Regulation of inducible peroxide stress responses
Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-s...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Mongkolsuk, Skorn [verfasserIn] Helmann, John D. [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|
| Erschienen: |
Oxford, UK: Blackwell Science Ltd. ; 2002 |
|---|
| Umfang: |
Online-Ressource |
|---|
| Reproduktion: |
2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
|---|---|
| Übergeordnetes Werk: |
In: Molecular microbiology - Oxford [u.a.] : Wiley-Blackwell, 1987, 45(2002), 1, Seite 0 |
| Übergeordnetes Werk: |
volume:45 ; year:2002 ; number:1 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1046/j.1365-2958.2002.03015.x |
|---|
| Katalog-ID: |
NLEJ243557124 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ243557124 | ||
| 003 | DE-627 | ||
| 005 | 20210707182707.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 120427s2002 xx |||||o 00| ||und c | ||
| 024 | 7 | |a 10.1046/j.1365-2958.2002.03015.x |2 doi | |
| 035 | |a (DE-627)NLEJ243557124 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 100 | 1 | |a Mongkolsuk, Skorn |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Regulation of inducible peroxide stress responses |
| 264 | 1 | |a Oxford, UK |b Blackwell Science Ltd. |c 2002 | |
| 300 | |a Online-Ressource | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. | ||
| 533 | |d 2002 |f Blackwell Publishing Journal Backfiles 1879-2005 |7 |2002|||||||||| | ||
| 700 | 1 | |a Helmann, John D. |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i In |t Molecular microbiology |d Oxford [u.a.] : Wiley-Blackwell, 1987 |g 45(2002), 1, Seite 0 |h Online-Ressource |w (DE-627)NLEJ243926537 |w (DE-600)1501537-3 |x 1365-2958 |7 nnns |
| 773 | 1 | 8 | |g volume:45 |g year:2002 |g number:1 |g pages:0 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x |q text/html |x Verlag |z Deutschlandweit zugänglich |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a ZDB-1-DJB | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 45 |j 2002 |e 1 |h 0 | ||
| author_variant |
s m sm j d h jd jdh |
|---|---|
| matchkey_str |
article:13652958:2002----::euainfnuilprxdsr |
| hierarchy_sort_str |
2002 |
| publishDate |
2002 |
| allfields |
10.1046/j.1365-2958.2002.03015.x doi (DE-627)NLEJ243557124 DE-627 ger DE-627 rakwb Mongkolsuk, Skorn verfasserin aut Regulation of inducible peroxide stress responses Oxford, UK Blackwell Science Ltd. 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Helmann, John D. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 45(2002), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:45 year:2002 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 2002 1 0 |
| spelling |
10.1046/j.1365-2958.2002.03015.x doi (DE-627)NLEJ243557124 DE-627 ger DE-627 rakwb Mongkolsuk, Skorn verfasserin aut Regulation of inducible peroxide stress responses Oxford, UK Blackwell Science Ltd. 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Helmann, John D. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 45(2002), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:45 year:2002 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 2002 1 0 |
| allfields_unstemmed |
10.1046/j.1365-2958.2002.03015.x doi (DE-627)NLEJ243557124 DE-627 ger DE-627 rakwb Mongkolsuk, Skorn verfasserin aut Regulation of inducible peroxide stress responses Oxford, UK Blackwell Science Ltd. 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Helmann, John D. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 45(2002), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:45 year:2002 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 2002 1 0 |
| allfieldsGer |
10.1046/j.1365-2958.2002.03015.x doi (DE-627)NLEJ243557124 DE-627 ger DE-627 rakwb Mongkolsuk, Skorn verfasserin aut Regulation of inducible peroxide stress responses Oxford, UK Blackwell Science Ltd. 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Helmann, John D. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 45(2002), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:45 year:2002 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 2002 1 0 |
| allfieldsSound |
10.1046/j.1365-2958.2002.03015.x doi (DE-627)NLEJ243557124 DE-627 ger DE-627 rakwb Mongkolsuk, Skorn verfasserin aut Regulation of inducible peroxide stress responses Oxford, UK Blackwell Science Ltd. 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Helmann, John D. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 45(2002), 1, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:45 year:2002 number:1 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 45 2002 1 0 |
| source |
In Molecular microbiology 45(2002), 1, Seite 0 volume:45 year:2002 number:1 pages:0 |
| sourceStr |
In Molecular microbiology 45(2002), 1, Seite 0 volume:45 year:2002 number:1 pages:0 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Molecular microbiology |
| authorswithroles_txt_mv |
Mongkolsuk, Skorn @@aut@@ Helmann, John D. @@aut@@ |
| publishDateDaySort_date |
2002-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ243926537 |
| id |
NLEJ243557124 |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ243557124</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707182707.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2002 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1365-2958.2002.03015.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243557124</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Mongkolsuk, Skorn</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Regulation of inducible peroxide stress responses</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Science Ltd.</subfield><subfield code="c">2002</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2002</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2002||||||||||</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Helmann, John D.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Molecular microbiology</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1987</subfield><subfield code="g">45(2002), 1, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243926537</subfield><subfield code="w">(DE-600)1501537-3</subfield><subfield code="x">1365-2958</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:45</subfield><subfield code="g">year:2002</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">45</subfield><subfield code="j">2002</subfield><subfield code="e">1</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| series2 |
Blackwell Publishing Journal Backfiles 1879-2005 |
| author |
Mongkolsuk, Skorn |
| spellingShingle |
Mongkolsuk, Skorn Regulation of inducible peroxide stress responses |
| authorStr |
Mongkolsuk, Skorn |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ243926537 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| author_role |
aut aut |
| collection |
NL |
| publishPlace |
Oxford, UK |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
1365-2958 |
| topic_title |
Regulation of inducible peroxide stress responses |
| publisher |
Blackwell Science Ltd. |
| publisherStr |
Blackwell Science Ltd. |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| hierarchy_parent_title |
Molecular microbiology |
| hierarchy_parent_id |
NLEJ243926537 |
| hierarchy_top_title |
Molecular microbiology |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ243926537 (DE-600)1501537-3 |
| title |
Regulation of inducible peroxide stress responses |
| ctrlnum |
(DE-627)NLEJ243557124 |
| title_full |
Regulation of inducible peroxide stress responses |
| author_sort |
Mongkolsuk, Skorn |
| journal |
Molecular microbiology |
| journalStr |
Molecular microbiology |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
2002 |
| contenttype_str_mv |
zzz |
| container_start_page |
0 |
| author_browse |
Mongkolsuk, Skorn Helmann, John D. |
| container_volume |
45 |
| physical |
Online-Ressource |
| format_se |
Elektronische Aufsätze |
| author-letter |
Mongkolsuk, Skorn |
| doi_str_mv |
10.1046/j.1365-2958.2002.03015.x |
| author2-role |
verfasserin |
| title_sort |
regulation of inducible peroxide stress responses |
| title_auth |
Regulation of inducible peroxide stress responses |
| abstract |
Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. |
| abstractGer |
Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. |
| abstract_unstemmed |
Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative. |
| collection_details |
GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE |
| container_issue |
1 |
| title_short |
Regulation of inducible peroxide stress responses |
| url |
http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x |
| remote_bool |
true |
| author2 |
Helmann, John D. |
| author2Str |
Helmann, John D. |
| ppnlink |
NLEJ243926537 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| doi_str |
10.1046/j.1365-2958.2002.03015.x |
| up_date |
2024-07-06T05:49:56.860Z |
| _version_ |
1803807617829568512 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ243557124</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707182707.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">120427s2002 xx |||||o 00| ||und c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1046/j.1365-2958.2002.03015.x</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ243557124</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Mongkolsuk, Skorn</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Regulation of inducible peroxide stress responses</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Science Ltd.</subfield><subfield code="c">2002</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Bacteria adapt to the presence of reactive oxygen species (ROS) by increasing the expression of detoxification enzymes and protein and DNA repair functions. These responses are co-ordinated by transcription factors that regulate target genes in response to ROS. We compare three classes of peroxide-sensing regulators: OxyR, PerR and OhrR. In all three cases, peroxides effect changes in the redox status of cysteine residues, but the molecular details are distinct. OxyR is converted into a transcriptional activator by the formation of a disulphide bond between two reactive cysteine residues. PerR is a metalloprotein that functions as a peroxide- sensitive repressor. Oxidation is modulated by metal ion composition and may also involve disulphide bond formation. OhrR represses an organic peroxide resistance protein and mediates derepression in response to organic peroxides. Peroxide sensing in this system requires a single conserved cysteine, which is oxidized to form a cysteine–sulphenic acid derivative.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="d">2002</subfield><subfield code="f">Blackwell Publishing Journal Backfiles 1879-2005</subfield><subfield code="7">|2002||||||||||</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Helmann, John D.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">In</subfield><subfield code="t">Molecular microbiology</subfield><subfield code="d">Oxford [u.a.] : Wiley-Blackwell, 1987</subfield><subfield code="g">45(2002), 1, Seite 0</subfield><subfield code="h">Online-Ressource</subfield><subfield code="w">(DE-627)NLEJ243926537</subfield><subfield code="w">(DE-600)1501537-3</subfield><subfield code="x">1365-2958</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:45</subfield><subfield code="g">year:2002</subfield><subfield code="g">number:1</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1046/j.1365-2958.2002.03015.x</subfield><subfield code="q">text/html</subfield><subfield code="x">Verlag</subfield><subfield code="z">Deutschlandweit zugänglich</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-DJB</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">45</subfield><subfield code="j">2002</subfield><subfield code="e">1</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| score |
7.399823 |