A. Basak

发表

Clostridium perfringens ε-toxin shows structural similarity to the pore-forming toxin aerolysin

D. Moss, R. Titball, A. Cole, 2004, Nature Structural &Molecular Biology.

Molecular basis of toxicity of Clostridium perfringens epsilon toxin

R. Titball, C. Naylor, A. Basak, 2011, The FEBS journal.

NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes.

M. Cosgrove, C. Naylor, A. Basak, 2001, Acta crystallographica. Section D, Biological crystallography.

Structure of the food-poisoning Clostridium perfringens enterotoxin reveals similarity to the aerolysin-like pore-forming toxins.

D. Moss, J. G. Smedley, B. McClane, 2011, Journal of molecular biology.

Comparison of a nontoxic variant of Clostridium perfringens α-toxin with the toxic wild-type strain.

N. Justin, M. Flores-Díaz, A. Alape-Girón, 2010, Acta crystallographica. Section D, Biological crystallography.

Clostridium perfringens epsilon toxin mutant Y30A-Y196A as a recombinant vaccine candidate against enterotoxemia

D. Moss, R. Titball, C. Naylor, 2014, Vaccine.

Clostridium perfringensα-toxin interaction with red cells and model membranes.

C. P. Winlove, C. Winlove, R. Titball, 2015, Soft matter.

The Rational Design of Bacterial Toxin Inhibitors

R. Titball, A. Basak, G. Clark, 2007 .

The first strain of Clostridium perfringens isolated from an avian source has an alpha-toxin with divergent structural and kinetic properties.

D. Moss, N. Justin, R. Titball, 2002, Biochemistry.

Identification of residues in the carboxy-terminal domain of Clostridium perfringens alpha-toxin (phospholipase C) which are required for its biological activities.

D. Moss, M. Flores-Díaz, A. Alape-Girón, 2000, Archives of biochemistry and biophysics.

Purification, crystallization and preliminary X-ray diffraction studies of alpha-toxin of Clostridium perfringens.

D. Stuart, R. Titball, A. Basak, 1994, Journal of molecular biology.

The Clostridium perfringensα-toxin

R. Titball, C. Naylor, A. Basak, 1999 .

CHAPTER 35 – Clostridium perfringens ɛ-toxin

R. Titball, A. Cole, M. Popoff, 2006 .

Protection against avian necrotic enteritis after immunisation with NetB genetic or formaldehyde toxoids☆

R. Titball, F. Van Immerseel, A. Basak, 2013, Vaccine.

Molecular Architecture and Functional Analysis of NetB, a Pore-forming Toxin from Clostridium perfringens*

D. Moss, R. Titball, C. Naylor, 2012, The Journal of Biological Chemistry.

Opening of the active site of Clostridium perfringens alpha-toxin may be triggered by membrane binding.

D. Moss, R. Titball, C. Naylor, 2000, International journal of medical microbiology : IJMM.

Clostridium perfringens from Analysis of NetB , a Pore-forming Toxin Molecular Architecture and Functional Protein Structure and Folding :

D. Moss, A. Cole, A. Basak, 2013 .

Structure of the key toxin in gas gangrene

D. Moss, N. Justin, J. Eaton, 1998, Nature Structural &Molecular Biology.

Clostridium absonum alpha-toxin: new insights into clostridial phospholipase C substrate binding and specificity.

Shinichi Nakamura, David S Moss, D. Moss, 2003, Journal of molecular biology.

Crystal structure of the C. perfringens alpha-toxin with the active site closed by a flexible loop region.

David S Moss, D. Moss, J. Eaton, 2002, Journal of molecular biology.

Circular permutation of βB2‐crystallin changes the hierarchy of domain assembly

A. Basak, C. Slingsby, E. Mayr, 1998, Protein science : a publication of the Protein Society.

Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin.

D. Moss, R. Titball, A. Cole, 2004, Nature structural & molecular biology.

Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein

T. G. Martin, R. Titball, C. Naylor, 2016, Nature Communications.

Structural Insights into Clostridium perfringens Delta Toxin Pore Formation

C. Naylor, M. Gibert, M. Popoff, 2013, PloS one.

Clostridium perfringens epsilon toxin H149A mutant as a platform for receptor binding studies

D. Moss, R. Titball, C. Naylor, 2013, Protein science : a publication of the Protein Society.

CHAPTER 27 – Membrane-damaging and cytotoxic phospholipases

R. Titball, A. Basak, 2006 .

Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin.

R. Titball, C. Naylor, A. Basak, 1999, Journal of molecular biology.

Structural relationships between small β-pore-forming toxins from Clostridium perfringens

R. Titball, C. Naylor, M. Popoff, 2015 .

The pore structure of Clostridium perfringens epsilon toxin

Alice R. Clark, A. R. Clark, D. Moss, 2019, Nature Communications.

Gamma-D crystallin gene (CRYGD) mutation causes autosomal dominant congenital cerulean cataracts

O. Gribouval, A. Basak, M. Abitbol, 2003, Journal of medical genetics.

Glucose 6-phosphate dehydrogenase mutations causing enzyme deficiency in a model of the tertiary structure of the human enzyme.

T. Vulliamy, L. Luzzatto, P. Rowland, 1996, Blood.

The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 A resolution.

P. Rowland, A. Basak, S. Gover, 1994, Structure.

The crystal structure of bluetongue virus VP7

Jonathan Grimes, D. Stuart, J. Grimes, 1995, Nature.

The Bacterial Zinc‐Metallophospholipases C

R. Titball, A. Basak, 2005 .

An atomic model of the outer layer of the bluetongue virus core derived from X-ray crystallography and electron cryomicroscopy.

W Chiu, J Jakana, D I Stuart, 1997, Structure.

Crystal structure of the top domain of African horse sickness virus VP7: comparisons with bluetongue virus VP7.

D. Stuart, J. Grimes, P. Roy, 1996, Journal of virology.

Structures of orbivirus VP7: implications for the role of this protein in the viral life cycle.

D. Stuart, J. Grimes, P. Roy, 1997, Structure.

Crystal structure of the top domain of African horse sickness virus VP7: comparisons with bluetongue virus VP7

P. Roy, P. Gouet, A. Basak, 1996 .

Identification of residues critical for toxicity in Clostridium perfringens phospholipase C, the key toxin in gas gangrene.

J. M. Gutierrez, S. Cole, B. Lomonte, 2000, European journal of biochemistry.

Site‐directed mutagenesis to facilitate X‐ray structural studies of leuconostoc mesenteroides glucose 6‐phosphate dehydrogenase

P. Rowland, A. Basak, S. Gover, 1993, Protein science : a publication of the Protein Society.

Preliminary crystallographic study of bluetongue virus capsid protein, VP7.

D. Stuart, P. Roy, A. Basak, 1992, Journal of molecular biology.

High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract.

Neer Asherie, Christine Slingsby, G. Benedek, 2003, Journal of molecular biology.

The N-terminal domain of betaB2-crystallin resembles the putative ancestral homodimer.

R. Jaenicke, A. Basak, C. Slingsby, 2000, Journal of molecular biology.

Identification of a Key Residue for Oligomerisation and Pore-Formation of Clostridium perfringens NetB

D. Moss, R. Titball, C. Naylor, 2014, Toxins.

Structure of a C. perfringens enterotoxin mutant in complex with a modified Claudin-2 extracellular loop 2.

D. Moss, B. McClane, I. Blasig, 2014, Journal of molecular biology.

The Clostridium perfringens alpha-toxin.

R. Titball, C. Naylor, A. Basak, 1999, Anaerobe.

Crystallization and preliminary crystallographic analysis of the Clostridium perfringens enterotoxin.

B. McClane, A. Basak, D. C. Briggs, 2010, Acta crystallographica. Section F, Structural biology and crystallization communications.