J. Johnston

发表

The TB Structural Genomics Consortium: a decade of progress.

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

Structure of naphthoate synthase (MenB) from Mycobacterium tuberculosis in both native and product-bound forms.

Edward N Baker, Vickery L Arcus, V. Arcus, 2005, Acta crystallographica. Section D, Biological crystallography.

Structural genomics of Mycobacterium tuberculosis.

J. Johnston, 2004 .

Crystal Structures of E. coli Native MenH and Two Active Site Mutants

Zhihong Guo, E. Baker, J. Johnston, 2013, PloS one.

Structural and functional analysis of Rv0554 from Mycobacterium tuberculosis: testing a putative role in menaquinone biosynthesis.

Zhihong Guo, E. Baker, J. Johnston, 2010, Acta crystallographica. Section D, Biological crystallography.

Crystal Structure of a Putative Methyltransferase from Mycobacterium tuberculosis: Misannotation of a Genome Clarified by Protein Structural Analysis

V. Arcus, E. Baker, M. Parker, 2003, Journal of bacteriology.

Allosteric inhibition of Staphylococcus aureus MenD by 1,4-dihydroxy naphthoic acid: a feedback inhibition mechanism of the menaquinone biosynthesis pathway

W. Jiao, T. Allison, J. Johnston, 2022, bioRxiv.

Allosteric regulation of menaquinone (vitamin K2) biosynthesis in the human pathogen Mycobacterium tuberculosis

E. Baker, J. Johnston, E. M. Bulloch, 2020, The Journal of Biological Chemistry.

Allosteric Regulation of Vitamin K2 Biosynthesis in a Human Pathogen

E. Baker, J. Johnston, E. M. Bulloch, 2019, bioRxiv.

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.

Advances in menaquinone biosynthesis: sublocalisation and allosteric regulation.

J. Johnston, E. M. Bulloch, 2020, Current opinion in structural biology.

Exploiting Structural Modelling Tools to Explore Host-Translocated Effector Proteins

J. Johnston, Claudia-Nicole Meisrimler, Sahel Amoozadeh, 2021, International journal of molecular sciences.

Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein.

Alistair S Brown, E. Baker, J. Johnston, 2014, Journal of structural biology.

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.

Structure of a double CACHE chemoreceptor ligand-binding domain from Pseudomonas syringae provides insights into the basis of proline recognition.

J. Johnston, M. Gerth, Maximilian Ehrhardt, 2021, Biochemical and biophysical research communications.

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.

Structural Views along the Mycobacterium tuberculosis MenDReaction Pathway Illuminate Key Aspects of ThiaminDiphosphate-Dependent EnzymeMechanisms Graphical

E. Baker, J. Johnston, E. M. Bulloch, 2016 .

Mass spectral determination of phosphopantetheinylation specificity for carrier proteins in Mycobacterium tuberculosis

E. Baker, J. Johnston, G. Bashiri, 2016, FEBS open bio.

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.

Structural Views along the Mycobacterium tuberculosis MenD Reaction Pathway Illuminate Key Aspects of Thiamin Diphosphate-Dependent Enzyme Mechanisms.

E. Baker, J. Johnston, E. M. Bulloch, 2016, Structure.

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.

Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein.

Alistair S Brown, E. Baker, J. Johnston, 2014, Journal of structural biology.