schliessen

Filtern

 

Bibliotheken

Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology

Since their discovery as a substrate for ribonucleotide reductase (RNR), the role of thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory function. Both proteins act by changing the structure and activity of a broad spectrum of target proteins, typically by mod... Full description

Journal Title: Annual Review of Genetics 2009-12-01, Vol.43 (1), p.335-367
Main Author: Meyer, Yves
Other Authors: Buchanan, Bob B , Vignols, Florence , Reichheld, Jean-Philippe
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: Alma/SFX Local Collection
Publisher: United States: Annual Reviews
ID: ISSN: 0066-4197
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: cdi_hal_primary_oai_HAL_hal_00685724v1
title: Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology
format: Article
creator:
  • Meyer, Yves
  • Buchanan, Bob B
  • Vignols, Florence
  • Reichheld, Jean-Philippe
subjects:
  • Analysis
  • animal structures
  • Animals
  • Biochemistry
  • Biochemistry, Molecular Biology
  • Biodiversity
  • Bioinformatics
  • Biology
  • Biomolecules
  • Cells
  • Cellular Biology
  • Computer Science
  • Enzymes
  • Escherichia coli
  • Escherichia coli - enzymology
  • Evolution
  • Gene mutations
  • Genetics
  • Genomics
  • Glutaredoxins
  • Glutaredoxins - metabolism
  • Glutathione
  • Humans
  • Life Sciences
  • light regulation
  • Mammals
  • Mammals - metabolism
  • Molecular Biology
  • Molecular Networks
  • Oxidation
  • Oxidation-Reduction
  • Oxidative stress
  • Phylogenetics
  • Plant breeding
  • Plants genetics
  • Populations
  • Populations and Evolution
  • Quantitative Methods
  • redox regulation
  • redox-linked mutants
  • redoxins
  • Reduction
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae - enzymology
  • Systematics
  • Systematics, Phylogenetics and taxonomy
  • taxonomy
  • Thioredoxin
  • Thioredoxins
  • Thioredoxins - metabolism
  • Vegetal Biology
ispartof: Annual Review of Genetics, 2009-12-01, Vol.43 (1), p.335-367
description: Since their discovery as a substrate for ribonucleotide reductase (RNR), the role of thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory function. Both proteins act by changing the structure and activity of a broad spectrum of target proteins, typically by modifying redox status. Trx and Grx are members of families with multiple and partially redundant genes. The number of genes clearly increased with the appearance of multicellular organisms, in part because of new types of Trx and Grx with orthologs throughout the animal and plant kingdoms. The function of Trx and Grx also broadened as cells achieved increased complexity, especially in the regulation arena. In view of these progressive changes, the ubiquitous distribution of Trx and the wide occurrence of Grx enable these proteins to serve as indicators of the evolutionary history of redox regulation. In so doing, they add a unifying element that links the diverse forms of life to one another in an uninterrupted continuum. It is anticipated that future research will embellish this continuum and further elucidate the properties of these proteins and their impact on biology. The new information will be important not only to our understanding of the role of Trx and Grx in fundamental cell processes but also to future societal benefits as the proteins find new applications in a range of fields.
language: eng
source: Alma/SFX Local Collection
identifier: ISSN: 0066-4197
fulltext: fulltext
issn:
  • 0066-4197
  • 1545-2948
url: Link


@attributes
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
RANK2.6895103
LOCALfalse
PrimoNMBib
record
control
sourceidgale_proqu
recordidTN_cdi_hal_primary_oai_HAL_hal_00685724v1
sourceformatXML
sourcesystemPC
galeidA246463356
sourcerecordidA246463356
originalsourceidFETCH-LOGICAL-a5817-d601af9f9f3f399c6ff816f910b793726f70b79b5204b7f2913c3e998375856e3
addsrcrecordideNqVkltv1DAQRiMEokvhL6CIPiAeUsaX-AIvbKvSIq1AQu2z5U3GW1dZe8mlZf89DlkurRAU-SHR5MyxPfmy7IDAISFcvLYhDC1eFysM2BcEKAFVEMYpkAfZjJS8LKjm6mE2AxCi4ETLvexJ110BAJe0fJztES004VTNsqPzSx9brONXH7rchjo_bYbe_qi8yS-Cd1sfVvlJg2sMfZf7kH8eP-dHPjZxtX2aPXK26fDZ7rmfXbw_OT8-KxafTj8czxeFLRWRRS2AWKfTYo5pXQnnFBFOE1hKzSQVTo5vy5ICX0pHNWEVQ60Vk6UqBbL97OPkjRsM1rdoNq1f23ZrovWmTsMwNdbDxtw4A0AMLh3UAFqCqJJLO66wwiWjlXVQ1mUSvpqEl7a55TqbL8xYS_NTpaT8miT25cRu2vhlwK43a99V2DQ2YBw6o0BSDelC_yQl44RzBSP54g55FYc2pBma9C-hJIKyBB1M0Mo2aHxwsW9tNSrNnHLBBWOl-DtFBOeSq9F1-AcqrRrXvooBnU_1W9r7Nfy2w9upoWpj17Xofs6VgBnTa3bpNd_Ta6b0mim9qfv5biDDco31r95dXBMwv6OvfG97H0M6l2_uucm7yTFCtkmYx5vuv875DfBDFIw
sourcetypeOpen Access Repository
isCDItrue
recordtypearticle
pqid201051623
display
typearticle
titleThioredoxins and Glutaredoxins: Unifying Elements in Redox Biology
sourceAlma/SFX Local Collection
creatorMeyer, Yves ; Buchanan, Bob B ; Vignols, Florence ; Reichheld, Jean-Philippe
creatorcontribMeyer, Yves ; Buchanan, Bob B ; Vignols, Florence ; Reichheld, Jean-Philippe
descriptionSince their discovery as a substrate for ribonucleotide reductase (RNR), the role of thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory function. Both proteins act by changing the structure and activity of a broad spectrum of target proteins, typically by modifying redox status. Trx and Grx are members of families with multiple and partially redundant genes. The number of genes clearly increased with the appearance of multicellular organisms, in part because of new types of Trx and Grx with orthologs throughout the animal and plant kingdoms. The function of Trx and Grx also broadened as cells achieved increased complexity, especially in the regulation arena. In view of these progressive changes, the ubiquitous distribution of Trx and the wide occurrence of Grx enable these proteins to serve as indicators of the evolutionary history of redox regulation. In so doing, they add a unifying element that links the diverse forms of life to one another in an uninterrupted continuum. It is anticipated that future research will embellish this continuum and further elucidate the properties of these proteins and their impact on biology. The new information will be important not only to our understanding of the role of Trx and Grx in fundamental cell processes but also to future societal benefits as the proteins find new applications in a range of fields.
identifier
0ISSN: 0066-4197
1EISSN: 1545-2948
2DOI: 10.1146/annurev-genet-102108-134201
3PMID: 19691428
languageeng
publisherUnited States: Annual Reviews
subjectAnalysis ; animal structures ; Animals ; Biochemistry ; Biochemistry, Molecular Biology ; Biodiversity ; Bioinformatics ; Biology ; Biomolecules ; Cells ; Cellular Biology ; Computer Science ; Enzymes ; Escherichia coli ; Escherichia coli - enzymology ; Evolution ; Gene mutations ; Genetics ; Genomics ; Glutaredoxins ; Glutaredoxins - metabolism ; Glutathione ; Humans ; Life Sciences ; light regulation ; Mammals ; Mammals - metabolism ; Molecular Biology ; Molecular Networks ; Oxidation ; Oxidation-Reduction ; Oxidative stress ; Phylogenetics ; Plant breeding ; Plants genetics ; Populations ; Populations and Evolution ; Quantitative Methods ; redox regulation ; redox-linked mutants ; redoxins ; Reduction ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Systematics ; Systematics, Phylogenetics and taxonomy ; taxonomy ; Thioredoxin ; Thioredoxins ; Thioredoxins - metabolism ; Vegetal Biology
ispartofAnnual Review of Genetics, 2009-12-01, Vol.43 (1), p.335-367
rights
0Copyright © 2009 by Annual Reviews. All rights reserved 2009
1Copyright Annual Reviews, Inc. 2009
2Distributed under a Creative Commons Attribution 4.0 International License
lds50peer_reviewed
oafree_for_read
citedbyFETCH-LOGICAL-a5817-d601af9f9f3f399c6ff816f910b793726f70b79b5204b7f2913c3e998375856e3
citesFETCH-LOGICAL-a5817-d601af9f9f3f399c6ff816f910b793726f70b79b5204b7f2913c3e998375856e3
orcidid0000-0002-2031-0407
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
thumbnail$$Usyndetics_thumb_exl
backlink
0$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19691428$$D View this record in MEDLINE/PubMed
1$$Uhttps://hal.archives-ouvertes.fr/hal-00685724$$DView record in HAL
search
creatorcontrib
0Meyer, Yves
1Buchanan, Bob B
2Vignols, Florence
3Reichheld, Jean-Philippe
title
0Thioredoxins and Glutaredoxins: Unifying Elements in Redox Biology
1Annual Review of Genetics
addtitleAnnu Rev Genet
descriptionSince their discovery as a substrate for ribonucleotide reductase (RNR), the role of thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory function. Both proteins act by changing the structure and activity of a broad spectrum of target proteins, typically by modifying redox status. Trx and Grx are members of families with multiple and partially redundant genes. The number of genes clearly increased with the appearance of multicellular organisms, in part because of new types of Trx and Grx with orthologs throughout the animal and plant kingdoms. The function of Trx and Grx also broadened as cells achieved increased complexity, especially in the regulation arena. In view of these progressive changes, the ubiquitous distribution of Trx and the wide occurrence of Grx enable these proteins to serve as indicators of the evolutionary history of redox regulation. In so doing, they add a unifying element that links the diverse forms of life to one another in an uninterrupted continuum. It is anticipated that future research will embellish this continuum and further elucidate the properties of these proteins and their impact on biology. The new information will be important not only to our understanding of the role of Trx and Grx in fundamental cell processes but also to future societal benefits as the proteins find new applications in a range of fields.
subject
0Analysis
1animal structures
2Animals
3Biochemistry
4Biochemistry, Molecular Biology
5Biodiversity
6Bioinformatics
7Biology
8Biomolecules
9Cells
10Cellular Biology
11Computer Science
12Enzymes
13Escherichia coli
14Escherichia coli - enzymology
15Evolution
16Gene mutations
17Genetics
18Genomics
19Glutaredoxins
20Glutaredoxins - metabolism
21Glutathione
22Humans
23Life Sciences
24light regulation
25Mammals
26Mammals - metabolism
27Molecular Biology
28Molecular Networks
29Oxidation
30Oxidation-Reduction
31Oxidative stress
32Phylogenetics
33Plant breeding
34Plants genetics
35Populations
36Populations and Evolution
37Quantitative Methods
38redox regulation
39redox-linked mutants
40redoxins
41Reduction
42Saccharomyces cerevisiae
43Saccharomyces cerevisiae - enzymology
44Systematics
45Systematics, Phylogenetics and taxonomy
46taxonomy
47Thioredoxin
48Thioredoxins
49Thioredoxins - metabolism
50Vegetal Biology
issn
00066-4197
11545-2948
fulltexttrue
rsrctypearticle
creationdate2009
recordtypearticle
recordideNqVkltv1DAQRiMEokvhL6CIPiAeUsaX-AIvbKvSIq1AQu2z5U3GW1dZe8mlZf89DlkurRAU-SHR5MyxPfmy7IDAISFcvLYhDC1eFysM2BcEKAFVEMYpkAfZjJS8LKjm6mE2AxCi4ETLvexJ110BAJe0fJztES004VTNsqPzSx9brONXH7rchjo_bYbe_qi8yS-Cd1sfVvlJg2sMfZf7kH8eP-dHPjZxtX2aPXK26fDZ7rmfXbw_OT8-KxafTj8czxeFLRWRRS2AWKfTYo5pXQnnFBFOE1hKzSQVTo5vy5ICX0pHNWEVQ60Vk6UqBbL97OPkjRsM1rdoNq1f23ZrovWmTsMwNdbDxtw4A0AMLh3UAFqCqJJLO66wwiWjlXVQ1mUSvpqEl7a55TqbL8xYS_NTpaT8miT25cRu2vhlwK43a99V2DQ2YBw6o0BSDelC_yQl44RzBSP54g55FYc2pBma9C-hJIKyBB1M0Mo2aHxwsW9tNSrNnHLBBWOl-DtFBOeSq9F1-AcqrRrXvooBnU_1W9r7Nfy2w9upoWpj17Xofs6VgBnTa3bpNd_Ta6b0mim9qfv5biDDco31r95dXBMwv6OvfG97H0M6l2_uucm7yTFCtkmYx5vuv875DfBDFIw
startdate20091201
enddate20091201
creator
0Meyer, Yves
1Buchanan, Bob B
2Vignols, Florence
3Reichheld, Jean-Philippe
general
0Annual Reviews
1Annual Reviews, Inc
scope
0CGR
1CUY
2CVF
3ECM
4EIF
5NPM
6AAYXX
7CITATION
8BSHEE
97QG
107QL
117QP
127QR
137SN
147SS
157TK
167TM
178FD
18C1K
19FR3
20K9.
21P64
22RC3
237X8
241XC
25BOBZL
26CLFQK
orcididhttps://orcid.org/0000-0002-2031-0407
sort
creationdate20091201
titleThioredoxins and Glutaredoxins: Unifying Elements in Redox Biology
authorMeyer, Yves ; Buchanan, Bob B ; Vignols, Florence ; Reichheld, Jean-Philippe
facets
frbrtype5
frbrgroupidcdi_FETCH-LOGICAL-a5817-d601af9f9f3f399c6ff816f910b793726f70b79b5204b7f2913c3e998375856e3
rsrctypearticles
prefilterarticles
languageeng
creationdate2009
topic
0Analysis
1animal structures
2Animals
3Biochemistry
4Biochemistry, Molecular Biology
5Biodiversity
6Bioinformatics
7Biology
8Biomolecules
9Cells
10Cellular Biology
11Computer Science
12Enzymes
13Escherichia coli
14Escherichia coli - enzymology
15Evolution
16Gene mutations
17Genetics
18Genomics
19Glutaredoxins
20Glutaredoxins - metabolism
21Glutathione
22Humans
23Life Sciences
24light regulation
25Mammals
26Mammals - metabolism
27Molecular Biology
28Molecular Networks
29Oxidation
30Oxidation-Reduction
31Oxidative stress
32Phylogenetics
33Plant breeding
34Plants genetics
35Populations
36Populations and Evolution
37Quantitative Methods
38redox regulation
39redox-linked mutants
40redoxins
41Reduction
42Saccharomyces cerevisiae
43Saccharomyces cerevisiae - enzymology
44Systematics
45Systematics, Phylogenetics and taxonomy
46taxonomy
47Thioredoxin
48Thioredoxins
49Thioredoxins - metabolism
50Vegetal Biology
toplevel
0peer_reviewed
1online_resources
creatorcontrib
0Meyer, Yves
1Buchanan, Bob B
2Vignols, Florence
3Reichheld, Jean-Philippe
collection
0Medline
1MEDLINE
2MEDLINE (Ovid)
3MEDLINE
4MEDLINE
5PubMed
6CrossRef
7Academic OneFile (A&I only)
8Animal Behavior Abstracts
9Bacteriology Abstracts (Microbiology B)
10Calcium & Calcified Tissue Abstracts
11Chemoreception Abstracts
12Ecology Abstracts
13Entomology Abstracts (Full archive)
14Neurosciences Abstracts
15Nucleic Acids Abstracts
16Technology Research Database
17Environmental Sciences and Pollution Management
18Engineering Research Database
19ProQuest Health & Medical Complete (Alumni)
20Biotechnology and BioEngineering Abstracts
21Genetics Abstracts
22MEDLINE - Academic
23Hyper Article en Ligne (HAL)
24OpenAIRE (Open Access)
25OpenAIRE
jtitleAnnual Review of Genetics
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
au
0Meyer, Yves
1Buchanan, Bob B
2Vignols, Florence
3Reichheld, Jean-Philippe
formatjournal
genrearticle
ristypeJOUR
atitleThioredoxins and Glutaredoxins: Unifying Elements in Redox Biology
jtitleAnnual Review of Genetics
addtitleAnnu Rev Genet
date2009-12-01
risdate2009
volume43
issue1
spage335
epage367
pages335-367
issn0066-4197
eissn1545-2948
abstractSince their discovery as a substrate for ribonucleotide reductase (RNR), the role of thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory function. Both proteins act by changing the structure and activity of a broad spectrum of target proteins, typically by modifying redox status. Trx and Grx are members of families with multiple and partially redundant genes. The number of genes clearly increased with the appearance of multicellular organisms, in part because of new types of Trx and Grx with orthologs throughout the animal and plant kingdoms. The function of Trx and Grx also broadened as cells achieved increased complexity, especially in the regulation arena. In view of these progressive changes, the ubiquitous distribution of Trx and the wide occurrence of Grx enable these proteins to serve as indicators of the evolutionary history of redox regulation. In so doing, they add a unifying element that links the diverse forms of life to one another in an uninterrupted continuum. It is anticipated that future research will embellish this continuum and further elucidate the properties of these proteins and their impact on biology. The new information will be important not only to our understanding of the role of Trx and Grx in fundamental cell processes but also to future societal benefits as the proteins find new applications in a range of fields.
copUnited States
pubAnnual Reviews
pmid19691428
doi10.1146/annurev-genet-102108-134201
orcididhttps://orcid.org/0000-0002-2031-0407
oafree_for_read