about
Myosin VI regulates endocytosis of the cystic fibrosis transmembrane conductance regulatorMyosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cellsThe interaction between cytoplasmic dynein and dynactin is required for fast axonal transportMyosin superfamily evolutionary historyLong-Term Live Cell Imaging of Cell Migration: Effects of Pathogenic Fungi on Human Epithelial Cell Migration.The cytoskeletal system of nucleated erythrocytes. I. Composition and function of major elements.Human oral keratinocytes: a model system to analyze host-pathogen interactions.The short apical membrane half-life of rescued {Delta}F508-cystic fibrosis transmembrane conductance regulator (CFTR) results from accelerated endocytosis of {Delta}F508-CFTR in polarized human airway epithelial cells.Actin- and microtubule-dependent organelle motors: interrelationships between the two motility systems.PDZ domain interaction controls the endocytic recycling of the cystic fibrosis transmembrane conductance regulator.Rab-GDI inhibits myosin V-dependent vesicle transport in squid giant axon.Characterization of antibodies to the head and tail domains of squid brain myosin V.Length and appearance of projections on neuronal microtubules in vitro after negative staining: evidence against a crosslinking function for MAPs.Membrane associated nonmuscle myosin II functions as a motor for actin-based vesicle transport in clam oocyte extracts.Rho-kinase is required for myosin-II-mediated vesicle transport during M-phase in extracts of clam oocytes.GTPase rho is involved in myosin-II-mediated contraction of pseudo-contractile rings and transport of vesicles in extracts of clam oocytes.Reconstitution of active pseudo-contractile rings and myosin-II-mediated vesicle transport in extracts of clam oocytes.Effects of Vanadate on Actin-dependent Vesicle Motility in Extracts of Clam Oocytes.Localization of Myosin on Tubulovesicular Organelles in the Squid Giant Axon by Immuno-EM.Effects of myosin-II antibody on actin-dependent vesicle transport in extracts of clam oocytes.Stimulation of cell motility and expression of late markers of differentiation in human oral keratinocytes by Candida albicans.Substructure of sidearms on squid axoplasmic vesicles and microtubules visualized by negative contrast electron microscopyDynamic instability of native microtubules from squid axons is rare and independent of gliding and vesicle transportComparison of proteolytic cleavage patterns of alpha-tubulins and beta-tubulins from taxonomically distant speciesComparative study of shark and beef brain microtubulesCalmodulin regulates fast axonal transport of squid axoplasm organellesMovement of axoplasmic organelles on actin filaments from skeletal muscleInteraction of actin- and microtubule-based motors in squid axoplasm probed with antibodies to myosin V and kinesinActin bundles in neuronal growth cone observed with the Pol-ScopeMyosin V in the brain: mutations lead to neurological defectsGlobular tail fragment of myosin-V displaces vesicle-associated motor and blocks vesicle transport in squid nerve cell extractsInteractions between recombinant conventional squid kinesin and native myosin-VTumor necrosis factor-alpha induces changes in mitochondrial cellular distribution in motor neuronsVoltage-controlled cellular viability of preosteoblasts on polarized cpTi with varying surface oxide thicknessInhibition of Microtubule-Dependent, Minus-End Directed Transport of Axoplasmic Organelles by an Antibody Specific for the Intermediate Chain of Dynein
P50
Q24298963-87B9E35C-8267-49C2-8E08-54AE4BFB8CB5Q24304047-21FFC4DC-BBAB-4F84-862B-D661B92E4CE2Q24644297-583E1398-CD21-4249-BA50-CDB5AAD27637Q28207779-C01B659D-59A1-4797-9F56-F34C0D8B047AQ35820462-3FE34F9A-7857-4B73-A3A7-5BED818BA9FFQ36206240-C5F88854-0A97-47E1-BD86-E07CF1BDADFAQ39653256-0DFB65CA-E1D4-4D88-9C6B-389F4C3846D8Q39728531-AEA3AC89-3F91-4F5D-B9FF-A74F30A9AE45Q40529200-40FEE72B-AB1B-4090-9BF2-E04CEA394142Q40712140-C22837AD-7FA1-46E1-B781-1DDC59A4FD39Q44635482-E71A5907-693A-4D15-AA1B-4143BB760C7CQ48589934-18786B0A-55B3-4590-90BC-79153B437429Q48736085-A8A0D83A-F152-4CBC-98E3-76CE68687466Q48787614-A92A17A6-E414-4319-B5D5-80789123C27DQ48819601-5E028E0C-E040-42B2-B4C0-73D00CD065DDQ48846850-D2242ECB-CC32-4E81-A2B1-99C439A344C2Q48875148-C7469469-75DA-47A2-AFEF-2967FBC5D2C7Q48908668-50E20107-E8F2-4156-83AD-2F883FBFA8F2Q50004591-396CDA9D-36C4-4A04-AADD-4339F2798FE5Q50721314-05D42DC2-1A07-4F10-8765-A0C9734603D0Q51757188-3C1A400A-D6B9-4C50-803E-451D0AD86454Q68985084-C1DC90BB-2E0B-414A-B5C8-3CFCF6678EE9Q69041593-11ED35DC-8B08-40D1-9D72-0EA7E482304EQ70197885-8DB01864-BF14-4AA1-8767-D9844AB0571BQ71095800-269C6204-4A04-431B-9AF7-09A2B683C544Q71700690-6A94C767-7497-45DC-BE4E-CF23F25ACEA8Q72790852-87AC8630-CC07-468D-85F3-36FF2F27F48EQ73198082-EF516F35-935A-4574-A012-86D255EE7BEDQ73924651-024B51B5-56C6-4DB0-B9E6-CB381B05E7B3Q77486271-3EF72051-EC85-418B-A4B6-0D46CF69A6D5Q78469368-FB9BEC91-41C1-4A46-9AEF-DDB6797EC836Q79219100-72CE04FB-310A-4EDA-93AD-C9C7398F1219Q80121942-A9096FAB-869B-4B9C-9DDE-9547466E7334Q87018488-6A9CF410-837F-45A2-9BF3-563132675D49Q88224496-DFDDA7BD-D4B5-4BA5-9972-4034EC464B47
P50
description
American cell biologist
@en
celbioloog
@nl
name
George M Langford
@ast
George M Langford
@es
George M Langford
@nl
George M. Langford
@en
type
label
George M Langford
@ast
George M Langford
@es
George M Langford
@nl
George M. Langford
@en
altLabel
George Langford
@en
prefLabel
George M Langford
@ast
George M Langford
@es
George M Langford
@nl
George M. Langford
@en
P108
P1153
7004301651
P1960
Xx-5zIgAAAAJ
P2038
George_Langford
P21
P31
P496
0000-0001-9737-2182
P569
1944-08-26T00:00:00Z