Results 211 to 220 of about 400,542 (252)

Optimization of B Cell Responses in Human Immune System Mice Through Organoid Based Screening

Advanced Science, EarlyView.
Human immune system (HIS) mice show limited B cell responses to immunization. Using HIS mouse spleen organoids, this study identifies cytokine combinations and innate immune signals that drive human B cell expansion, differentiation, and class‐switch. Applying these signals in vivo through temporal separation enables antigen‐specific IgG responses and ...
Haiqiao Sun, He Li, Xu Zhu, Zijian Zhang, Deshan Ren, Shuai Ding, Yan Li   +6 more
wiley   +1 more source

Multimodal Imaging Reveals Rapid Catecholamine Uptake and Release by Neutrophils

Advanced Science, EarlyView.
We show that immune cells (neutrophils) synthesize, uptake, and store catecholamine neurotransmitters such as dopamine or adrenaline. They also release them in response to specific stimuli (serotonin), which we directly visualize using fluorescent nanosensors. We further demonstrate that catecholamines affect neutrophil functions (NETosis) and platelet
Jennifer Mohr, Anne Schmitz, Meshkat Dinarvand, Franziska Wulfert, Sangeetha Shankar, Bjoern F. Hill, Michael Wojak, Juliana Gretz, Marie Britz, Elsa Neubert, Magdalena Shumanska, Sofia Kaushik, Linda Kartaschew, Ivan Bogeski, James Daniel, Sebastian Jung, Johannes Eble, Guido Wabnitz, Luise Erpenbeck, Sebastian Kruss   +19 more
wiley   +1 more source

WT1‐Targeted Oral Bifidobacterium longum Vaccine Enhances Checkpoint Blockade Efficacy in Pancreatic Cancer

Advanced Science, EarlyView.
Oral WT1‐targeted Bifidobacterium longum vaccine promotes WT1‐associated cellular immunity and enhances anti‐PD‐1/anti‐CTLA‐4 efficacy in pancreatic cancer. ABSTRACT Pancreatic ductal adenocarcinoma (PDAC) remains largely unresponsive to immune checkpoint inhibitors (ICI) due to its profoundly immunosuppressive tumor microenvironment.
Taiki Yamazaki, Aori Minami, Misako Hirota, Mirei Hirano, Ryota Sato, Atsuki Honma, Hideto Ueki, Toshiro Shirakawa   +7 more
wiley   +1 more source

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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

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   +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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources