Drug Binding Assays do not Reveal Specific Binding of Lacosamide to Collapsin Response Mediator Protein 2 (CRMP‐2)
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منابع مشابه
Collapsin response mediator protein-2 (Crmp2) regulates trafficking by linking endocytic regulatory proteins to dynein motors.
Endocytosis is a conserved cellular process in which nutrients, lipids, and receptors are internalized and transported to early endosomes, where they are sorted and either channeled to degradative pathways or recycled to the plasma membrane. MICAL-L1 and EHD1 are important regulatory proteins that control key endocytic transport steps. However, the precise mechanisms by which they mediate trans...
متن کاملPhosphorylation of CRMP2 (collapsin response mediator protein 2) is involved in proper dendritic field organization.
Collapsin response mediator proteins (CRMPs) are intracellular proteins that mediate signals for several extracellular molecules, such as Semaphorin3A and neurotrophins. The phosphorylation of CRMP1 and CRMP2 by Cdk5 at Ser522 is involved in axonal guidance and spine development. Here, we found that the Ser522-phosphorylated CRMP1 and/or CRMP2 are enriched in the dendrites of cultured cortical ...
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Yuying Wang, Joel M. Brittain, Brian W. Jarecki, Ki Duk Park, Sarah M. Wilson, Bo Wang, Rachel Hale, Samy O. Meroueh, Theodore R. Cummins, and Rajesh Khanna Running head: CRMP-2 modifies LCM’s actions on Na channels From the Departments of Pharmacology and Toxicology, Chemistry, Biochemistry and Molecular Biology and Center for Computational Biology, and Bioinformatics, and Program in Medical N...
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Aberrant ion channel function has been heralded as a main underlying mechanism driving epilepsy and its symptoms. However, it has become increasingly clear that treatment strategies targeting voltage-gated sodium or calcium channels merely mask the symptoms of epilepsy without providing disease-modifying benefits. Ion channel function is likely only one important cog in a highly complex machine...
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Isotherms of the binding of the anthracycIine antibiotic, adriamycin (adriblastin), to DNA histone complexes was studied by means of spectroscopic analysis. The results indicated that: (a) binding of adriamycin to histones reduced the interaction of histones with DNA, (b) binding of the drug to DNA did not change the binding affinity of histone to DNA and, (c) in the explored binding range...
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ژورنال
عنوان ژورنال: CNS Neuroscience & Therapeutics
سال: 2012
ISSN: 1755-5930,1755-5949
DOI: 10.1111/j.1755-5949.2012.00313.x