Search Results - "TORMAY, Peter"
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Comparison of the Moonlighting Actions of the Two Highly Homologous Chaperonin 60 Proteins of Mycobacterium tuberculosis
Published in Infection and Immunity (01-07-2010)“…Evidence is emerging that the two chaperonin (Cpn) 60 proteins of Mycobacterium tuberculosis, Cpn60.1 and Cpn60.2, have moonlighting actions that may…”
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Mycobacterium tuberculosis Mutant Lacking the groEL Homologue cpn60.1 Is Viable but Fails To Induce an Inflammatory Response in Animal Models of Infection
Published in Infection and Immunity (01-04-2008)“…The causative agent of tuberculosis, Mycobacterium tuberculosis, has two chaperonin (Cpn60) proteins and one cochaperonin (Cpn10) protein. We show here that…”
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Big Data in Pharmaceutical R&D: Creating a Sustainable R&D Engine
Published in Pharmaceutical medicine (2015)“…Over the last 20 years, productivity in the pharmaceutical industry has been diminishing because of constantly increasing costs while output has overall been…”
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The Intercellular Signaling Activity of the Mycobacterium tuberculosis Chaperonin 60.1 Protein Resides in the Equatorial Domain
Published in The Journal of biological chemistry (08-04-2005)“…The major heat shock protein, chaperonin 60, has been established to have intercellular signaling activity in addition to its established protein-folding…”
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Mycobacterium tuberculosisChaperonin 60.1 Is a More Potent Cytokine Stimulator than Chaperonin 60.2 (Hsp 65) and Contains a CD14-Binding Domain
Published in Infection and Immunity (01-12-2001)“…Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit…”
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Bacterial selenocysteine synthase
Published in European journal of biochemistry (15-06-1998)“…Selenocysteine synthase from Escherichia coli is a pyridoxal‐5′‐phosphate‐containing enzyme which catalyses the conversion of seryl‐tRNASec into…”
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Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infection
Published in Nature medicine (01-06-2001)“…Elevated expression of heat-shock proteins (HSPs) can benefit a microbial pathogen struggling to penetrate host defenses during infection, but at the same time…”
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Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain
Published in Infection and immunity (01-12-2001)“…Much attention has focused on the Mycobacterium tuberculosis molecular chaperone chaperonin (Cpn) 60.2 (Hsp 65) in the pathology of tuberculosis because of its…”
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two homologous chaperonin 60 proteins of Mycobacterium tuberculosis have distinct effects on monocyte differentiation into osteoclasts
Published in Cellular microbiology (01-10-2008)“…Mycobacterium tuberculosis produces two homologous chaperonin (Cpn)60 proteins, Cpn60.1 and Cpn60.2 (Hsp65). Both proteins stimulate human and murine monocyte…”
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Selenoprotein synthesis in E. coli
Published in European journal of biochemistry (01-06-1992)“…The product of the selD gene from Escherichia coli catalyses the formation of an activated selenium compound which is required for the synthesis of Sec‐tRNA…”
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Comparative cell signalling activity of ultrapure recombinant chaperonin 60 proteins from prokaryotes and eukaryotes
Published in Immunology (01-06-2005)“…Summary Heat‐shock protein (hsp)60/chaperonin 60 is a potent immunogen which has recently been claimed to have cell‐signalling actions upon myeloid and…”
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Barriers to heterologous expression of a selenoprotein gene in bacteria
Published in Journal of Bacteriology (01-02-1997)“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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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
Published in Cell stress & chaperones (01-04-2002)“…As part of a program of work to understand the interaction of bacterial chaperonins with human leukocytes, we have examined 2 of the 3 chaperonin 60 (Cpn 60)…”
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Bacterial selenocysteine synthase--structural and functional properties
Published in European journal of biochemistry (15-06-1998)“…Selenocysteine synthase from Escherichia coli is a pyridoxal-5'-phosphate-containing enzyme which catalyses the conversion of seryl-tRNA(Sec) into…”
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Selenoprotein synthesis in E. coli. Purification and characterisation of the enzyme catalysing selenium activation
Published in European journal of biochemistry (15-06-1992)“…The product of the selD gene from Escherichia coli catalyses the formation of an activated selenium compound which is required for the synthesis of Sec-tRNA…”
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Domain structure of the selenocysteine-specific translation factor SelB in prokaryotes
Published in Biomedical and environmental sciences (01-09-1997)“…Translation factor SelB is the key component for the specific decoding of UGA codons with selenocysteine at the ribosome. SelB binds selenocysteyl-tRNA(Sec),…”
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