Results 251 to 260 of about 401,752 (293)

Epithelial TRIM27 Inhibits Intestinal Inflammation in Ulcerative Colitis by the USP7/TRIM27‐IKK Double Negative‐Feedback

Advanced Science, EarlyView.
ABSTRACT The E3 ubiquitin ligase tripartite motif 27 (TRIM27) is a negative regulator of NF‐κB activation and the innate immune response, and TRIM27 deficiency significantly impairs dextran sulfate sodium (DSS)‐induced colitis. The function of TRIM27 in intestinal epithelial cells (IECs), the mechanism by which TRIM27 inhibits the NF‐κB pathway and its
Weimin Xu, Zhebin Hua, Zhujiang Dai, Shasha Zhang, Yihan Jiang, Wensong Ge, YingWei Chen, Zhongchuan Wang, Bing Zhang, Chen‐Ying Liu, Peng Du   +10 more
wiley   +1 more source

Penicillin binding proteins of Vibriocholerae

Biochemical and Biophysical Research Communications, 1990
Eleven penicillin binding proteins (PBPs) of Vibrio cholerae have been identified using [125I] labelled p-hydroxybenzyl penicillin (PenX). These proteins are localised in the inner membrane and have molecular weights ranging from 97,000 to 22,000.
T K, Sengupta, A N, Chatterjee, J, Das
openaire   +3 more sources

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Penicillin‐binding proteins in Listeria monocytogenes

Apmis, 1989
The Penicillin‐Binding Proteins (PBP) of Listeria monocytogenes 29‐CCM‐A: 454 (ATCC 15313) are described by the use of 125I‐Penicillin X as radiotracer. The membranes of this tolerant bacilli contained at least five proteins with different affinities for the radiotracer or Dicloxacillin. The molecular weights of these proteins were estimated as 76, 74,
Gabriel Gutkind
exaly   +3 more sources

Resistant penicillin-binding proteins

Cellular and Molecular Life Sciences CMLS, 1998
Low-affinity penicillin-binding proteins (PBPs), which participate in the beta-lactam resistance of several pathogenic bacteria, have different origins. Natural transformation and recombination events with DNA acquired from neighbouring intrinsically resistant organisms are responsible for the appearance of mosaic genes encoding two or three low ...
R, Hakenbeck, J, Coyette
openaire   +2 more sources

Ion binding of penicillins to proteins

Biochimica et Biophysica Acta (BBA) - General Subjects, 1970
Abstract 1. 1. A new method is described, utilising the reactions of hydrated electrons ( e aq − ), to demonstrate that reversible ion binding occurs between a series of penicillins and the proteins, bovine serum albumin and lysozyme. 2. 2.
G O, Phillips, D M, Power, C, Robinson, J V, Davies   +3 more
openaire   +2 more sources

Resistance to β-Lactams in Neisseria ssp Due to Chromosomally Encoded Penicillin-Binding Proteins

Antibiotics, 2016
International audienceNeisseria meningitidis and Neisseria gonorrhoeae are human pathogens that cause a variety of life-threatening systemic and local infections, such as meningitis or gonorrhoea.
André Zapun, Cecile Morlot, Muhamed-Kheir Taha   +2 more
exaly   +2 more sources

Penicillin-Binding Proteins of Bacteria

1977
The penicillin-binding components of bacteria are presumably enzymes of cell wall peptidoglycan synthesis, and one or more of these is a presumed killing site for penicillins. All organisms which have so far been examined contain multiple penicillin-binding components, e.g., there are five in Bacillus subtilis, six in Escherichia coli, and four in ...
J W, Kozarich, C E, Buchanan, S J, Curtis, S, Hammarström, J L, Strominger   +4 more
openaire   +2 more sources

Penicillin-Binding Proteins in Bacteria

Annals of Internal Medicine, 1982
The last 5 to 6 years have witnessed an outburst of renewed interest in the beta-lactam antibiotics. One of the main factors contributing to this was the introduction of the simple and powerful technique of sodium dodecyl sulphate electrophoresis for the identification of bacterial membrane components--penicillin binding proteins--that bind radioactive
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A Method to Assay Penicillin-Binding Proteins

2008
Key enzymes that assemble the bacterial cell wall are also the target of the Beta-lactam class of antibiotics. The covalent binding of labeled penicillin to these proteins has been used in numerous studies in drug discovery, antibiotic mechanisms of action and resistance, and cell wall physiology.
Michael J, Pucci, Thomas J, Dougherty
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Affinity of Carumonam for Penicillin-Binding Proteins

Chemotherapy, 2009
Direct labeling experiments with [14C]-carumonam as well as competition binding assays with [14C]-benzylpenicillin and [14C]-ceftriaxone have demonstrated that penicillin-binding protein (PBP) 3 of Escherichia coli, Enterobacter cloacae and Pseu-domonas aeruginosa has the highest affinity for carumonam (Ro 17–2301, AMA-1080).
R L, Then, I, Kohl
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