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Martin J. Blaser

Researcher at Center for Advanced Biotechnology and Medicine

Publications -  841
Citations -  114575

Martin J. Blaser is an academic researcher from Center for Advanced Biotechnology and Medicine. The author has contributed to research in topics: Helicobacter pylori & CagA. The author has an hindex of 147, co-authored 820 publications receiving 104104 citations. Previous affiliations of Martin J. Blaser include Nagoya University & University of Maryland, Baltimore.

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Molecular mechanisms of Campylobacter fetus surface layer protein expression.

TL;DR: Recent studies indicate that C. fetus reassorts a single promoter, controlling SLP expression, and one, or more, complete open reading frame strictly by DNA inversion, and that rearrangement is independent of the distance between sites of inversion.
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Analysis of Malassezia microbiota in healthy superficial human skin and in psoriatic lesions by multiplex real-time PCR.

TL;DR: In this article, the authors compared the Malassezia microbiota from six healthy body locations and two psoriatic lesions, and evaluated its stability over time using multiplex real-time PCR.
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Quantitation and Composition of Cutaneous Microbiota in Diabetic and Nondiabetic Men

TL;DR: The feet of diabetic men had decreased populations of Staphylococcus species, increased populations of S. aureus, and increased bacterial diversity, compared with the feet of controls, and these ecologic changes may affect the risk for wound infections.
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Isolation and characterization of two Campylobacter glycine-extracted proteins that bind to HeLa cell membranes.

TL;DR: It is concluded that CBF1 (PEB1) is surface exposed and may be the key protein for C. jejuniAdherent and nonadherent strains contain different isotypes of these two proteins which could be useful markers of C.Jejuni adhesion.
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Purification and characterization of a family of high molecular weight surface-array proteins from Campylobacter fetus.

TL;DR: There is a family of surface-array proteins of C. fetus with common structural and antigenic characteristics; it is concluded that these molecules have similar biochemical characteristics to surface- array proteins described for other bacteria; but however, by amino-terminal sequence analysis these are unique.