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GSH‐Responsive Nanoparticles Enhance Hepatocellular Carcinoma Immunotherapy Through Synergistic Effects of Cuproptosis and PI3K Inhibitor Combination

Advanced Science, EarlyView.
ABSTRACT Cuproptosis, an emerging form of programmed cell death, is capable of inducing mitochondrial dysfunction. Moreover, the PI3K‐AKT‐mTOR signaling pathway contributes to tumor cell progression by reprogramming mitochondrial morphology and function.
Lei Wu, Jintong Na, Xiyu Liu, Dongsheng Tang, Zhungang Yang, Zheng Cao, Xinyue He, Haihua Xiao, Liping Zhong, Yuan Liao, Yongxiang Zhao   +10 more
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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
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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
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Penicillin-Binding Proteins inFusobacteriumSpecies

Anaerobe, 1996
Abstract PBPs were identified in four species ofFusobacterium. Each species had a distinctive PBP pattern, although some intra-species variation was noted. Most species had five or six PBPs, ranging in molecular weight from ∼100 kDa to ∼40 kDa. The two strains ofF. nucleatumtested had characteristic “wavy” PBP patterns.F. mortiferumwas distinctive in
K. Tunér, H.M. Wexler, D. Reeves, S.M. Finegold   +3 more
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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
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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
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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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Penicillin-binding proteins: evergreen drug targets

Current Opinion in Pharmacology, 2014
The penicillin-binding proteins (PBPs) are well known targets for the β-lactam antibiotics. They continue to be a focus of interest for pharmaceutical design, as exemplified by the number of new agents under clinical investigation as well as novel experimental molecules.
Frère, Jean-Marie, Page, Malcolm G. P.
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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,
G O, Gutkind, M E, Mollerach, R A, De Torres   +2 more
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Variability of Penicillin-Binding Proteins from Penicillin-Sensitive Streptococcus pneumoniae

Journal of Infectious Diseases, 1991
Penicillin-binding proteins (PBPs) from penicillin-susceptible strains of Streptococcus pneumoniae are believed to be fairly similar in contrast to PBPs occurring in resistant isolates. The antigenic variation of PBPs 1a and 2b in 65 penicillin-susceptible strains from different geographic areas and a wide variety of isolation sites was analyzed using ...
Hakenbeck R, Briese T, Chalkley L, Ellerbrok H, Kalliokoski R, Latorre C, Leinonen M, Martin C   +7 more
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