Results 171 to 180 of about 3,215 (217)
A De Novo <i>DNM1L</i> Mutation in Twins with Variable Symptoms, Including Paraparesis and Optic Neuropathy. [PDF]
BiomoleculesNasca A +8 more
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Dynamin-Related Protein 1 (Drp1) in Inflammatory Bowel Disease: Molecular Pathways Connecting Mitochondrial Dynamics with Intestinal Inflammation and Homeostasis. [PDF]
Int J Mol SciChi Y +6 more
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Blue Light Induces Retinal Ganglion Cell Damage by Stimulating Drp1-Dependent Mitochondrial Fission and Activating NF-κB/NOX4 Axis. [PDF]
Invest Ophthalmol Vis SciHan XH +9 more
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DRP1 bridges complement component C5a and podocyte injury in lupus nephritis. [PDF]
Mol TherLei J, Wen Z.
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Erythroblast enucleation at a glance.
J Cell SciNewton LM, Fowler VM, Humbert PO.
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Journal of Cell Science, 2009 The superfamily of dynamins includes classical dynamins and dynamin-related proteins. Classical dynamins are proteins that share sequence similarity with the first described dynamin, which is a large GTPase with five characteristic domains.
Jenny E Hinshaw, Hinshaw Jenny E
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Endocrine Reviews, 1995
I. Introduction THE transport of proteins, hormones, and nutrients to different locations within a cell is an essential process for many of the functions of eukaryotic cells. It is of particular importance in complex multicellular organisms to enable the cells to communicate with one another.
J P, Liu, P J, Robinson
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I. Introduction THE transport of proteins, hormones, and nutrients to different locations within a cell is an essential process for many of the functions of eukaryotic cells. It is of particular importance in complex multicellular organisms to enable the cells to communicate with one another.
J P, Liu, P J, Robinson
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Dynamins in human diseases: differential requirement of dynamin activity in distinct tissues
Current Opinion in Cell Biology, 2023Dynamin, a 100-kDa GTPase, is one of the most-characterized membrane fission machineries catalyzing vesicle release from plasma membrane during endocytosis. The human genome encodes three dynamins: DNM1, DNM2 and DNM3, with high amino acid similarity but distinct expression patterns. Ever since the discoveries of dynamin mutations associated with human
Ya-Wen Liu
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Current Opinion in Cell Biology, 2002
The GTPase dynamin is essential for endocytosis, but its mechanism of action remains uncertain. Structures of its GTPase domain, as well as that of assembled dynamin, have led to major advances in understanding the structural basis of its mode of action.
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The GTPase dynamin is essential for endocytosis, but its mechanism of action remains uncertain. Structures of its GTPase domain, as well as that of assembled dynamin, have led to major advances in understanding the structural basis of its mode of action.
openaire +2 more sources