about
Deficiency of the cytoskeletal protein SPECC1L leads to oblique facial cleftingThe ATAC acetyl transferase complex controls mitotic progression by targeting non-histone substrates.Cellular Mechanisms of Ciliary Length ControlNeurodegeneration and microtubule dynamics: death by a thousand cutsKif26b controls endothelial cell polarity through the Dishevelled/Daam1-dependent planar cell polarity-signaling pathway.HDAC6 inhibitor blocks amyloid beta-induced impairment of mitochondrial transport in hippocampal neuronsSingle molecule imaging reveals differences in microtubule track selection between Kinesin motorsNatural product Celastrol destabilizes tubulin heterodimer and facilitates mitotic cell death triggered by microtubule-targeting anti-cancer drugsMolecular Basis for Specific Regulation of Neuronal Kinesin-3 Motors by Doublecortin Family ProteinsStructural basis of tubulin tyrosination by tubulin tyrosine ligaseStructures of a diverse set of colchicine binding site inhibitors in complex with tubulin provide a rationale for drug discoveryThe major alpha-tubulin K40 acetyltransferase alphaTAT1 promotes rapid ciliogenesis and efficient mechanosensationTargeting Microtubules for Wound RepairThe promise and perils of HDAC inhibitors in neurodegenerationEmergent complexity of the cytoskeleton: from single filaments to tissueSelective targeting of tumorigenic cancer cell lines by microtubule inhibitorsUnderstanding the basis of drug resistance of the mutants of αβ-tubulin dimer via molecular dynamics simulationsαTAT1 is the major α-tubulin acetyltransferase in miceLoukoumasomes Are Distinct Subcellular Structures from Rods and Rings and Are Structurally Associated with MAP2 and the Nuclear Envelope in Retinal CellsCyclin-dependent kinases regulate splice-specific targeting of dynamin-related protein 1 to microtubules.Embryonic neurogenesis in Pseudopallene sp. (Arthropoda, Pycnogonida) includes two subsequent phases with similarities to different arthropod groupsMotor domain phosphorylation modulates kinesin-1 transportTgATAT-Mediated α-Tubulin Acetylation Is Required for Division of the Protozoan Parasite Toxoplasma gondiiDoublecortin (Dcx) family proteins regulate filamentous actin structure in developing neurons.Cytoskeletal changes in actin and microtubules underlie the developing surface mechanical properties of sensory and supporting cells in the mouse cochlea.Mal3, the Schizosaccharomyces pombe homolog of EB1, changes the microtubule latticeAltered dynein-dependent transport in piRNA pathway mutantsStarvation-induced hyperacetylation of tubulin is required for the stimulation of autophagy by nutrient deprivationDynamics of multiple nuclei in Ashbya gossypii hyphae depend on the control of cytoplasmic microtubules length by Bik1, Kip2, Kip3, and not on a capture/shrinkage mechanism.Regulation of mouse oocyte microtubule and organelle dynamics by PADI6 and the cytoplasmic lattices.Tubulin tyrosine ligase-like genes ttll3 and ttll6 maintain zebrafish cilia structure and motility.Highly acetylated tubulin permits enhanced interactions with and trafficking of plasmids along microtubulesTubulin acetyltransferase αTAT1 destabilizes microtubules independently of its acetylation activity.EB1, p150Glued, and Clasp1 control endothelial tubulogenesis through microtubule assembly, acetylation, and apical polarizationLoss of MEC-17 leads to microtubule instability and axonal degeneration.Cholesterol-mediated activation of acid sphingomyelinase disrupts autophagy in the retinal pigment epitheliumTubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respirationROS homeostasis as a prerequisite for the accomplishment of plant cytokinesis.Panobinostat (LBH589)-induced acetylation of tubulin impairs megakaryocyte maturation and platelet formation.TgICMAP1 is a novel microtubule binding protein in Toxoplasma gondii.
P2860
Q24307839-BBC1BA9E-E748-472F-B875-3E22C262784FQ24323898-A470FC1F-DB0C-4FE6-A986-E7E5B9AFC3CAQ26769756-DDB9A79B-3FD4-49F0-B6C0-BB0FDF00B092Q26781649-F6D9AD8A-5A02-4C7A-A609-75BD731DEBC5Q27306718-D134D86E-B2D1-421A-BCDE-E680F30FF63BQ27324238-F68AC550-85EB-4D70-92AA-7C18A4C45A64Q27325835-0525D627-E918-49B9-8888-9E9D6C022A9BQ27330384-2AFF0839-AF36-4703-BE6B-81667B052D00Q27671083-628AB9E7-5307-4B87-B43B-D538926AA129Q27676036-84159910-4E17-4C55-9404-E49DD9FA4DF9Q27702294-CB0286A5-7685-4547-B796-443FFE5A967EQ28000035-99395825-9AC8-4D72-BFD5-58F4BBC9FDFDQ28075978-6CE429A3-1105-448A-8543-0A546D3487BAQ28087539-54AFA849-817F-4D6A-9962-E93C23C3EAB4Q28238533-77D8E286-F6A0-43AB-B643-33FC2DFF2425Q28474745-744BF6D8-B0BE-410C-8F99-BE41770E9C59Q28482107-BF609CC5-ED8D-4B65-B378-8C5F8E6051B4Q28511187-05AE946F-8EA2-41C4-B6DE-E3AFB2B0B2AAQ28553081-F5DAD720-0B97-4F25-8933-0D831F4EB86BQ28591774-56345460-FF30-4DD4-8B9F-CED37020AB70Q28660883-B9D4AC60-C99E-4BF5-A4D4-80C72348A1A6Q28661717-C1A47786-84A6-4D2A-803D-44F3EB71DEA2Q28834427-EC8DB141-DDDC-4083-91E9-E8EC5365BBF3Q30418275-47DEE083-4950-48BD-B491-6E741A100185Q30453489-6389E2F9-438A-4B44-A16E-A9B7AFECC9E8Q30484323-E2E365AD-D08B-4254-98F6-1ED9A8ED5D8BQ30487843-330B4E96-93AD-4450-ACD7-B1AF1C39F41EQ30495728-B7C6FE25-7373-42C1-801D-2D760AF8CE1AQ30497174-7A469949-F107-40C6-AFF1-EFD79020F5B6Q30498051-71225791-72F2-4F4F-9C5B-038579B9DC49Q30499111-304DC332-6D0C-430F-B70A-4C534A8DFD76Q30537126-55D86B59-3056-431E-9F4C-A80102EF84D7Q30537332-4C28ABF3-E471-417C-9332-844BEA5F7333Q30539206-6F9393CE-AD4E-4B64-A8E4-E01AA912F126Q30573115-C2EADD76-60D4-425B-9522-E258CEDE6F5EQ30612009-434B54DD-6683-42D4-9222-82599DB21E73Q33346359-16E1B629-A896-4FC2-91C8-2F294BAA3B6AQ33363049-9243318F-A8B9-45BE-9DF6-C29565933D9BQ33400014-6980FE60-9F77-4051-B69C-EE3E2CE49E17Q33510162-0FE60387-4765-4598-9A2C-A2B2601BD7D8
P2860
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Tubulin modifications and their cellular functions.
@ast
Tubulin modifications and their cellular functions.
@en
type
label
Tubulin modifications and their cellular functions.
@ast
Tubulin modifications and their cellular functions.
@en
prefLabel
Tubulin modifications and their cellular functions.
@ast
Tubulin modifications and their cellular functions.
@en
P2860
P1476
Tubulin modifications and their cellular functions
@en
P2093
Kristen J Verhey
P2860
P356
10.1016/J.CEB.2007.11.010
P577
2008-01-15T00:00:00Z