about
Structural basis for conformational switching and GTP loading of the large G protein atlastinStructural basis of oligomerization in the stalk region of dynamin-like MxAStructural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3AStructures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranesThe crystal structure of dynaminStructural basis for mechanochemical role of Arabidopsis thaliana dynamin-related protein in membrane fissionInvited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamilyThe N-terminal amphipathic helix of the topological specificity factor MinE is associated with shaping membrane curvatureThe deletion of bacterial dynamin and flotillin genes results in pleiotrophic effects on cell division, cell growth and in cell shape maintenanceA mutation in the mitochondrial fission gene Dnm1l leads to cardiomyopathyAncient dynamin segments capture early stages of host-mitochondrial integrationMolecular paleontology and complexity in the last eukaryotic common ancestorMFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusionThe current approach to initial crystallization screening of proteins is under-sampled.Correcting mitochondrial fusion by manipulating mitofusin conformations.Human biallelic MFN2 mutations induce mitochondrial dysfunction, upper body adipose hyperplasia, and suppression of leptin expression.Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Nucleotide-dependent farnesyl switch orchestrates polymerization and membrane binding of human guanylate-binding protein 1.The Cryo-EM structure of a complete 30S translation initiation complex from Escherichia coliEvolution: On a bender--BARs, ESCRTs, COPs, and finally getting your coatFtsZ-less prokaryotic cell division as well as FtsZ- and dynamin-less chloroplast and non-photosynthetic plastid divisionIdentification of interaction partners of the dynamin-like protein DynA from Bacillus subtilis.Structural insights into membrane fusion at the endoplasmic reticulumLeoA, B and C from enterotoxigenic Escherichia coli (ETEC) are bacterial dynamins.Membrane elongation factors in organelle maintenance: the case of peroxisome proliferation.An inside-out origin for the eukaryotic cell.The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashionStructures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusionThe Effect of a Novel c.820C>T (Arg274Trp) Mutation in the Mitofusin 2 Gene on Fibroblast Metabolism and Clinical Manifestation in a Patient.Membrane tubulovesicular extensions (cytonemes): secretory and adhesive cellular organellesA mitofusin-dependent docking ring complex triggers mitochondrial fusion in vitro.Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion.Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity.Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module.Toward the assembly of a minimal divisome.Mx oligomer: a novel capsid pattern sensor?iniBAC induction Is Vitamin B12- and MutAB-dependent in Mycobacterium marinumStrasburger's legacy to mitosis and cytokinesis and its relevance for the Cell Theory.Genetic links between bacterial dynamin and flotillin proteins.A dynamin-like protein involved in bacterial cell membrane surveillance under environmental stress.
P2860
Q24310183-90257BDF-66ED-400A-90C9-AABD4FE724F0Q27660998-BF42782B-527B-46E1-9785-3D0D4578051CQ27666539-31C082CA-5AAC-4D51-A925-C7EA148A700AQ27667148-AA7FD7D8-E83B-4087-8D11-70172F5EF8F1Q27674161-A824AF91-599C-49DC-811B-F15BA1B1BC48Q27675752-15990B06-2DB1-4B78-80F1-10DD9D326FF1Q28079024-10061492-8378-4438-98A7-1C95ED6B5E4FQ28478761-20F4C101-77F5-49A7-A9C9-4739C5741311Q28489060-281BA507-5F2A-4D75-9BBD-9EC0CB94081BQ28509163-60A12F56-7822-4A7B-A3F3-2755F97784F3Q28652662-75DCF6B1-A64A-48CB-9DD8-87FF7BCE90EBQ28676963-61F182A7-9500-4F31-A96C-88FA41C81B08Q28854598-CF17C985-BC11-467B-905C-64337250006CQ30454574-8B792B25-E209-40F9-8B53-1145A72D70DBQ30839081-CCA691B1-E63D-44AE-B9BF-78BA7704BF80Q33649447-916F9A57-88A3-444A-AEA8-CC2B98885D70Q33842924-F5A7A2DD-506E-49A5-B4E5-1056D49B6CBBQ33913562-ACCE37CB-1B0F-488A-BE4C-83C173B8ED59Q33959135-6F4DFB68-09C6-4DD2-82AA-B6A2E99CE405Q34027290-BB9E5852-D12E-49BB-BF07-61D70CA56ADCQ34180676-BC75A330-6D93-478C-96DD-14F44938DDFCQ34444277-F7758065-5A35-4AAD-8495-166821C237D8Q34573057-A640E79C-F293-4618-8BFA-8B35345FF103Q35244503-065DFA85-F073-43A3-89AB-75C69F5B170EQ35270195-A02DC161-32F2-46ED-B957-DAC2962D28E4Q35372352-C1416EE7-0B8B-46CD-B8EB-25F8135F167FQ35943304-A4815BB0-DC88-4566-80D9-3DD0F70AEF76Q36078261-C69A30E9-5C5A-42A7-87AF-131BDB75DC00Q36246291-1BA1DF5E-1526-47B9-BD43-987B8A7AF6C5Q36849197-5288053D-FF96-438A-BA3D-25FEB55826BFQ37056311-A3E8DA4D-F5F4-4CE4-8F3D-CD2BDAC8AFC0Q37365417-779F6448-E5D2-4864-B643-2706B18958F5Q37764235-2CAFD44A-9465-4411-A753-49D1A9485EC8Q37891680-5D34F8CC-AC86-4D8D-9FBD-6151EEAEA6C1Q38241198-DE1C9FB3-1CAD-42B5-A18D-0ED0C9BAB44AQ38834397-BC23CB8F-0F41-4690-83E3-CF222809540DQ39543198-8DF6C3FB-31DA-40E4-A8E0-272A6A16E0E1Q39625937-2444A6F4-187C-4C47-B513-5CE7A2DA92D9Q40026488-B3B7BE00-0B97-4676-AB6B-BC2184CD25FEQ40924758-FED4F2F9-8BD7-4FD3-ADAF-AE93534B1E61
P2860
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в листопаді 2006
@uk
name
A bacterial dynamin-like protein
@en
A bacterial dynamin-like protein
@nl
type
label
A bacterial dynamin-like protein
@en
A bacterial dynamin-like protein
@nl
prefLabel
A bacterial dynamin-like protein
@en
A bacterial dynamin-like protein
@nl
P2860
P356
P1433
P1476
A bacterial dynamin-like protein
@en
P2093
P2860
P2888
P304
P356
10.1038/NATURE05312
P407
P577
2006-11-22T00:00:00Z
P6179
1024290909