NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans
•Methylglyoxal dehydrogenase activity is observed only in the glutathione-depleted cells.•The first report on methylglyoxal-oxidizing alcohol dehydrogenase in microorganisms.•Candida alcohol dehydrogenase is involved in methylglyoxal oxidation and reduction.•Accumulated methylglyoxal inhibits cell g...
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| Veröffentlicht in: | FEBS letters 2014-04, Vol.588 (7), p.1144-1153 |
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| creator | Kwak, Min-Kyu Ku, MyungHee Kang, Sa-Ouk |
| description | •Methylglyoxal dehydrogenase activity is observed only in the glutathione-depleted cells.•The first report on methylglyoxal-oxidizing alcohol dehydrogenase in microorganisms.•Candida alcohol dehydrogenase is involved in methylglyoxal oxidation and reduction.•Accumulated methylglyoxal inhibits cell growth in alcohol dehydrogenase disruptants.•Alcohol dehydrogenase regulates cell cycle by catalyzing methylglyoxal in C. albicans.
We purified a fraction that showed NAD+-linked methylglyoxal dehydrogenase activity, directly catalyzing methylglyoxal oxidation to pyruvate, which was significantly increased in glutathione-depleted Candida albicans. It also showed NADH-linked methylglyoxal-reducing activity. The fraction was identified as a NAD+-linked alcohol dehydrogenase (ADH1) through mass spectrometric analyses. In ADH1-disruptants of both the wild type and glutathione-depleted cells, the intracellular methylglyoxal concentration increased significantly; defects in growth, differentiation, and virulence were observed; and G2-phase arrest was induced. |
| doi_str_mv | 10.1016/j.febslet.2014.02.042 |
| format | Article |
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We purified a fraction that showed NAD+-linked methylglyoxal dehydrogenase activity, directly catalyzing methylglyoxal oxidation to pyruvate, which was significantly increased in glutathione-depleted Candida albicans. It also showed NADH-linked methylglyoxal-reducing activity. The fraction was identified as a NAD+-linked alcohol dehydrogenase (ADH1) through mass spectrometric analyses. In ADH1-disruptants of both the wild type and glutathione-depleted cells, the intracellular methylglyoxal concentration increased significantly; defects in growth, differentiation, and virulence were observed; and G2-phase arrest was induced.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2014.02.042</identifier><identifier>PMID: 24607541</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>2′,7′-dichlorofluorescein diacetate ; 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide ; 5-fluoroorotic acid ; ADH ; alcohol dehydrogenase ; Alcohol Dehydrogenase - chemistry ; Alcohol Dehydrogenase - genetics ; Alcohol Dehydrogenase - metabolism ; Alcohol dehydrogenase 1 ; Amino Acid Sequence ; Animals ; Candida albicans ; Candida albicans - enzymology ; Candida albicans - growth & development ; Candida albicans - pathogenicity ; Conserved Sequence ; DCFH-DA ; FACS ; fast protein liquid chromatography ; Female ; fluorescence-activated cell sorting ; FOA ; FPLC ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; G2 Phase Cell Cycle Checkpoints ; G2-phase arrest ; GCS1 ; Glutathione ; Glutathione - metabolism ; GSH ; high performance liquid chromatography ; HPLC ; Hyphae - enzymology ; Hyphae - growth & development ; Kinetics ; Methylglyoxal ; methylglyoxal dehydrogenase ; Mgd ; Mice ; Mice, Inbred BALB C ; Microbial Viability ; Molecular Sequence Data ; MTT ; NAD(P) ; NADH ; nicotinamide adenine dinucleotide (phosphate) ; octadecyl silica ; ODS ; open reading frame ; ORF ; Oxidation-Reduction ; PAGE ; phenazine methosulfate ; phenylmethylsulfonyl fluoride ; PMS ; PMSF ; polyacrylamide gel electrophoresis ; propidium iodide ; Pyruvaldehyde - metabolism ; reactive oxygen species ; Reactive Oxygen Species - metabolism ; reduced nicotinamide adenine dinucleotide ; revolutions per minute ; ROS ; rpm ; Virulence ; γ-glutamylcysteine synthetase</subject><ispartof>FEBS letters, 2014-04, Vol.588 (7), p.1144-1153</ispartof><rights>2014 Federation of European Biochemical Societies</rights><rights>FEBS Letters 588 (2014) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4638-f38807edfb8588994a7ec692e4b51d695c04cec4fb580953a69211f1360d82ff3</citedby><cites>FETCH-LOGICAL-c4638-f38807edfb8588994a7ec692e4b51d695c04cec4fb580953a69211f1360d82ff3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2014.02.042$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2014.02.042$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24607541$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kwak, Min-Kyu</creatorcontrib><creatorcontrib>Ku, MyungHee</creatorcontrib><creatorcontrib>Kang, Sa-Ouk</creatorcontrib><title>NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>•Methylglyoxal dehydrogenase activity is observed only in the glutathione-depleted cells.•The first report on methylglyoxal-oxidizing alcohol dehydrogenase in microorganisms.•Candida alcohol dehydrogenase is involved in methylglyoxal oxidation and reduction.•Accumulated methylglyoxal inhibits cell growth in alcohol dehydrogenase disruptants.•Alcohol dehydrogenase regulates cell cycle by catalyzing methylglyoxal in C. albicans.
We purified a fraction that showed NAD+-linked methylglyoxal dehydrogenase activity, directly catalyzing methylglyoxal oxidation to pyruvate, which was significantly increased in glutathione-depleted Candida albicans. It also showed NADH-linked methylglyoxal-reducing activity. The fraction was identified as a NAD+-linked alcohol dehydrogenase (ADH1) through mass spectrometric analyses. In ADH1-disruptants of both the wild type and glutathione-depleted cells, the intracellular methylglyoxal concentration increased significantly; defects in growth, differentiation, and virulence were observed; and G2-phase arrest was induced.</description><subject>2′,7′-dichlorofluorescein diacetate</subject><subject>3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide</subject><subject>5-fluoroorotic acid</subject><subject>ADH</subject><subject>alcohol dehydrogenase</subject><subject>Alcohol Dehydrogenase - chemistry</subject><subject>Alcohol Dehydrogenase - genetics</subject><subject>Alcohol Dehydrogenase - metabolism</subject><subject>Alcohol dehydrogenase 1</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Candida albicans</subject><subject>Candida albicans - enzymology</subject><subject>Candida albicans - growth & development</subject><subject>Candida albicans - pathogenicity</subject><subject>Conserved Sequence</subject><subject>DCFH-DA</subject><subject>FACS</subject><subject>fast protein liquid chromatography</subject><subject>Female</subject><subject>fluorescence-activated cell sorting</subject><subject>FOA</subject><subject>FPLC</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>G2 Phase Cell Cycle Checkpoints</subject><subject>G2-phase arrest</subject><subject>GCS1</subject><subject>Glutathione</subject><subject>Glutathione - metabolism</subject><subject>GSH</subject><subject>high performance liquid chromatography</subject><subject>HPLC</subject><subject>Hyphae - enzymology</subject><subject>Hyphae - growth & development</subject><subject>Kinetics</subject><subject>Methylglyoxal</subject><subject>methylglyoxal dehydrogenase</subject><subject>Mgd</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Microbial Viability</subject><subject>Molecular Sequence Data</subject><subject>MTT</subject><subject>NAD(P)</subject><subject>NADH</subject><subject>nicotinamide adenine dinucleotide (phosphate)</subject><subject>octadecyl silica</subject><subject>ODS</subject><subject>open reading frame</subject><subject>ORF</subject><subject>Oxidation-Reduction</subject><subject>PAGE</subject><subject>phenazine methosulfate</subject><subject>phenylmethylsulfonyl fluoride</subject><subject>PMS</subject><subject>PMSF</subject><subject>polyacrylamide gel electrophoresis</subject><subject>propidium iodide</subject><subject>Pyruvaldehyde - metabolism</subject><subject>reactive oxygen species</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>reduced nicotinamide adenine dinucleotide</subject><subject>revolutions per minute</subject><subject>ROS</subject><subject>rpm</subject><subject>Virulence</subject><subject>γ-glutamylcysteine synthetase</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUFv1DAQhS0EotvCTwDliFQl2I7tOCdUlpYiVeUAHJHl2JNdL1672NnS_Hu82oVrexqP5s0b630IvSG4IZiI95tmhCF7mBqKCWswbTCjz9CCyK6tWybkc7TAZVLzrm9P0GnOG1x6SfqX6IQygTvOyAL9vL34dF57F36BrbQ3cR19ZWE92xRXEHSGilQJVjuvJ8jVFqb17Fd-jg_aVyYGA2FKenIxVC5USx2ss7oYDc7okF-hF6P2GV4f6xn6cXX5fXld33z9_GV5cVMbJlpZj62UuAM7DpJL2fdMd2BET4ENnFjRc4OZAcPGgUvc81aXGSEjaQW2ko5je4beHXzvUvy9gzyprcsGvNcB4i6rEgqVrCMdeVzKS7xYMEKLlB-kJsWcE4zqLrmtTrMiWO0hqI06QlB7CApTVSCUvbfHE7thC_b_1r_Ui-D6IPjjPMxPc1VXlx_ptz3RPVDCyktQWaw-HKygxHvvIKlsHBQs1iUwk7LRPfLbv2Uqr78</recordid><startdate>20140402</startdate><enddate>20140402</enddate><creator>Kwak, Min-Kyu</creator><creator>Ku, MyungHee</creator><creator>Kang, Sa-Ouk</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>7TM</scope><scope>M7N</scope></search><sort><creationdate>20140402</creationdate><title>NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans</title><author>Kwak, Min-Kyu ; Ku, MyungHee ; Kang, Sa-Ouk</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4638-f38807edfb8588994a7ec692e4b51d695c04cec4fb580953a69211f1360d82ff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>2′,7′-dichlorofluorescein diacetate</topic><topic>3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide</topic><topic>5-fluoroorotic acid</topic><topic>ADH</topic><topic>alcohol dehydrogenase</topic><topic>Alcohol Dehydrogenase - chemistry</topic><topic>Alcohol Dehydrogenase - genetics</topic><topic>Alcohol Dehydrogenase - metabolism</topic><topic>Alcohol dehydrogenase 1</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Candida albicans</topic><topic>Candida albicans - enzymology</topic><topic>Candida albicans - growth & development</topic><topic>Candida albicans - pathogenicity</topic><topic>Conserved Sequence</topic><topic>DCFH-DA</topic><topic>FACS</topic><topic>fast protein liquid chromatography</topic><topic>Female</topic><topic>fluorescence-activated cell sorting</topic><topic>FOA</topic><topic>FPLC</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>G2 Phase Cell Cycle Checkpoints</topic><topic>G2-phase arrest</topic><topic>GCS1</topic><topic>Glutathione</topic><topic>Glutathione - metabolism</topic><topic>GSH</topic><topic>high performance liquid chromatography</topic><topic>HPLC</topic><topic>Hyphae - enzymology</topic><topic>Hyphae - growth & development</topic><topic>Kinetics</topic><topic>Methylglyoxal</topic><topic>methylglyoxal dehydrogenase</topic><topic>Mgd</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Microbial Viability</topic><topic>Molecular Sequence Data</topic><topic>MTT</topic><topic>NAD(P)</topic><topic>NADH</topic><topic>nicotinamide adenine dinucleotide (phosphate)</topic><topic>octadecyl silica</topic><topic>ODS</topic><topic>open reading frame</topic><topic>ORF</topic><topic>Oxidation-Reduction</topic><topic>PAGE</topic><topic>phenazine methosulfate</topic><topic>phenylmethylsulfonyl fluoride</topic><topic>PMS</topic><topic>PMSF</topic><topic>polyacrylamide gel electrophoresis</topic><topic>propidium iodide</topic><topic>Pyruvaldehyde - metabolism</topic><topic>reactive oxygen species</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>reduced nicotinamide adenine dinucleotide</topic><topic>revolutions per minute</topic><topic>ROS</topic><topic>rpm</topic><topic>Virulence</topic><topic>γ-glutamylcysteine synthetase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kwak, Min-Kyu</creatorcontrib><creatorcontrib>Ku, MyungHee</creatorcontrib><creatorcontrib>Kang, Sa-Ouk</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Nucleic Acids Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kwak, Min-Kyu</au><au>Ku, MyungHee</au><au>Kang, Sa-Ouk</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2014-04-02</date><risdate>2014</risdate><volume>588</volume><issue>7</issue><spage>1144</spage><epage>1153</epage><pages>1144-1153</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>•Methylglyoxal dehydrogenase activity is observed only in the glutathione-depleted cells.•The first report on methylglyoxal-oxidizing alcohol dehydrogenase in microorganisms.•Candida alcohol dehydrogenase is involved in methylglyoxal oxidation and reduction.•Accumulated methylglyoxal inhibits cell growth in alcohol dehydrogenase disruptants.•Alcohol dehydrogenase regulates cell cycle by catalyzing methylglyoxal in C. albicans.
We purified a fraction that showed NAD+-linked methylglyoxal dehydrogenase activity, directly catalyzing methylglyoxal oxidation to pyruvate, which was significantly increased in glutathione-depleted Candida albicans. It also showed NADH-linked methylglyoxal-reducing activity. The fraction was identified as a NAD+-linked alcohol dehydrogenase (ADH1) through mass spectrometric analyses. In ADH1-disruptants of both the wild type and glutathione-depleted cells, the intracellular methylglyoxal concentration increased significantly; defects in growth, differentiation, and virulence were observed; and G2-phase arrest was induced.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>24607541</pmid><doi>10.1016/j.febslet.2014.02.042</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 2′,7′-dichlorofluorescein diacetate 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide 5-fluoroorotic acid ADH alcohol dehydrogenase Alcohol Dehydrogenase - chemistry Alcohol Dehydrogenase - genetics Alcohol Dehydrogenase - metabolism Alcohol dehydrogenase 1 Amino Acid Sequence Animals Candida albicans Candida albicans - enzymology Candida albicans - growth & development Candida albicans - pathogenicity Conserved Sequence DCFH-DA FACS fast protein liquid chromatography Female fluorescence-activated cell sorting FOA FPLC Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism G2 Phase Cell Cycle Checkpoints G2-phase arrest GCS1 Glutathione Glutathione - metabolism GSH high performance liquid chromatography HPLC Hyphae - enzymology Hyphae - growth & development Kinetics Methylglyoxal methylglyoxal dehydrogenase Mgd Mice Mice, Inbred BALB C Microbial Viability Molecular Sequence Data MTT NAD(P) NADH nicotinamide adenine dinucleotide (phosphate) octadecyl silica ODS open reading frame ORF Oxidation-Reduction PAGE phenazine methosulfate phenylmethylsulfonyl fluoride PMS PMSF polyacrylamide gel electrophoresis propidium iodide Pyruvaldehyde - metabolism reactive oxygen species Reactive Oxygen Species - metabolism reduced nicotinamide adenine dinucleotide revolutions per minute ROS rpm Virulence γ-glutamylcysteine synthetase |
| title | NAD+-linked alcohol dehydrogenase 1 regulates methylglyoxal concentration in Candida albicans |
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