A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane. - Wikidata - awgldk - TriplyDB

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

http://www.wikidata.org/entity/Q30713856

about

CLASP modulates microtubule-cortex interaction during self-organization of acentrosomal microtubules.Molecular diversity of phospholipase D in angiosperms Multifunctional Microtubule-Associated Proteins in Plants Phospholipase D and phosphatidic acid in plant defence response: from protein-protein and lipid-protein interactions to hormone signalling Proteomic Analysis of Microtubule Interacting Proteins over the Course of Xylem Tracheary Element Formation in Arabidopsis The connection of cytoskeletal network with plasma membrane and the cell wall Phospholipase D Global analysis of transcriptome responses and gene expression profiles to cold stress of Jatropha curcas L.Microtubule organization in three-dimensional confined geometries: evaluating the role of elasticity through a combined in vitro and modeling approach.Understanding phase behavior of plant cell cortex microtubule organization Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation.Analysis of cortical arrays from Tradescantia virginiana at high resolution reveals discrete microtubule subpopulations and demonstrates that confocal images of arrays can be misleading.A bacterial acetyltransferase destroys plant microtubule networks and blocks secretion Rationalization of paclitaxel insensitivity of yeast β-tubulin and human βIII-tubulin isotype using principal component analysis.Phospholipid signaling in plants: holding on to phospholipase D.Lipid profiling demonstrates that suppressing Arabidopsis phospholipase Dδ retards ABA-promoted leaf senescence by attenuating lipid degradation Proteins implicated in mediating self-incompatibility-induced alterations to the actin cytoskeleton of Papaver pollen.Phospholipase D: enzymology, functionality, and chemical modulation Microtubules in plants Crosstalk between Phospholipase D and Sphingosine Kinase in Plant Stress Signaling.Characterisation of Lipid Changes in Ethylene-Promoted Senescence and Its Retardation by Suppression of Phospholipase Dδ in Arabidopsis Leaves.Regulation of developmental and environmental signaling by interaction between microtubules and membranes in plant cells.Evaluating the microtubule cytoskeleton and its interacting proteins in monocots by mining the rice genome Function and regulation of phospholipid signalling in plants.Overexpression of Cucumber Phospholipase D alpha Gene (CsPLDα) in Tobacco Enhanced Salinity Stress Tolerance by Regulating Na+-K+ Balance and Lipid Peroxidation.Molecular, cellular, and physiological responses to phosphatidic acid formation in plants.Microtubules, signalling and abiotic stress.Cytoskeleton-dependent endomembrane organization in plant cells: an emerging role for microtubules.Phospholipids: molecules regulating cytoskeletal organization in plant abiotic stress tolerance Lipid remodelling: Unravelling the response to cold stress in Arabidopsis and its extremophile relative Eutrema salsugineum Protein Phosphatase 2Cs and Microtubule-Associated Stress Protein 1 Control Microtubule Stability, Plant Growth, and Drought Response.Phospholipase D δ knock-out mutants are tolerant to severe drought stress.Phospholipase d activation correlates with microtubule reorganization in living plant cells.Phospholipid signaling during stramenopile development.A mechanochemical model explains interactions between cortical microtubules in plants.Cold acclimation and low temperature resistance in cotton: Gossypium hirsutum phospholipase Dalpha isoforms are differentially regulated by temperature and light.Signal transduction during cold stress in plants.Phospholipases Dζ1 and Dζ2 have distinct roles in growth and antioxidant systems in Arabidopsis thaliana responding to salt stress.Ca2+ influx and phosphoinositide signalling are essential for the establishment and maintenance of cell polarity in monospores from the red alga Porphyra yezoensis.Depletion of the membrane-associated acyl-coenzyme A-binding protein ACBP1 enhances the ability of cold acclimation in Arabidopsis.

P2860

Q24646813-48835D50-8670-4287-BE5A-8584DCB2E895 Q24803089-0C839334-3BE8-49C9-A078-4808DD209D67 Q26752489-985EDDD5-13BF-4523-942E-F20DEE6EFAEB Q27011789-0CF2225C-6C80-45A1-9798-6890202FA154 Q27318808-31655382-65B6-48AD-8CB8-6CA8AF302A6B Q28081889-E687BAFF-AD91-4385-9057-255193FD8F16 Q28253553-BBE5DE37-72DF-4217-9A74-A7B18B1F8998 Q28661206-BDC38139-9F34-4106-B121-5D3211C06A2E Q30478862-9C2DF79A-41AE-4F3E-A10E-75013D76859E Q30495370-F4F2CCDE-68F8-4284-B129-7015B49663F9 Q31022309-57F48F01-DEC9-46A8-B973-0D3876833312 Q33330238-1B2900B0-B259-4523-8C1D-91C3D04B5639 Q34154462-53E9DAEC-2109-457A-93BA-A1B6BBB879D0 Q34360044-937C8157-75D1-4D5A-B561-1640982AFC17 Q34457650-8DE26202-EC64-4F05-B225-57A8F1016A9E Q34770084-D2C1EB21-C974-4182-8771-443C3D7F85D1 Q35205950-0999980F-B6E6-4F74-81EA-EAD460907E8B Q35599714-AB11EBF8-E9D7-4DD9-BAD0-775124628191 Q35636268-52B280AD-3652-4834-A741-3D4E40C470F9 Q35970361-910297E2-1D26-42F9-8208-694DF33B61E5 Q36328733-EB4966A9-1FFE-4592-BE30-FB9E88818759 Q36547297-08066E74-640B-471D-9715-92A3AE27F2C1 Q37254248-D5AFD852-1536-4F11-AB5D-760EB51F1D66 Q37257492-A0222CEA-E8F5-48A8-B71D-0D4352F03F5F Q37740642-51C19C3C-F4F9-4812-9C88-B2C8AA1E4227 Q37856598-FD6961F6-1113-4490-92C9-8099FB6302A5 Q38073298-9ECFB3C9-55B5-4948-9271-DE9968757820 Q38104402-3326C3DD-F9A3-4FB4-B4B5-387A513370FA Q38192886-CF809C02-CE62-401C-96DB-9549FBCD0E25 Q38619520-FB212336-7C7C-4F21-B344-812F71C7B9A9 Q38907587-4D6BD9EF-8F65-4A38-91FD-0ECD10FD20D9 Q38974052-801F7394-8BBB-4760-8313-7E00FA1ECD94 Q40631632-C0EC174F-B492-441E-9ADA-60BA0C1EB704 Q41883075-251E63F7-D834-4163-9693-7623519AE3CC Q41908925-B0286B47-02B4-47FB-8893-A899D50BABFE Q42660948-C87D7A63-D5E7-4D0D-9811-8B4001D8FBD0 Q42878154-65CB33F0-4F79-4BF4-8A06-D543A9ACC649 Q43031242-D87C4B4A-A0BE-43AD-8CF8-CAC188E6A974 Q43073281-4E7D3783-318D-41AD-A0C0-206A05500FE4 Q43182561-18336B94-D947-426A-A685-093D0A6D5FB9

P2860

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

http://www.wikidata.org/entity/Q30713856

description

2001 nî lūn-bûn

@nan

2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

@ast

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

@en

type

label

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

@ast

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

@en

prefLabel

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

@ast

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

@en

P1433

Q30713856-2295F2E8-E3CF-4915-8521-0F14D02EF8BC

P1476

Q30713856-825535C7-5FBA-429F-BACA-F39ED49901D4

P2093

Q30713856-505AB750-DD85-430F-9865-9CEBB471995E

Q30713856-5B9237EC-134C-4FAB-8D8A-370E04B72961

Q30713856-91C2743C-6C10-48C1-9354-6FCBF61039A4

Q30713856-938EF859-C6E5-403B-825D-3B127990A9A0

Q30713856-CB1471ED-73A2-4701-B36F-179FF7EC333A

Q30713856-E4C8097D-1B13-4752-ACC6-67F671D62E5B

Q30713856-EBF8E545-3E13-4449-ABBB-39FAC785449B

Q30713856-F180BACF-71AA-45D5-88B3-4945067D21B7

P304

Q30713856-E5113C18-603B-4705-BEA9-F108A6BFC567

P31

Q30713856-88F4827E-4C6B-46D3-B22A-4345EDCD364C

P356

Q30713856-1D228814-5863-40AD-A874-EA6F235D022E

P433

Q30713856-2F2EEFBF-9EA7-49A4-BBC8-8F0437E7F4EC

P478

Q30713856-0A6844EB-843D-44B4-AC4D-DE0C916C5CB3

P577

Q30713856-608206AE-6E92-4BC8-94A8-7AD3E8DE732D

P5875

Q30713856-16C3A80D-814A-460C-B317-35441C3FC418

P698

Q30713856-20F3F634-B8C6-47D8-979F-D49784D4B519

P356

P1433

P1476

A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane.

@en

P2093

Collings DA

http://www.w3.org/2001/XMLSchema#string

Cyr RJ

http://www.w3.org/2001/XMLSchema#string

Gardiner JC

http://www.w3.org/2001/XMLSchema#string

Gilroy S

http://www.w3.org/2001/XMLSchema#string

Harper JD

http://www.w3.org/2001/XMLSchema#string

Marc J

http://www.w3.org/2001/XMLSchema#string

Ritchie S

http://www.w3.org/2001/XMLSchema#string

Weerakoon ND

http://www.w3.org/2001/XMLSchema#string

P304

2143-2158

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1105/TPC.13.9.2143

http://www.w3.org/2001/XMLSchema#string

P433

9

http://www.w3.org/2001/XMLSchema#string

P478

13

http://www.w3.org/2001/XMLSchema#string

P577

2001-09-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

277472934

http://www.w3.org/2001/XMLSchema#string

P698

11549769

http://www.w3.org/2001/XMLSchema#string