Results 191 to 200 of about 20,967 (222)

Clinical emergence of a novel sequence type (ST3672) NDM-1-producing <i>Vibrio parahaemolyticus</i> in foodborne disease. [PDF]

Front Microbiol
Ni C, Wang J, Yang C, Gao S, Xu Z, Wang Y, Peng H, Cao W, Han Y.   +8 more
europepmc   +1 more source

<i>Aquilaria sinensis</i> essential oil inhibits biofilm formation and virulence of <i>Staphylococcus aureus</i>. [PDF]

Front Microbiol
Wang F, Ding ZW, Wang YJ, Xu KZ, Dar OI, Wang M, Sethupathy S, Liu YY, Tang S.   +8 more
europepmc   +1 more source

Histidinol dehydrogenase (HisD): a critical regulator of <i>Staphylococcus aureus</i> virulence and a promising target for antivirulence therapy. [PDF]

Microbiol Spectr
Jiang W, Chen H, Liu Z, Dang Y, Da Y, Liu Z, Zhu Y, Gao L, Yan W, Han J, You C.   +10 more
europepmc   +1 more source

Expanding the amyloid landscape: structural plasticity of antimicrobial peptides

Landau M, Ragonis-Bachar P, Strati F, Gustavsson E, Khokhlov A, Barnea E, Rayan B, Upcher A.   +7 more
europepmc   +1 more source

Functions of a hemolysin-like protein in the cyanobacterium Synechocystis sp. PCC 6803

Functions of a hemolysin-like protein in the cyanobacterium Synechocystis sp. PCC 6803
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Pore-Forming Bacterial Protein Hemolysins (Cytolysins)

Critical Reviews in Microbiology, 1991
Protein toxins forming pores in biological membranes occur frequently in Gram-positive and Gram-negative bacteria. They kill either bacteria or eukaryotic cells (at most, a few seem to act on both groups of organisms). Most of the toxins affecting eukaryotes have clearly been shown to be related to the pathogenicity of the producing organisms.
V, Braun, T, Focareta
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The Biochemistry of Hemolysin Toxin Activation:  Characterization of HlyC, an Internal Protein Acyltransferase

Biochemistry, 1998
Hemolysin toxin produced and secreted by pathogenic Escherichia coli is one of a family of cytolytic, structurally homologous protein toxins known as RTX (repeats in toxin) toxins. RTX toxins are products of a gene cluster, CABD. The A gene product, nontoxic hemolysin (proHlyA), is made toxic by posttranslational fatty acylation of two internal lysine ...
Trent, M. Stephen, Worsham, Lesa M.S., Ernst-Fonberg, M. Lou   +2 more
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Unfolding and Translocation of Proteins Through an Alpha-Hemolysin Nanopore by ClpXP

2020
Proteins present a significant challenge for nanopore-based sequence analysis. This is partly due to their stable tertiary structures that must be unfolded for linear translocation, and the absence of regular charge density. To address these challenges, here we describe how ClpXP, an ATP-dependent protein unfoldase, can be harnessed to unfold and ...
Jeff, Nivala, Logan, Mulroney, Qing, Luan, Robin, Abu-Shumays, Mark, Akeson   +4 more
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Identification of Lawsonia intracellularis putative hemolysin protein A and characterization of its immunoreactivity

Veterinary Microbiology, 2017
Despite the recent global increase in fatal endemic outbreaks of proliferative enteropathy (PE) caused by the obligate intracellular bacterium Lawsonia intracelluralis (LI) in the swine industry, development of effective prevention strategies or immunodiagnostic tests has been delayed due to the difficulty of cultivating this pathogen in vitro ...
Jehyung, Kim, Gayeon, Won, Suyeon, Park, John Hwa, Lee   +3 more
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Hemolysins: Pore-forming proteins in invertebrates

Experientia, 1990
Invertebrates possess lytic molecules which lyse vertebrate erythrocytes. In all the species studied so far, hemolytic activity depends on proteins which possess a wide range of reactivity. It is generally calcium-dependent and heat-labile, although calcium-independent and heat-stable hemolysins have also been detected.
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