary X-ray crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Mycobacterium tuberculosis.

Edward N Baker, Emily J Parker, H. Baker, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Structural insights into the architecture and membrane interactions of the conserved COMMD proteins

Michael D Healy, J. Lott, P. Cullen, 2018, eLife.

The Structure of the Transcriptional Repressor KstR in Complex with CoA Thioester Cholesterol Metabolites Sheds Light on the Regulation of Cholesterol Catabolism in Mycobacterium tuberculosis*

E. Baker, J. Lott, Chen Gao, 2016, The Journal of Biological Chemistry.

The Structure of an Ancient Conserved Domain Establishes a Structural Basis for Stable Histidine Phosphorylation and Identifies a New Family of Adenosine-specific Kinases*

L. Delbaere, E. Baker, J. Johnston, 2006, Journal of Biological Chemistry.

The TB structural genomics consortium: providing a structural foundation for drug discovery.

Shekhar C Mande, Tom Alber, David Eisenberg, 2002, Current drug targets. Infectious disorders.

The potential impact of structural genomics on tuberculosis drug discovery.

Edward N Baker, Vickery L Arcus, V. Arcus, 2006, Drug discovery today.

Implications of binding mode and active site flexibility for inhibitor potency against the salicylate synthase from Mycobacterium tuberculosis.

E. Baker, J. Johnston, E. M. Bulloch, 2012, Biochemistry.

Inhibition Studies of Mycobacterium tuberculosis Salicylate Synthase (MbtI)

E. Baker, E. M. Bulloch, R. Payne, 2010, ChemMedChem.

Collaborative networks enable the rapid establishment of serological assays for SARS-CoV-2 during nationwide lockdown in New Zealand

M. Baker, C. Day, J. Lott, 2020, PeerJ.

Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin.

Edward N Baker, Brent W Segelke, Li-Wei Hung, 2005, Journal of molecular biology.

A functional role of Rv1738 in Mycobacterium tuberculosis persistence suggested by racemic protein crystallography

E. Baker, J. Lott, S. Kent, 2015, Proceedings of the National Academy of Sciences.

A flexible and economical medium-throughput strategy for protein production and crystallization.

V. Arcus, H. Baker, E. Baker, 2005, Acta crystallographica. Section D, Biological crystallography.

Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex.

E. Baker, J. Johnston, E. M. Bulloch, 2015, Acta crystallographica. Section D, Biological crystallography.

The substrate capture mechanism of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase provides a mode for inhibition.

E. Baker, E. Parker, E. M. Bulloch, 2013, Biochemistry.

Structural characterization of human peptidyl-arginine deiminase type III by X-ray crystallography.

J. Lott, T. V. Lee, O. Rechiche, 2021, Acta crystallographica. Section F, Structural biology communications.

Protein structure prediction and analysis as a tool for functional genomics.

Edward N Baker, Vickery L Arcus, V. Arcus, 2003, Applied bioinformatics.

Expression and purification of an adenylation domain from a eukaryotic nonribosomal peptide synthetase: using structural genomics tools for a challenging target.

V. Arcus, J. Lott, Richard D. Johnson, 2010, Protein expression and purification.

Crystallization of a protein using dehydration without a precipitant.

E. Baker, J. Lott, M. Sharpe, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Crystallization and preliminary X-ray crystallographic analysis of MbtI, a protein essential for siderophore biosynthesis in Mycobacterium tuberculosis.

E. Baker, J. Lott, R. J. Ramsay, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Structures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site.

E. Baker, E. Parker, J. Lott, 2015, Biochemistry.

Alternative substrates reveal catalytic cycle and key binding events in the reaction catalysed by anthranilate phosphoribosyltransferase from Mycobacterium tuberculosis.

E. Baker, E. Parker, E. M. Bulloch, 2014, The Biochemical journal.

Datasets, processing and refinement details for Mtb-AnPRT: inhibitor structures with various space groups

E. Baker, E. Parker, J. Lott, 2017, Data in brief.

Implications of binding mode and active site flexibility for inhibitor potency against the salicylate synthase from Mycobacterium tuberculosis.

J. Johnston, E. M. Bulloch, Alexandra Manos-Turvey, 2012, Biochemistry.

The substrate capture mechanism of Mycobacterium tuberculosis anthranilate phosphoribosyltransferase provides a mode for inhibition.

E. M. Bulloch, J. Lott, G. Evans, 2013, Biochemistry.

Structures of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Variants Reveal the Conformational Changes That Facilitate Delivery of the Substrate to the Active Site.

E. Baker, E. Parker, J. Lott, 2015, Biochemistry.

Structure of the bacterial type II NADH dehydrogenase: a monotopic membrane protein with an essential role in energy generation

E. Baker, C. Day, J. Lott, 2014, Molecular microbiology.

Revealing the Inter-Module Interactions of Multi-Modular Nonribosomal Peptide Synthetases.

J. Lott, J Shaun Lott, T Verne Lee, 2017, Structure.