Proteins associated with cork formation in Quercus suber L. stem tissues
Identifieur interne : 000036 ( PascalFrancis/Corpus ); précédent : 000035; suivant : 000037Proteins associated with cork formation in Quercus suber L. stem tissues
Auteurs : Cândido P. P. Ricardo ; Isabel Martins ; Rita Francisco ; Kjell Sergeant ; Carla Pinheiro ; Alexandre Campos ; Jenny Renaut ; Pedro FevereiroSource :
- Journal of proteomics : (Print) [ 1874-3919 ] ; 2011.
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Abstract
Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation.
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Format Inist (serveur)
| NO : | PASCAL 11-0407790 INIST |
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| ET : | Proteins associated with cork formation in Quercus suber L. stem tissues |
| AU : | RICARDO (Cândido P. P.); MARTINS (Isabel); FRANCISCO (Rita); SERGEANT (Kjell); PINHEIRO (Carla); CAMPOS (Alexandre); RENAUT (Jenny); FEVEREIRO (Pedro); RENAUT (Jenny); SVENSSON (Birte); JORRIN-NOVO (Jesus); PANIS (Bart) |
| AF : | Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN/2780-157 Oeiras/Portugal (1 aut., 2 aut., 3 aut., 5 aut., 6 aut., 8 aut.); Instituto Superior de Agronomia, Universidade Técnica de Lisboa, Tapada da Ajuda/1349-017 Lisboa/Portugal (1 aut.); Centre de Recherche Public-Gabriel Lippmann, Department Environment and Agrobiotechnologies, 41, rue du Brill/4422 Belvaux/Luxembourg (4 aut., 7 aut.); Faculdade de Ciencias, Universidade de Lisboa, Campo Grande/1749-016 Lisboa/Portugal (8 aut.); Laboratory of Tropical Crop Improvement, Department of Biosystems, K. U. Leuven, Kasteelpark Arenberg 13/3001 Heverlee/Belgique (4 aut.) |
| DT : | Publication en série; Niveau analytique |
| SO : | Journal of proteomics : (Print); ISSN 1874-3919; Royaume-Uni; Da. 2011; Vol. 74; No. 8; Pp. 1266-1278; Bibl. 66 ref. |
| LA : | Anglais |
| EA : | Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation. |
| CC : | 002A04B |
| FD : | Protéine; Quercus suber; Tissu; Protéomique |
| FG : | Fagaceae; Dicotyledones; Angiospermae; Spermatophyta |
| ED : | Protein; Quercus suber; Tissue; Proteomics |
| EG : | Fagaceae; Dicotyledones; Angiospermae; Spermatophyta |
| SD : | Proteína; Quercus suber; Tejido; Proteómica |
| LO : | INIST-18007.354000191153520090 |
| ID : | 11-0407790 |
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Pascal:11-0407790Le document en format XML
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P." last="Ricardo">Cândido P. P. Ricardo</name><affiliation><inist:fA14 i1="01"><s1>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN</s1><s2>2780-157 Oeiras</s2><s3>PRT</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14></affiliation><affiliation><inist:fA14 i1="02"><s1>Instituto Superior de Agronomia, Universidade Técnica de Lisboa, Tapada da Ajuda</s1><s2>1349-017 Lisboa</s2><s3>PRT</s3><sZ>1 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Martins, Isabel" sort="Martins, Isabel" uniqKey="Martins I" first="Isabel" last="Martins">Isabel Martins</name><affiliation><inist:fA14 i1="01"><s1>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN</s1><s2>2780-157 Oeiras</s2><s3>PRT</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Francisco, Rita" sort="Francisco, Rita" uniqKey="Francisco R" first="Rita" last="Francisco">Rita Francisco</name><affiliation><inist:fA14 i1="01"><s1>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN</s1><s2>2780-157 Oeiras</s2><s3>PRT</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Sergeant, Kjell" sort="Sergeant, Kjell" uniqKey="Sergeant K" first="Kjell" last="Sergeant">Kjell Sergeant</name><affiliation><inist:fA14 i1="03"><s1>Centre de Recherche Public-Gabriel Lippmann, Department Environment and Agrobiotechnologies, 41, rue du Brill</s1><s2>4422 Belvaux</s2><s3>LUX</s3><sZ>4 aut.</sZ><sZ>7 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Pinheiro, Carla" sort="Pinheiro, Carla" uniqKey="Pinheiro C" first="Carla" last="Pinheiro">Carla Pinheiro</name><affiliation><inist:fA14 i1="01"><s1>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN</s1><s2>2780-157 Oeiras</s2><s3>PRT</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Campos, Alexandre" sort="Campos, Alexandre" uniqKey="Campos A" first="Alexandre" last="Campos">Alexandre Campos</name><affiliation><inist:fA14 i1="01"><s1>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN</s1><s2>2780-157 Oeiras</s2><s3>PRT</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Renaut, Jenny" sort="Renaut, Jenny" uniqKey="Renaut J" first="Jenny" last="Renaut">Jenny Renaut</name><affiliation><inist:fA14 i1="03"><s1>Centre de Recherche Public-Gabriel Lippmann, Department Environment and Agrobiotechnologies, 41, rue du Brill</s1><s2>4422 Belvaux</s2><s3>LUX</s3><sZ>4 aut.</sZ><sZ>7 aut.</sZ></inist:fA14></affiliation></author><author><name sortKey="Fevereiro, Pedro" sort="Fevereiro, Pedro" uniqKey="Fevereiro P" first="Pedro" last="Fevereiro">Pedro Fevereiro</name><affiliation><inist:fA14 i1="01"><s1>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN</s1><s2>2780-157 Oeiras</s2><s3>PRT</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></inist:fA14></affiliation><affiliation><inist:fA14 i1="04"><s1>Faculdade de Ciencias, Universidade de Lisboa, Campo Grande</s1><s2>1749-016 Lisboa</s2><s3>PRT</s3><sZ>8 aut.</sZ></inist:fA14></affiliation></author></analytic><series><title level="j" type="main">Journal of proteomics : (Print)</title><idno type="ISSN">1874-3919</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of proteomics : (Print)</title><idno type="ISSN">1874-3919</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Protein</term><term>Proteomics</term><term>Quercus suber</term><term>Tissue</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Protéine</term><term>Quercus suber</term><term>Tissu</term><term>Protéomique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation.</div></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>1874-3919</s0></fA01><fA05><s2>74</s2></fA05><fA06><s2>8</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Proteins associated with cork formation in Quercus suber L. stem tissues</s1></fA08><fA09 i1="01" i2="1" l="ENG"><s1>Plant Proteomics in Europe</s1></fA09><fA11 i1="01" i2="1"><s1>RICARDO (Cândido P. P.)</s1></fA11><fA11 i1="02" i2="1"><s1>MARTINS (Isabel)</s1></fA11><fA11 i1="03" i2="1"><s1>FRANCISCO (Rita)</s1></fA11><fA11 i1="04" i2="1"><s1>SERGEANT (Kjell)</s1></fA11><fA11 i1="05" i2="1"><s1>PINHEIRO (Carla)</s1></fA11><fA11 i1="06" i2="1"><s1>CAMPOS (Alexandre)</s1></fA11><fA11 i1="07" i2="1"><s1>RENAUT (Jenny)</s1></fA11><fA11 i1="08" i2="1"><s1>FEVEREIRO (Pedro)</s1></fA11><fA12 i1="01" i2="1"><s1>RENAUT (Jenny)</s1><s9>ed.</s9></fA12><fA12 i1="02" i2="1"><s1>SVENSSON (Birte)</s1><s9>ed.</s9></fA12><fA12 i1="03" i2="1"><s1>JORRIN-NOVO (Jesus)</s1><s9>ed.</s9></fA12><fA12 i1="04" i2="1"><s1>PANIS (Bart)</s1><s9>ed.</s9></fA12><fA14 i1="01"><s1>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN</s1><s2>2780-157 Oeiras</s2><s3>PRT</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>8 aut.</sZ></fA14><fA14 i1="02"><s1>Instituto Superior de Agronomia, Universidade Técnica de Lisboa, Tapada da Ajuda</s1><s2>1349-017 Lisboa</s2><s3>PRT</s3><sZ>1 aut.</sZ></fA14><fA14 i1="03"><s1>Centre de Recherche Public-Gabriel Lippmann, Department Environment and Agrobiotechnologies, 41, rue du Brill</s1><s2>4422 Belvaux</s2><s3>LUX</s3><sZ>4 aut.</sZ><sZ>7 aut.</sZ></fA14><fA14 i1="04"><s1>Faculdade de Ciencias, Universidade de Lisboa, Campo Grande</s1><s2>1749-016 Lisboa</s2><s3>PRT</s3><sZ>8 aut.</sZ></fA14><fA15 i1="01"><s1>Laboratory of Tropical Crop Improvement, Department of Biosystems, K. U. Leuven, Kasteelpark Arenberg 13</s1><s2>3001 Heverlee</s2><s3>BEL</s3><sZ>4 aut.</sZ></fA15><fA20><s1>1266-1278</s1></fA20><fA21><s1>2011</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>18007</s2><s5>354000191153520090</s5></fA43><fA44><s0>0000</s0><s1>© 2011 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>66 ref.</s0></fA45><fA47 i1="01" i2="1"><s0>11-0407790</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Journal of proteomics : (Print)</s0></fA64><fA66 i1="01"><s0>GBR</s0></fA66><fC01 i1="01" l="ENG"><s0>Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation.</s0></fC01><fC02 i1="01" i2="X"><s0>002A04B</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Protéine</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Protein</s0><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Proteína</s0><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Quercus suber</s0><s2>NS</s2><s5>02</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Quercus suber</s0><s2>NS</s2><s5>02</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Quercus suber</s0><s2>NS</s2><s5>02</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Tissu</s0><s5>03</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Tissue</s0><s5>03</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Tejido</s0><s5>03</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Protéomique</s0><s5>04</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Proteomics</s0><s5>04</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Proteómica</s0><s5>04</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Fagaceae</s0><s2>NS</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Fagaceae</s0><s2>NS</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Fagaceae</s0><s2>NS</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Dicotyledones</s0><s2>NS</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Dicotyledones</s0><s2>NS</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Dicotyledones</s0><s2>NS</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Angiospermae</s0><s2>NS</s2></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Angiospermae</s0><s2>NS</s2></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Angiospermae</s0><s2>NS</s2></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Spermatophyta</s0><s2>NS</s2></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Spermatophyta</s0><s2>NS</s2></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Spermatophyta</s0><s2>NS</s2></fC07><fN21><s1>283</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard><server><NO>PASCAL 11-0407790 INIST</NO><ET>Proteins associated with cork formation in Quercus suber L. stem tissues</ET><AU>RICARDO (Cândido P. P.); MARTINS (Isabel); FRANCISCO (Rita); SERGEANT (Kjell); PINHEIRO (Carla); CAMPOS (Alexandre); RENAUT (Jenny); FEVEREIRO (Pedro); RENAUT (Jenny); SVENSSON (Birte); JORRIN-NOVO (Jesus); PANIS (Bart)</AU><AF>Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN/2780-157 Oeiras/Portugal (1 aut., 2 aut., 3 aut., 5 aut., 6 aut., 8 aut.); Instituto Superior de Agronomia, Universidade Técnica de Lisboa, Tapada da Ajuda/1349-017 Lisboa/Portugal (1 aut.); Centre de Recherche Public-Gabriel Lippmann, Department Environment and Agrobiotechnologies, 41, rue du Brill/4422 Belvaux/Luxembourg (4 aut., 7 aut.); Faculdade de Ciencias, Universidade de Lisboa, Campo Grande/1749-016 Lisboa/Portugal (8 aut.); Laboratory of Tropical Crop Improvement, Department of Biosystems, K. U. Leuven, Kasteelpark Arenberg 13/3001 Heverlee/Belgique (4 aut.)</AF><DT>Publication en série; Niveau analytique</DT><SO>Journal of proteomics : (Print); ISSN 1874-3919; Royaume-Uni; Da. 2011; Vol. 74; No. 8; Pp. 1266-1278; Bibl. 66 ref.</SO><LA>Anglais</LA><EA>Cork (phellem) formation in Quercus suber stem was studied by proteomic analysis of young shoots of increasing age (Y0, Y1 and Y4) and recently-formed phellem (Y8Ph) and xylem (Y8X) from an 8-year-old branch. In this study 99 proteins were identified, 45 excised from Y8X and 54 from Y8Ph. These ones, specifically associated with phellem, are of "carbohydrate metabolism" (28%), "defence" (22%), "protein folding, stability and degradation" (19%), "regulation/ signalling" (11%), "secondary metabolism" (9%), "energy metabolism" (6%), and "membrane transport" (2%). The identification in phellem of galactosidases, xylosidases, apiose/xylose synthase, laccases and diphenol oxidases suggests intense cell wall reorganization, possibly with participation of hemicellulose/pectin biosynthesis and phenol oxidation. The identification of proteasome subunits, heat shock proteins, cyclophylin, subtilisin-like proteases, 14-3-3 proteins, Rab2 protein and enzymes interacting with nucleosides/nucleic acids gives additional evidence for cellular reorganization, involving cellular secretion, protein turnover regulation and active control processes. The high involvement in phellem of defence proteins (thioredoxin-dependent peroxidase, glutathione-S-transferase, SGT1 protein, cystatin, and chitinases) suggests a strong need for cell protection from the intense stressful events occurring in active phellem, namely, desiccation, pests/disease protection, detoxification and cell death. Identically, highly enhanced defence functions were previously reported for potato periderm formation.</EA><CC>002A04B</CC><FD>Protéine; Quercus suber; Tissu; Protéomique</FD><FG>Fagaceae; Dicotyledones; Angiospermae; Spermatophyta</FG><ED>Protein; Quercus suber; Tissue; Proteomics</ED><EG>Fagaceae; Dicotyledones; Angiospermae; Spermatophyta</EG><SD>Proteína; Quercus suber; Tejido; Proteómica</SD><LO>INIST-18007.354000191153520090</LO><ID>11-0407790</ID></server></inist></record>Pour manipuler ce document sous Unix (Dilib)
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