Molecular properties of a novel, hydrophilic cation-binding protein associated with the plasma membrane.
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Multifunctional Microtubule-Associated Proteins in PlantsThe Arabidopsis thaliana immunophilin ROF1 directly interacts with PI(3)P and PI(3,5)P2 and affects germination under osmotic stressExpression of developmentally regulated plasma membrane polypeptide (DREPP2) in rice root tip and interaction with Ca(2+)/CaM complex and microtubule.Interaction of the trans-frame potyvirus protein P3N-PIPO with host protein PCaP1 facilitates potyvirus movementComparative proteomics and metallomics studies in Arabidopsis thaliana leaf tissues: evaluation of the selenium addition in transgenic and nontransgenic plants using two-dimensional difference gel electrophoresis and laser ablation imaging.Root iTRAQ protein profile analysis of two Citrus species differing in aluminum-tolerance in response to long-term aluminum-toxicity.Characterization of the role of calcium in regulating the microtubule-destabilizing activity of MDP25.Calciomics: integrative studies of Ca2+-binding proteins and their interactomes in biological systems.DEVELOPMENTALLY REGULATED PLASMA MEMBRANE PROTEIN of Nicotiana benthamiana contributes to potyvirus movement and transports to plasmodesmata via the early secretory pathway and the actomyosin system.PCaPs, possible regulators of PtdInsP signals on plasma membrane.Plasma membrane-associated cation-binding protein 1-like protein negatively regulates intercellular movement of BaMV.Enhancement of cell wall protein SRPP expression during emergent root hair development in Arabidopsis.A hydrophilic cation-binding protein of Arabidopsis thaliana, AtPCaP1, is localized to plasma membrane via N-myristoylation and interacts with calmodulin and the phosphatidylinositol phosphates PtdIns(3,4,5)P(3) and PtdIns(3,5)P(2).A novel-type phosphatidylinositol phosphate-interactive, Ca-binding protein PCaP1 in Arabidopsis thaliana: stable association with plasma membrane and partial involvement in stomata closure.The Ca(2+) -binding protein PCaP2 located on the plasma membrane is involved in root hair development as a possible signal transducer.In planta proximity dependent biotin identification (BioID).
P2860
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P2860
Molecular properties of a novel, hydrophilic cation-binding protein associated with the plasma membrane.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Molecular properties of a nove ...... ated with the plasma membrane.
@en
Molecular properties of a nove ...... ated with the plasma membrane.
@nl
type
label
Molecular properties of a nove ...... ated with the plasma membrane.
@en
Molecular properties of a nove ...... ated with the plasma membrane.
@nl
prefLabel
Molecular properties of a nove ...... ated with the plasma membrane.
@en
Molecular properties of a nove ...... ated with the plasma membrane.
@nl
P2093
P356
P1476
Molecular properties of a nove ...... ated with the plasma membrane.
@en
P2093
Masayoshi Maeshima
Momoe Suito
Nahoko Nagasaki
Rie Tomioka
P304
P356
10.1093/JXB/ERL284
P577
2007-01-29T00:00:00Z