P. Tormay

发表

Effect of Mycobacterium tuberculosis chaperonins on bronchial eosinophilia and hyper‐responsiveness in a murine model of allergic inflammation

B. Henderson, C. Page, D. Spina, 2004, Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology.

A Mycobacterium tuberculosis Mutant Lacking the groEL Homologue cpn60.1 Is Viable but Fails To Induce an Inflammatory Response in Animal Models of Infection

G. Besra, P. Lund, B. Henderson, 2008, Infection and Immunity.

Comparative cell signalling activity of ultrapure recombinant chaperonin 60 proteins from prokaryotes and eukaryotes

B. Henderson, P. Tormay, S. Poole, 2005, Immunology.

The two homologous chaperonin 60 proteins of Mycobacterium tuberculosis have distinct effects on monocyte differentiation into osteoclasts

B. Henderson, C. Morris, P. Tormay, 2008, Cellular microbiology.

Molecular Chaperones and Cell Signalling: Cell-Cell Signalling Properties of Chaperonins

P. Tormay, A. Coates, 2005 .

Rhizobium leguminosarum chaperonin 60.3, but not chaperonin 60.1, induces cytokine production by human monocytes: activity is dependent on interaction with cell surface CD14

R. George, P. Lund, B. Henderson, 2002, Cell stress & chaperones.

Barriers to heterologous expression of a selenoprotein gene in bacteria

A. Böck, P. Tormay, 1997, Journal of bacteriology.

Selenoprotein synthesis in E. coli. Purification and characterisation of the enzyme catalysing selenium activation.

A. Böck, K. Forchhammer, A. Ehrenreich, 1992, European journal of biochemistry.

Comparison of the Moonlighting Actions of the Two Highly Homologous Chaperonin 60 Proteins of Mycobacterium tuberculosis

B. Henderson, C. Botanch, Y. Riffo-Vasquez, 2010, Infection and Immunity.

Mycobacterium tuberculosisChaperonin 60.1 Is a More Potent Cytokine Stimulator than Chaperonin 60.2 (Hsp 65) and Contains a CD14-Binding Domain

J. Lewthwaite, Mahavir Singh, P. Tormay, 2001, Infection and Immunity.

Role of stoichiometry between mRNA, translation factor SeIB and selenocysteyl‐tRNA in selenoprotein synthesis

A. Böck, P. Tormay, A. Sawers, 1996, Molecular microbiology.

The Intercellular Signaling Activity of the Mycobacterium tuberculosis Chaperonin 60.1 Protein Resides in the Equatorial Domain*

B. Henderson, P. Tormay, A. Coates, 2005, Journal of Biological Chemistry.

Big Data in Pharmaceutical R&D: Creating a Sustainable R&D Engine

P. Tormay, 2015, Pharmaceutical Medicine.

Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infection

Gerhard Walzl, Graham R. Stewart, Joanna Betts, 2001, Nature Medicine.

Genes coding for the selenocysteine-inserting tRNA species from Desulfomicrobium baculatum and Clostridium thermoaceticum: structural and evolutionary implications

A. Böck, J. Heider, R. Wilting, 1994, Journal of bacteriology.

Identification of the formate dehydrogenases and genetic determinants of formate-dependent nitrite reduction by Escherichia coli K12.

L. Griffiths, J. Cole, P. Tormay, 1993, Journal of general microbiology.

Bacterial selenocysteine synthase--structural and functional properties.

P. Christen, A. Böck, R. Wilting, 1998, European journal of biochemistry.

Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB.

A. Böck, R. Wilting, P. Tormay, 1996, Journal of molecular biology.

The two homologous chaperonin 60 proteins of Mycobacterium tuberculosis have distinct effects on monocyte differentiation into osteoclasts

B. Henderson, C. Morris, P. Tormay, 2008, Cellular microbiology.

A Mycobacterium tuberculosis Mutant Lacking the groEL Homologue cpn60.1 Is Viable but Fails To Induce an Inflammatory Response in Animal Models of Infection

G. Besra, P. Lund, B. Henderson, 2008, Infection and Immunity.

Molecular Chaperones and Cell Signalling: Cell-Cell Signalling Properties of Chaperonins

P. Tormay, A. Coates, 2005 .