AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
about
The ascorbate-glutathione-α-tocopherol triad in abiotic stress responsePhytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae.ScOPT1 and AtOPT4 function as proton-coupled oligopeptide transporters with broad but distinct substrate specificities.Mechanism of heavy metal ion activation of phytochelatin (PC) synthase: blocked thiols are sufficient for PC synthase-catalyzed transpeptidation of glutathione and related thiol peptidesThe biological functions of glutathione revisited in arabidopsis transgenic plants with altered glutathione levelsA new pathway for heavy metal detoxification in animals. Phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegansDetoxification of arsenic by phytochelatins in plantsPhytochelatins are involved in differential arsenate tolerance in Holcus lanatusCharacterization of the phytochelatin synthase of Schistosoma mansoniPhytochelatinsPhytochelatin synthesis is essential for the detoxification of excess zinc and contributes significantly to the accumulation of zinc.Molecular characterization of the homo-phytochelatin synthase of soybean Glycine max: relation to phytochelatin synthase.Arabidopsis thaliana expresses a second functional phytochelatin synthase.The new RENT family of repetitive elements in Nicotiana species harbors gene regulatory elements related to the tCUP cryptic promoter.Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis.Cell-Surface display of heterologous proteins: From high-throughput screening to environmental applications.Kinetic mechanism of glutathione synthetase from Arabidopsis thaliana.Expression of the novel wheat gene TM20 confers enhanced cadmium tolerance to bakers' yeastCentaurin-like protein Cnt5 contributes to arsenic and cadmium resistance in fission yeast.Detoxification of multiple heavy metals by a half-molecule ABC transporter, HMT-1, and coelomocytes of Caenorhabditis elegansARS5 is a component of the 26S proteasome complex, and negatively regulates thiol biosynthesis and arsenic tolerance in ArabidopsisThe N-terminal extension domain of the C. elegans half-molecule ABC transporter, HMT-1, is required for protein-protein interactions and functionHeterologous expression of Ceratophyllum demersum phytochelatin synthase, CdPCS1, in rice leads to lower arsenic accumulation in grainPhytochelatin-metal(loid) transport into vacuoles shows different substrate preferences in barley and ArabidopsisPossible molecular mechanisms involved in nickel, zinc and selenium hyperaccumulation in plants.A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis.Tonoplast-localized Abc2 transporter mediates phytochelatin accumulation in vacuoles and confers cadmium tolerance.Cellular mechanisms for heavy metal detoxification and tolerance.Cadmium tolerance and accumulation in Indian mustard is enhanced by overexpressing gamma-glutamylcysteine synthetase.Structural biology of plant sulfur metabolism: from assimilation to biosynthesis.Tentative identification of the second substrate binding site in Arabidopsis phytochelatin synthaseCloning and characterization of a Phragmites australis phytochelatin synthase (PaPCS) and achieving Cd tolerance in tall fescue.Phytochelatin synthase is required for tolerating metal toxicity in a basidiomycete yeast and is a conserved factor involved in metal homeostasis in fungi.Cadmium-inducible expression of the ABC-type transporter AtABCC3 increases phytochelatin-mediated cadmium tolerance in Arabidopsis.Long-distance root-to-shoot transport of phytochelatins and cadmium in Arabidopsis.Adaptive Engineering of Phytochelatin-based Heavy Metal Tolerance.Weeds, worms, and more. Papain's long-lost cousin, phytochelatin synthase.Enhanced metal tolerance correlates with heterotypic variation in SpMTL, a metallothionein-like protein from the hyperaccumulator Sedum plumbizincicola.Feedback inhibition by thiols outranks glutathione depletion: a luciferase-based screen reveals glutathione-deficient γ-ECS and glutathione synthetase mutants impaired in cadmium-induced sulfate assimilation.Pseudomonas syringae enhances herbivory by suppressing the reactive oxygen burst in Arabidopsis
P2860
Q27027101-97E3E329-3880-4613-B3A9-E342E5089A54Q27931537-E2D0E931-1473-447A-A498-85F9C04D2A60Q27934925-3567095C-26C4-43D6-ACA6-107B2E524571Q28144302-D8EF7E4B-8A6A-4906-84BF-BACC4A99A1BEQ28201457-2BE4FE7B-74B8-467F-9A4A-6F1A9DCA99B9Q28213578-FFB44452-FEB1-46C2-BB3D-D21777280CEFQ28344012-A152908E-BE3E-4694-8C4B-EE21A3DFB08DQ28365127-22F56F85-13BF-4CBE-9366-DA13B83D2CB1Q28478247-63086CD1-DD04-4ECC-90AD-2752DF53A0A8Q29039645-6B608182-D2FC-49FF-B8DC-749CB2CFDA26Q30319230-CA35050D-B9B6-43D8-882A-8CD8D3990A17Q30320891-611969D3-C2AF-4401-B9DA-145F41A0ED3DQ30320902-605A2DEE-8B33-40B4-B43B-740A5B153ABCQ30782651-92BAB075-2762-40D0-9EC9-EB7CDD52B0E7Q31036535-81B42868-1CB2-45F2-B95E-4512A4BE0176Q31107604-78838E02-241B-40E5-A137-8ED6CCED633BQ33205673-D7EE3E30-C872-4D5B-B629-F79E0FDD3BF8Q33328158-38297BF2-8C96-4CD8-8A2E-0DE1E4CFA4FFQ33392297-F5E1B2EC-B609-4BFC-9A9C-1E9AACA653A5Q33539805-07BA5687-5B97-4429-9C00-130C73F038F0Q33697917-FC9AE870-B2AC-4080-BF82-EA3384998D7CQ33707693-0D30081C-0FB4-4A30-9306-6C5D985CBCE3Q33928857-CC333B47-A10C-4C7A-975C-4815275573B0Q34011202-66B0E7C2-C2AA-4CC8-B3D8-78BA9E829A09Q34187890-E316B926-E702-4FD0-A413-1B4ECAB5A956Q34206102-230B2744-A863-4B06-90E4-576C13E4C00BQ34412507-21EA23C9-70AB-4FA4-A1F2-B6CA905F9FA3Q34461884-52032381-78BB-4039-B22F-945EA682FB4BQ34506202-361877BE-1F99-4F8E-8288-BEE9CF9CE77EQ34638385-06B1F858-CC09-4DC6-9FD9-E88141965D9AQ35067860-73E6C0B9-CBF1-4C6B-B622-0637C82F9E25Q35227132-C8E1CA2F-BA7F-4B9C-8444-362B90D9B0A8Q35540508-5E245BB2-2F3E-4D05-A81C-DB3AEB08D3C2Q35759695-7B091247-3CFA-4303-9DBA-24334723DF87Q35812458-4A3F1A16-D4DC-4B9A-9BC8-7FD71757CD7BQ35837156-1131ED6B-809E-4A12-803C-C1AFDC38EB85Q35890913-B90D16DB-C166-41E2-BE6A-ABFE3B5EC4AAQ36268087-F082D7BC-0757-49C5-9F99-CD5D8C7A60B7Q36395859-7DD98B09-37C9-437F-A9AA-37A2B1D02D1AQ36488003-473D9D3C-FB03-40B6-871B-43EE2299E5F4
P2860
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
@ast
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
@en
type
label
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
@ast
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
@en
prefLabel
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
@ast
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
@en
P2093
P2860
P356
P1476
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
@en
P2093
P2860
P304
P356
10.1073/PNAS.96.12.7110
P407
P577
1999-06-01T00:00:00Z