LIS1, CLIP-170's key to the dynein/dynactin pathway.The ALS8 protein VAPB interacts with the ER-Golgi recycling protein YIF1A and regulates membrane delivery into dendritesMammalian CLASPs are required for mitotic spindle organization and kinetochore alignmentMicrotubule-binding proteins CLASP1 and CLASP2 interact with actin filamentsPericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis.SLAIN2 links microtubule plus end-tracking proteins and controls microtubule growth in interphaseAsymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi networkDynamic microtubules regulate dendritic spine morphology and synaptic plasticityAn EB1-binding motif acts as a microtubule tip localization signalRole of CLASP2 in microtubule stabilization and the regulation of persistent motilityA complex of Kif18b and MCAK promotes microtubule depolymerization and is negatively regulated by Aurora kinasesBicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complexCLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortexLaminin-based cell adhesion anchors microtubule plus ends to the epithelial cell basal cortex through LL5alpha/betaRegulation of localization and activity of the microtubule depolymerase MCAKBicaudal D induces selective dynein-mediated microtubule minus end-directed transportMicrotubule plus-end tracking proteins in neuronal developmentBicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entryStructure-function relationship of CAP-Gly domainsMammalian end binding proteins control persistent microtubule growthTermination of Protofilament Elongation by Eribulin Induces Lattice Defects that Promote Microtubule CatastrophesCLASPs attach microtubule plus ends to the cell cortex through a complex with LL5betaBICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to cellular structures.EB1 and EB3 control CLIP dissociation from the ends of growing microtubulesDifferential expression of liprin-α family proteins in the brain suggests functional diversificationTRAK/Milton motor-adaptor proteins steer mitochondrial trafficking to axons and dendritesMICAL3 Flavoprotein Monooxygenase Forms a Complex with Centralspindlin and Regulates Cytokinesis.Dynamic behavior of GFP-CLIP-170 reveals fast protein turnover on microtubule plus ends.STIM1 is a MT-plus-end-tracking protein involved in remodeling of the ER.Aurora B spatially regulates EB3 phosphorylation to coordinate daughter cell adhesion with cytokinesis.Dynamic microtubules produce an asymmetric E-cadherin-Bazooka complex to maintain segment boundaries.CLASP2 interacts with p120-catenin and governs microtubule dynamics at adherens junctions.Actin-microtubule coordination at growing microtubule endsMicrotubule minus-end regulation at spindle poles by an ASPM-katanin complexA highly expressed family 1 beta-glucosidase with transglycosylation capacity from the anaerobic fungus Piromyces sp. E2.Deconvolution of Buparlisib's mechanism of action defines specific PI3K and tubulin inhibitors for therapeutic intervention.Probing cytoskeletal modulation of passive and active intracellular dynamics using nanobody-functionalized quantum dots.Genomic DNA analysis of genes encoding (hemi-)cellulolytic enzymes of the anaerobic fungus Piromyces sp. E2.Cel6A, a major exoglucanase from the cellulosome of the anaerobic fungi Piromyces sp. E2 and Piromyces equi.A role for the Rab6B Bicaudal-D1 interaction in retrograde transport in neuronal cells.
P50
Q24293597-BA7B2A0E-1B67-490C-BB92-80004E5868E6Q24294526-8F86FAE0-4DAC-456A-9588-1464EEE7134AQ24298000-690B4094-16D8-499B-BBF7-C0B4E0281CC2Q24299232-EDA12EE2-A1FA-4FB9-AF52-3B929A3448F3Q24305350-DF31042C-DBB1-4376-ACF9-35B1283FB0FFQ24305975-7B2D8CB6-9018-4849-8D91-CFCA12BD1CAEQ24307694-C892F000-D85B-44B5-A8DA-2D0DD1DA98FBQ24316951-6A9E8CAD-B326-4C2B-9FFA-8C45C800004AQ24317437-389BD51F-BC9F-4849-BB80-E32F17F0EC7CQ24317546-BB1E3E30-1AD4-49AA-B5E7-D8B6FB0ACC19Q24319371-132B6C36-7197-45DA-9A91-FA7D6483FC15Q24321547-E8170EE2-7D59-41EB-B1FA-C9B186A9ABDDQ24337317-A2FEF2E8-B03D-4A9A-AE81-68A1982A21EBQ24602789-694C2FF0-A703-4764-A379-5EA5350779C2Q24614530-B223DDBD-ABEE-4CA9-A9C2-69B6E3E073ECQ24644322-7591A2E7-2EBC-4FFE-924A-B9F2CD556BACQ26766239-149890CD-8834-4A11-9CB2-B8E43CF42C84Q27324750-3B78B7ED-326E-47B0-9239-CCB54B9E9975Q27648001-8B857852-560D-4FD0-BFC5-EA3C7675DB3BQ27653991-B37B4016-892D-4297-9AF4-9FF9200C7452Q27711854-BE679A45-DB02-46EE-BC6C-AEAAAC3E8EB7Q28250713-398137D5-DDBA-4C8C-B9AB-6CEDFBFA81A9Q28274497-6502DDBC-1902-4D12-879D-9B407E919C98Q28506248-D1270B30-97B6-452B-A0E1-1041F0EB4E61Q28506845-59E8DC9B-5152-4885-80C1-D5C161F34E31Q28594138-2CFA7DEC-6D3D-4C9D-A335-AFB6BB81445BQ29568898-6665711E-F83D-4A25-915B-0CA15FEBA3C9Q30481430-AA5DCAD5-B1BD-4864-8515-E5405D852353Q30485016-D47B0CB7-4907-4B67-867B-E59A8B15F585Q30540082-DFF3A173-F181-4054-B29D-CD9D2AE7DDC2Q30540536-E9424C4D-A8FC-4C1F-BFBC-EBB45618340DQ30560513-60A44C73-7B7E-4C91-A76D-51FD4143E83AQ30629472-EDA83C65-2C1A-4527-80F9-108A5796FF40Q30665196-BF47F13F-55EF-4262-8D19-BF3D02EB2F4CQ30706233-E4421C74-8FB9-4C28-ABBD-5983E6C0269EQ30841629-ECE343F4-EB57-4DEE-9B1C-A6D6FC38868BQ30842804-0FE6E58A-96F3-421A-9DFD-F79DA183453BQ31007368-083812AC-2A93-48CD-A673-D695ACBC02D5Q31148853-B5108086-0052-41CF-BBFA-C89CCF7F4563Q33294582-2C52EF5A-1E2F-40E4-B821-6D465C4298E7
P50
description
Nederlandse hoogleraar
@nl
Russian cell biologist
@en
russische Zellbiologin
@de
name
Anna Achmanova
@nl
Anna Achmanova
@sl
Anna Akhmanova
@ca
Anna Akhmanova
@de
Anna Akhmanova
@en
Anna Akhmanova
@es
Anna Akhmanova
@fr
Ахманова, Анна Сергеевна
@ru
type
label
Anna Achmanova
@nl
Anna Achmanova
@sl
Anna Akhmanova
@ca
Anna Akhmanova
@de
Anna Akhmanova
@en
Anna Akhmanova
@es
Anna Akhmanova
@fr
Ахманова, Анна Сергеевна
@ru
altLabel
A. Achmanova
@nl
A. Akhmanova
@nl
A.S. Akhmanova
@en
A.S. Akhmanova
@nl
Anna Akhmanova
@nl
Ахманова, Анна Сергеевна
@sq
prefLabel
Anna Achmanova
@nl
Anna Achmanova
@sl
Anna Akhmanova
@ca
Anna Akhmanova
@de
Anna Akhmanova
@en
Anna Akhmanova
@es
Anna Akhmanova
@fr
Ахманова, Анна Сергеевна
@ru
P27
P1006
P214
P1006
P101
P1053
B-8896-2011
P19
P2080
P21
P213
0000 0003 9099 6464