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Weeds, worms, and more. Papain's long-lost cousin, phytochelatin synthase.
scientific article published in September 2004
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scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
review article
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Europe PubMed Central
title
Weeds, worms, and more. Papain's long-lost cousin, phytochelatin synthase
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
author
Daniel J. Rigden
series ordinal
3
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
author name string
Philip A Rea
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
Olena K Vatamaniuk
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
language of work or name
English
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publication date
1 September 2004
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
number of pages
12
1 reference
based on heuristic
inferred from page(s)
published in
Plant Physiology
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
volume
136
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
issue
1
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
page(s)
2463-2474
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
cites work
Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase).
1 reference
stated in
PubMed Central
reference URL
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Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite acylation with gamma-glutamylcysteine during catalysis: stoichiometric and site-directed mutagenic analysis of arabidopsis thaliana PCS1-catalyzed phytochelatin synthesis
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PubMed Central
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Characterization of phytochelatin synthase-like protein encoded by alr0975 from a prokaryote, Nostoc sp. PCC 7120.
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PubMed Central
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24 September 2018
Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis
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Localization and functional characterization of metal-binding sites in phytochelatin synthases
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Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates
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Worms take the 'phyto' out of 'phytochelatins'.
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PubMed Central
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Molecular characterization of the homo-phytochelatin synthase of soybean Glycine max: relation to phytochelatin synthase
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Metal-binding properties of phytochelatin-related peptides
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Molecular mechanisms of plant metal tolerance and homeostasis
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Phylogenetic relationships within cation transporter families of Arabidopsis
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24 September 2018
Caenorhabditis elegans expresses a functional phytochelatin synthase.
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A new pathway for heavy metal detoxification in animals. Phytochelatin synthase is required for cadmium tolerance in Caenorhabditis elegans
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Phytochelatins and their roles in heavy metal detoxification
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Mechanism of heavy metal ion activation of phytochelatin (PC) synthase: blocked thiols are sufficient for PC synthase-catalyzed transpeptidation of glutathione and related thiol peptides
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Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain
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Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter
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Serine Proteases: Structure and Mechanism of Catalysis
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Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occurring Cys-His-Asp triad
1 reference
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reference URL
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based on heuristic
inferred from PubMed ID database lookup
Cadmium-sensitive, cad1 mutants of Arabidopsis thaliana are phytochelatin deficient
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/15375203
retrieved
12 December 2020
based on heuristic
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Identifiers
DOI
10.1104/PP.104.048579
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
PMCID
523314
0 references
PubMed ID
15375203
1 reference
stated in
Europe PubMed Central
PubMed ID
15375203
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15375203%20AND%20SRC:MED&resulttype=core&format=json
retrieved
1 January 2020
ResearchGate publication ID
8339695
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