New and classic families of secreted fungal heme peroxidases

Heme-containing peroxidases secreted by fungi are a fascinating group of biocatalysts with various ecological and biotechnological implications. For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant comp...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Applied microbiology and biotechnology 2010-07, Vol.87 (3), p.871-897
Hauptverfasser: Hofrichter, Martin, Ullrich, René, Pecyna, Marek J, Liers, Christiane, Lundell, Taina
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 897
container_issue 3
container_start_page 871
container_title Applied microbiology and biotechnology
container_volume 87
creator Hofrichter, Martin
Ullrich, René
Pecyna, Marek J
Liers, Christiane
Lundell, Taina
description Heme-containing peroxidases secreted by fungi are a fascinating group of biocatalysts with various ecological and biotechnological implications. For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant compounds as well as in the natural turnover of humic substances and organohalogens. The current review focuses on the most recently discovered and novel types of heme-dependent peroxidases, aromatic peroxygenases (APOs), and dye-decolorizing peroxidases (DyPs), which catalyze remarkable reactions such as peroxide-driven oxygen transfer and cleavage of anthraquinone derivatives, respectively, and represent own separate peroxidase superfamilies. Furthermore, several aspects of the “classic” fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments.
doi_str_mv 10.1007/s00253-010-2633-0
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_744622580</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>744622580</sourcerecordid><originalsourceid>FETCH-LOGICAL-c522t-752ed8ff16532cb1cdf2ade510ca9b5bbcff9a8af7b2f30d48ba9a9760acc5c33</originalsourceid><addsrcrecordid>eNqFkc2LFDEQxYMo7uzoH-BFG2Hx1FqpdNId2IssfsGiB91zqE4nYy_9MaamUf97M_Toggc9JZBfvbx6T4gnEl5KgPoVA6BWJUgo0ah8uSc2slJYgpHVfbEBWeuy1rY5E-fMtwASG2MeijOEymor9UZcfgzfC5q6wg_E3Psi0tgPfeBijgUHn8IhdEVcph0NxdcwhmIf0vyj74gDPxIPIg0cHp_Orbh5--bL1fvy-tO7D1evr0uvEQ_ZAYauiVEardC30ncRqQtagifb6rb1MVpqKNYtRgVd1bRkydYGyHvtldqKF6vuPs3flsAHN_bswzDQFOaFXV1VBlE38H9SKQVoc0hb8fwv8nZe0pTXcDrnZHQOKENyhXyamVOIbp_6kdJPJ8EdK3BrBS5X4I4VuKOFpyfhpR1D92fid-YZuDgBxJ6GmGjyPd9xaLVRDWYOV47z07QL6c7hv35_tg5Fmh3tUha--YwgFchG14C1-gXwpaZE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>501265959</pqid></control><display><type>article</type><title>New and classic families of secreted fungal heme peroxidases</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Hofrichter, Martin ; Ullrich, René ; Pecyna, Marek J ; Liers, Christiane ; Lundell, Taina</creator><creatorcontrib>Hofrichter, Martin ; Ullrich, René ; Pecyna, Marek J ; Liers, Christiane ; Lundell, Taina</creatorcontrib><description>Heme-containing peroxidases secreted by fungi are a fascinating group of biocatalysts with various ecological and biotechnological implications. For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant compounds as well as in the natural turnover of humic substances and organohalogens. The current review focuses on the most recently discovered and novel types of heme-dependent peroxidases, aromatic peroxygenases (APOs), and dye-decolorizing peroxidases (DyPs), which catalyze remarkable reactions such as peroxide-driven oxygen transfer and cleavage of anthraquinone derivatives, respectively, and represent own separate peroxidase superfamilies. Furthermore, several aspects of the “classic” fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-010-2633-0</identifier><identifier>PMID: 20495915</identifier><identifier>CODEN: AMBIDG</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Amino Acid Sequence ; Basidiomycota ; Biocatalysts ; Biodegradation ; Biological and medical sciences ; Biomedical and Life Sciences ; Biotechnology ; Catalysis ; Classification ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Fungi ; Fungi - chemistry ; Fungi - classification ; Fungi - enzymology ; Fungi - genetics ; Heme - metabolism ; Life Sciences ; Lignin ; Manganese ; Microbial Genetics and Genomics ; Microbiology ; Mini-Review ; Molecular Sequence Data ; Multigene Family ; Oxidation ; Oxygen transfer ; P450 ; peroxidases ; Peroxidases - chemistry ; Peroxidases - genetics ; Peroxidases - metabolism ; Peroxygenases ; Phenols ; Phylogeny ; Physiology ; Protein Transport ; Proteins ; Sequence Alignment ; Thyroid gland</subject><ispartof>Applied microbiology and biotechnology, 2010-07, Vol.87 (3), p.871-897</ispartof><rights>Springer-Verlag 2010</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c522t-752ed8ff16532cb1cdf2ade510ca9b5bbcff9a8af7b2f30d48ba9a9760acc5c33</citedby><cites>FETCH-LOGICAL-c522t-752ed8ff16532cb1cdf2ade510ca9b5bbcff9a8af7b2f30d48ba9a9760acc5c33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-010-2633-0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-010-2633-0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27922,27923,41486,42555,51317</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=22956382$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20495915$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hofrichter, Martin</creatorcontrib><creatorcontrib>Ullrich, René</creatorcontrib><creatorcontrib>Pecyna, Marek J</creatorcontrib><creatorcontrib>Liers, Christiane</creatorcontrib><creatorcontrib>Lundell, Taina</creatorcontrib><title>New and classic families of secreted fungal heme peroxidases</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>Heme-containing peroxidases secreted by fungi are a fascinating group of biocatalysts with various ecological and biotechnological implications. For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant compounds as well as in the natural turnover of humic substances and organohalogens. The current review focuses on the most recently discovered and novel types of heme-dependent peroxidases, aromatic peroxygenases (APOs), and dye-decolorizing peroxidases (DyPs), which catalyze remarkable reactions such as peroxide-driven oxygen transfer and cleavage of anthraquinone derivatives, respectively, and represent own separate peroxidase superfamilies. Furthermore, several aspects of the “classic” fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments.</description><subject>Amino Acid Sequence</subject><subject>Basidiomycota</subject><subject>Biocatalysts</subject><subject>Biodegradation</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Catalysis</subject><subject>Classification</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Fungi</subject><subject>Fungi - chemistry</subject><subject>Fungi - classification</subject><subject>Fungi - enzymology</subject><subject>Fungi - genetics</subject><subject>Heme - metabolism</subject><subject>Life Sciences</subject><subject>Lignin</subject><subject>Manganese</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mini-Review</subject><subject>Molecular Sequence Data</subject><subject>Multigene Family</subject><subject>Oxidation</subject><subject>Oxygen transfer</subject><subject>P450</subject><subject>peroxidases</subject><subject>Peroxidases - chemistry</subject><subject>Peroxidases - genetics</subject><subject>Peroxidases - metabolism</subject><subject>Peroxygenases</subject><subject>Phenols</subject><subject>Phylogeny</subject><subject>Physiology</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Sequence Alignment</subject><subject>Thyroid gland</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkc2LFDEQxYMo7uzoH-BFG2Hx1FqpdNId2IssfsGiB91zqE4nYy_9MaamUf97M_Toggc9JZBfvbx6T4gnEl5KgPoVA6BWJUgo0ah8uSc2slJYgpHVfbEBWeuy1rY5E-fMtwASG2MeijOEymor9UZcfgzfC5q6wg_E3Psi0tgPfeBijgUHn8IhdEVcph0NxdcwhmIf0vyj74gDPxIPIg0cHp_Orbh5--bL1fvy-tO7D1evr0uvEQ_ZAYauiVEardC30ncRqQtagifb6rb1MVpqKNYtRgVd1bRkydYGyHvtldqKF6vuPs3flsAHN_bswzDQFOaFXV1VBlE38H9SKQVoc0hb8fwv8nZe0pTXcDrnZHQOKENyhXyamVOIbp_6kdJPJ8EdK3BrBS5X4I4VuKOFpyfhpR1D92fid-YZuDgBxJ6GmGjyPd9xaLVRDWYOV47z07QL6c7hv35_tg5Fmh3tUha--YwgFchG14C1-gXwpaZE</recordid><startdate>20100701</startdate><enddate>20100701</enddate><creator>Hofrichter, Martin</creator><creator>Ullrich, René</creator><creator>Pecyna, Marek J</creator><creator>Liers, Christiane</creator><creator>Lundell, Taina</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7WY</scope><scope>7WZ</scope><scope>7X7</scope><scope>7XB</scope><scope>87Z</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8FL</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BEZIV</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FRNLG</scope><scope>FYUFA</scope><scope>F~G</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K60</scope><scope>K6~</scope><scope>K9.</scope><scope>L.-</scope><scope>LK8</scope><scope>M0C</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQBIZ</scope><scope>PQBZA</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20100701</creationdate><title>New and classic families of secreted fungal heme peroxidases</title><author>Hofrichter, Martin ; Ullrich, René ; Pecyna, Marek J ; Liers, Christiane ; Lundell, Taina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c522t-752ed8ff16532cb1cdf2ade510ca9b5bbcff9a8af7b2f30d48ba9a9760acc5c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Basidiomycota</topic><topic>Biocatalysts</topic><topic>Biodegradation</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Catalysis</topic><topic>Classification</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Fungi</topic><topic>Fungi - chemistry</topic><topic>Fungi - classification</topic><topic>Fungi - enzymology</topic><topic>Fungi - genetics</topic><topic>Heme - metabolism</topic><topic>Life Sciences</topic><topic>Lignin</topic><topic>Manganese</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Mini-Review</topic><topic>Molecular Sequence Data</topic><topic>Multigene Family</topic><topic>Oxidation</topic><topic>Oxygen transfer</topic><topic>P450</topic><topic>peroxidases</topic><topic>Peroxidases - chemistry</topic><topic>Peroxidases - genetics</topic><topic>Peroxidases - metabolism</topic><topic>Peroxygenases</topic><topic>Phenols</topic><topic>Phylogeny</topic><topic>Physiology</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Sequence Alignment</topic><topic>Thyroid gland</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hofrichter, Martin</creatorcontrib><creatorcontrib>Ullrich, René</creatorcontrib><creatorcontrib>Pecyna, Marek J</creatorcontrib><creatorcontrib>Liers, Christiane</creatorcontrib><creatorcontrib>Lundell, Taina</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ABI/INFORM Collection</collection><collection>ABI/INFORM Global (PDF only)</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ABI/INFORM Global (Alumni Edition)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ABI/INFORM Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hofrichter, Martin</au><au>Ullrich, René</au><au>Pecyna, Marek J</au><au>Liers, Christiane</au><au>Lundell, Taina</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New and classic families of secreted fungal heme peroxidases</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2010-07-01</date><risdate>2010</risdate><volume>87</volume><issue>3</issue><spage>871</spage><epage>897</epage><pages>871-897</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><coden>AMBIDG</coden><abstract>Heme-containing peroxidases secreted by fungi are a fascinating group of biocatalysts with various ecological and biotechnological implications. For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant compounds as well as in the natural turnover of humic substances and organohalogens. The current review focuses on the most recently discovered and novel types of heme-dependent peroxidases, aromatic peroxygenases (APOs), and dye-decolorizing peroxidases (DyPs), which catalyze remarkable reactions such as peroxide-driven oxygen transfer and cleavage of anthraquinone derivatives, respectively, and represent own separate peroxidase superfamilies. Furthermore, several aspects of the “classic” fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>20495915</pmid><doi>10.1007/s00253-010-2633-0</doi><tpages>27</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0175-7598
ispartof Applied microbiology and biotechnology, 2010-07, Vol.87 (3), p.871-897
issn 0175-7598
1432-0614
language eng
recordid cdi_proquest_miscellaneous_744622580
source MEDLINE; SpringerLink Journals - AutoHoldings
subjects Amino Acid Sequence
Basidiomycota
Biocatalysts
Biodegradation
Biological and medical sciences
Biomedical and Life Sciences
Biotechnology
Catalysis
Classification
Enzymes
Fundamental and applied biological sciences. Psychology
Fungal Proteins - chemistry
Fungal Proteins - genetics
Fungal Proteins - metabolism
Fungi
Fungi - chemistry
Fungi - classification
Fungi - enzymology
Fungi - genetics
Heme - metabolism
Life Sciences
Lignin
Manganese
Microbial Genetics and Genomics
Microbiology
Mini-Review
Molecular Sequence Data
Multigene Family
Oxidation
Oxygen transfer
P450
peroxidases
Peroxidases - chemistry
Peroxidases - genetics
Peroxidases - metabolism
Peroxygenases
Phenols
Phylogeny
Physiology
Protein Transport
Proteins
Sequence Alignment
Thyroid gland
title New and classic families of secreted fungal heme peroxidases
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T19%3A35%3A33IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=New%20and%20classic%20families%20of%20secreted%20fungal%20heme%20peroxidases&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Hofrichter,%20Martin&rft.date=2010-07-01&rft.volume=87&rft.issue=3&rft.spage=871&rft.epage=897&rft.pages=871-897&rft.issn=0175-7598&rft.eissn=1432-0614&rft.coden=AMBIDG&rft_id=info:doi/10.1007/s00253-010-2633-0&rft_dat=%3Cproquest_cross%3E744622580%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=501265959&rft_id=info:pmid/20495915&rfr_iscdi=true