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98878 Ensembl ENSG00000103966 ENSMUSG00000027293 UniProt Q9H223 Q9EQP2 RefSeq (mRNA) NM_139265 NM_133838 RefSeq (protein) NP_644670 NP_598599 Location (UCSC) Chr 15: 41.9 – 41.97 Mb Chr 2: 119.92 – 119.99 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse EH-domain containing 4, also known as EHD4, is a human gene belonging to the EHD protein family. References ^ a b c GRCh38 ...
EHD4 is implicated in vesicular transport from early endosome to ERC as well as in the lysosomal degradation pathway. Recent studies have shown that the EHD4 protein may only function within specific tissues. Nerve growth receptors such as TrkA/TrkB are commonly transported via EDH4.
Epizootic hemorrhagic disease (EHD) is a hemorrhagic disease of white-tailed deer (Odocoileus virginianus) caused by an infection of a virus from the genus Orbivirus subsequently called Epizootic hemorrhagic disease virus (EHDV).
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Epizootic hemorrhagic disease virus ' s genome is about 18-31 kDa in length and consists of 10 segments, where each segment encodes a single protein. [6] These proteins could be one of the seven structural proteins (VP1-VP7) or one of the four non-structural proteins (NS1, NS2, NS3a, or NS3b). [7]
The EH domain is a common motif in a family of proteins involved in endocytic trafficking. This family of four paralogs (EHD1-EHD4) has been implicated in receptor intracellular trafficking, particularly in internalization and recycling to the plasma membrane. The list of functions of EHD proteins is just starting to be populated. [8]
Mechanism of clathrin-dependent endocytosis. Receptor-mediated endocytosis (RME), also called clathrin-mediated endocytosis, is a process by which cells absorb metabolites, hormones, proteins – and in some cases viruses – by the inward budding of the plasma membrane (invagination).
Hypothetic models of VAMP2 conformations and engagement in SNARE complex assembly for neurotransmitter release. Vesicle associated membrane proteins (VAMPs) are a family of SNARE proteins with similar structure, and are mostly involved in vesicle fusion.