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CDK4/6 inhibition promotes CD8+ T cell expansion through tumor‐macrophage crosstalk by activating HIF‐1α and enhancing MIF‐CD44/CD74 signaling. This reprograms TAMs to boost MHC‐I antigen presentation, and CDK4/6 inhibitor‐trained M1 TAM supernatant therapy synergizes with low‐dose PD‐1 blockade to restore antitumor immunity.
Lin He +17 more
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ERK‐Mediated Phosphorylation of YAP Defines a Noncanonical FGF Signaling Mechanism in Stem Cells
With a powerful combination of in vivo, ex vivo, and in vitro models, the authors highlight a novel FGF‐ERK signaling regulation of YAP at the S128 site in neural crest‐derived stem cells. This study opens exciting new directions in stem cell biology and craniofacial biology, paving the way for potential innovations in the treatment of craniofacial ...
Xiaolei Zhao +16 more
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An autologous whole‐tumor‐cell vaccine (rWTC‐MBTA) is evaluated in murine CNS lymphoma. Subcutaneous vaccination activates dendritic cells, broadens T‐cell priming, and drives lymphocyte trafficking to brain tumors, producing durable tumor control. Longitudinal bioluminescence and adoptive‐transfer assays verify CNS engagement. Combination with anti‐PD‐
Yaping Zhang +10 more
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SETDB1 is progressively downregulated in ALD, correlating with disease severity. SETDB1 deficiency impairs LAP by disrupting Rubicon membrane localization, leading to defective lipid droplet clearance. Concurrently, loss of SETDB1 reduces nuclear LC3B, causing R‐loop accumulation and cGAS‐STING‐driven inflammation. Lipidated LC3B mediates LAP‐dependent
Yi Zhang +17 more
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Phospholipid transfer protein(PLTP) plays a critical role in forming a complex with kinase A (AURKA) and P65. This interaction facilitates phosphorylation of P65 at Ser536, leading to the activation of the NF‐κB signaling pathway. Ultimately, this leads to the upregulation of downstream cytokines, including IL‐6, IL‐8, and CSF‐1, which promotes M2 ...
Xinyue Liang +14 more
wiley +1 more source
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Resistant penicillin-binding proteins
Cellular and Molecular Life Sciences CMLS, 1998Low-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, 1990Eleven 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 of Bacteria
1977The 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 +4 more
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Penicillin-Binding Proteins in Bacteria
Annals of Internal Medicine, 1982The 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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