Results 201 to 210 of about 157,972 (251)
Continuous‐Flow Microfluidic Synthesis Enhances C2+ Selectivity for Cu2O Catalysts
Microfluidic devices are used to prepare Cu2O nanoparticles under laminar flow conditions, which exhibit enhanced selectivity in the CO2‐to‐C2+ reaction due to their nanoporosity and high defect concentration. Cu2O prepared using standard solution methods displays decreased CO2‐to‐C2+ selectivity due to the absence of similar properties. Altogether, we
Carlota Casas +16 more
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Schematic diagram showing compressive stress triggers glycolytic reprogramming and lactate accumulation in macrophages. Lactate mediates TRAF6 lactylation at K171/K180 dual sites, which enhances its K63‐linked ubiquitination to activate the NF‑κB pathway and promote M1 polarization. This cascade drives orthodontic tooth movement (OTM) and alveolar bone
Xinyi He +9 more
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To accelerate the inverse design of heterostructured metal matrix composites, a closed‐loop scientific machine learning framework integrates continual learning prediction with NSGA‐II‐PMCP optimization. The framework maps microstructural descriptors to strength, toughness, and modulus, expands high‐quality Pareto solutions, and guides experimentally ...
Zhiyan Zhong +11 more
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C2 Domains and Membrane Fusion
2011Publisher Summary This chapter describes C2 domains and membrane fusion. Membrane fusion or the controlled merger of two initially separated membranes is of fundamental importance in biology. This is particularly true for eukaryotic cells that contain a plethora of membrane-bound compartments.
Martens, Sascha, McMahon, Harvey T
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The C2 domains of synaptotagmin – partners in exocytosis
Trends in Biochemical Sciences, 2004Rapid signaling between neurons relies on the Ca(2+)-triggered exocytosis of neurotransmitters. Release is mediated by 'kiss-and-run' or complete fusion of secretory organelles with the plasma membrane. Current models indicate that exocytosis is regulated by synaptotagmin I (syt) and mediated by SNARE (soluble NSF-attachment protein receptor) proteins.
Jihong, Bai, Edwin R, Chapman
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Membrane binding and subcellular targeting of C2 domains
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2006C2 domains are a ubiquitous structural module and many of them function in Ca2+ -dependent membrane binding and thereby serve as Ca2+ effectors for divergent Ca2+ -mediated cellular processes. Extensive structural, biochemical, biophysical, and cellular studies of C2 domains and host proteins in the past decade have shown that due to their structural ...
Wonhwa, Cho, Robert V, Stahelin
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Science Signaling, 2001
The originally described C2 domains function as calcium-regulated phospholipid-binding domains. Several examples of proteins that have C2 domains (as identified by sequence similarity) have been found, yet these C2 domains have mutations in key residues that are required for calcium binding.
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The originally described C2 domains function as calcium-regulated phospholipid-binding domains. Several examples of proteins that have C2 domains (as identified by sequence similarity) have been found, yet these C2 domains have mutations in key residues that are required for calcium binding.
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Functional mapping of factor VIII C2 domain
Thrombosis and Haemostasis, 2011SummaryThe factor VIII (FVIII) is a cofactor of the coagulation cascade. The FVIII C2 domain is a critical domain that participates in the interactions with the von Willebrand factor and the phospholipidic surfaces. To assess the importance of each residue of this domain in the maintenance of the structure and the function of FVIII, a number (n=139) of
Pellequer, Jean-Luc +5 more
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Trends in Neurosciences, 2003
Abstract Ca 2+ influx into the presynaptic terminal triggers fusion of synaptic vesicles with the plasma membrane and release of neurotransmitters. A decade of intensive study of the synaptic vesicle protein synaptotagmin I has led to the general belief that this polypeptide functions as a Ca 2+ sensor in this process.
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Abstract Ca 2+ influx into the presynaptic terminal triggers fusion of synaptic vesicles with the plasma membrane and release of neurotransmitters. A decade of intensive study of the synaptic vesicle protein synaptotagmin I has led to the general belief that this polypeptide functions as a Ca 2+ sensor in this process.
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The Role of C2 Domains in PKC Signaling
2012More than two decades ago, the discovery of the first C2 domain in conventional Protein Kinase Cs (cPKCs) and of its role as a calcium-binding motif began to shed light on the activation mechanism of this family of Serine/Threonine kinases which are involved in several critical signal transduction pathways.
Carole A, Farah, Wayne S, Sossin
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