Extra-glycosomal localisation of Trypanosoma brucei hexokinase 2
[Display omitted] ► Trypanosoma brucei hexokinase 2 (TbHK2) localisation is lifecycle stage-dependent. ► TbHK2 localises to glycosomes and the flagellum in blood stage parasites. ► In insect stage parasites, distribution is different. ► TbHK2 knockout and parental parasites have similar speed and di...
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| Veröffentlicht in: | International journal for parasitology 2012-04, Vol.42 (4), p.401-409 |
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| creator | Joice, April C. Lyda, Todd L. Sayce, Andrew C. Verplaetse, Emilie Morris, Meredith T. Michels, Paul A.M. Robinson, Derrick R. Morris, James C. |
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► Trypanosoma brucei hexokinase 2 (TbHK2) localisation is lifecycle stage-dependent. ► TbHK2 localises to glycosomes and the flagellum in blood stage parasites. ► In insect stage parasites, distribution is different. ► TbHK2 knockout and parental parasites have similar speed and direction of motion.
The majority of the glycolytic enzymes in the African trypanosome are compartmentalised within peroxisome-like organelles, the glycosomes. Polypeptides harbouring peroxisomal targeting sequences (PTS type 1 or 2) are targeted to these organelles. This targeting is essential to parasite viability, as compartmentalisation of glycolytic enzymes prevents unregulated ATP-dependent phosphorylation of intermediate metabolites. Here, we report the surprising extra-glycosomal localisation of a PTS-2 bearing trypanosomal hexokinase, TbHK2. In bloodstream form parasites, the protein localises to both glycosomes and to the flagellum. Evidence for this includes fractionation and immunofluorescence studies using antisera generated against the authentic protein as well as detection of epitope-tagged recombinant versions of the protein. In the insect stage parasite, distribution is different, with the polypeptide localised to glycosomes and proximal to the basal bodies. The function of the extra-glycosomal protein remains unclear. While its association with the basal body suggests that it may have a role in locomotion in the insect stage parasite, no detectable defect in directional motility or velocity of cell movement were observed for TbHK2-deficient cells, suggesting that the protein may have a different function in the cell. |
| doi_str_mv | 10.1016/j.ijpara.2012.02.008 |
| format | Article |
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► Trypanosoma brucei hexokinase 2 (TbHK2) localisation is lifecycle stage-dependent. ► TbHK2 localises to glycosomes and the flagellum in blood stage parasites. ► In insect stage parasites, distribution is different. ► TbHK2 knockout and parental parasites have similar speed and direction of motion.
The majority of the glycolytic enzymes in the African trypanosome are compartmentalised within peroxisome-like organelles, the glycosomes. Polypeptides harbouring peroxisomal targeting sequences (PTS type 1 or 2) are targeted to these organelles. This targeting is essential to parasite viability, as compartmentalisation of glycolytic enzymes prevents unregulated ATP-dependent phosphorylation of intermediate metabolites. Here, we report the surprising extra-glycosomal localisation of a PTS-2 bearing trypanosomal hexokinase, TbHK2. In bloodstream form parasites, the protein localises to both glycosomes and to the flagellum. Evidence for this includes fractionation and immunofluorescence studies using antisera generated against the authentic protein as well as detection of epitope-tagged recombinant versions of the protein. In the insect stage parasite, distribution is different, with the polypeptide localised to glycosomes and proximal to the basal bodies. The function of the extra-glycosomal protein remains unclear. While its association with the basal body suggests that it may have a role in locomotion in the insect stage parasite, no detectable defect in directional motility or velocity of cell movement were observed for TbHK2-deficient cells, suggesting that the protein may have a different function in the cell.</description><identifier>ISSN: 0020-7519</identifier><identifier>EISSN: 1879-0135</identifier><identifier>DOI: 10.1016/j.ijpara.2012.02.008</identifier><identifier>PMID: 22619756</identifier><identifier>CODEN: IJPYBT</identifier><language>eng</language><publisher>Kidlington: Elsevier Ltd</publisher><subject>Antisera ; antiserum ; Basal bodies ; Biochemistry, Molecular Biology ; Biological and medical sciences ; bloodstream forms ; Cell migration ; cell motility ; Enzymes ; Flagella ; Flagella - chemistry ; Flagella - enzymology ; Flagellum ; fluorescent antibody technique ; fractionation ; Fundamental and applied biological sciences. Psychology ; Gene Deletion ; Glycolysis ; Glycosome ; Glycosomes ; Hexokinase ; Hexokinase - analysis ; Hexokinase - genetics ; Human protozoal diseases ; Immunofluorescence ; Infectious diseases ; insects ; Life cycle. Host-agent relationship. Pathogenesis ; Life Sciences ; Locomotion ; Medical sciences ; Metabolites ; Microbiology and Parasitology ; microbodies ; Microbodies - chemistry ; Microbodies - enzymology ; Organelles ; parasites ; Parasitic diseases ; Phosphorylation ; polypeptides ; Protozoa ; Protozoal diseases ; recombinant proteins ; Trypanosoma brucei ; Trypanosoma brucei brucei - chemistry ; Trypanosoma brucei brucei - enzymology ; Trypanosoma brucei brucei - genetics ; Trypanosoma brucei brucei - physiology ; Trypanosomiasis ; viability</subject><ispartof>International journal for parasitology, 2012-04, Vol.42 (4), p.401-409</ispartof><rights>2012 Australian Society for Parasitology Inc.</rights><rights>2015 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>2012 Australian Society for Parasitology. Published by Elsevier Ltd. All rights reserved. 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c584t-5b71882c89f79965fb85fbca13e09b311c539285e1144ee6e2c4ec6e4d0f01d73</citedby><cites>FETCH-LOGICAL-c584t-5b71882c89f79965fb85fbca13e09b311c539285e1144ee6e2c4ec6e4d0f01d73</cites><orcidid>0000-0001-8200-140X ; 0000-0001-5572-4127</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijpara.2012.02.008$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,315,782,786,887,3552,27931,27932,46002</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25845164$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22619756$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02323210$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Joice, April C.</creatorcontrib><creatorcontrib>Lyda, Todd L.</creatorcontrib><creatorcontrib>Sayce, Andrew C.</creatorcontrib><creatorcontrib>Verplaetse, Emilie</creatorcontrib><creatorcontrib>Morris, Meredith T.</creatorcontrib><creatorcontrib>Michels, Paul A.M.</creatorcontrib><creatorcontrib>Robinson, Derrick R.</creatorcontrib><creatorcontrib>Morris, James C.</creatorcontrib><title>Extra-glycosomal localisation of Trypanosoma brucei hexokinase 2</title><title>International journal for parasitology</title><addtitle>Int J Parasitol</addtitle><description>[Display omitted]
► Trypanosoma brucei hexokinase 2 (TbHK2) localisation is lifecycle stage-dependent. ► TbHK2 localises to glycosomes and the flagellum in blood stage parasites. ► In insect stage parasites, distribution is different. ► TbHK2 knockout and parental parasites have similar speed and direction of motion.
The majority of the glycolytic enzymes in the African trypanosome are compartmentalised within peroxisome-like organelles, the glycosomes. Polypeptides harbouring peroxisomal targeting sequences (PTS type 1 or 2) are targeted to these organelles. This targeting is essential to parasite viability, as compartmentalisation of glycolytic enzymes prevents unregulated ATP-dependent phosphorylation of intermediate metabolites. Here, we report the surprising extra-glycosomal localisation of a PTS-2 bearing trypanosomal hexokinase, TbHK2. In bloodstream form parasites, the protein localises to both glycosomes and to the flagellum. Evidence for this includes fractionation and immunofluorescence studies using antisera generated against the authentic protein as well as detection of epitope-tagged recombinant versions of the protein. In the insect stage parasite, distribution is different, with the polypeptide localised to glycosomes and proximal to the basal bodies. The function of the extra-glycosomal protein remains unclear. While its association with the basal body suggests that it may have a role in locomotion in the insect stage parasite, no detectable defect in directional motility or velocity of cell movement were observed for TbHK2-deficient cells, suggesting that the protein may have a different function in the cell.</description><subject>Antisera</subject><subject>antiserum</subject><subject>Basal bodies</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological and medical sciences</subject><subject>bloodstream forms</subject><subject>Cell migration</subject><subject>cell motility</subject><subject>Enzymes</subject><subject>Flagella</subject><subject>Flagella - chemistry</subject><subject>Flagella - enzymology</subject><subject>Flagellum</subject><subject>fluorescent antibody technique</subject><subject>fractionation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Deletion</subject><subject>Glycolysis</subject><subject>Glycosome</subject><subject>Glycosomes</subject><subject>Hexokinase</subject><subject>Hexokinase - analysis</subject><subject>Hexokinase - genetics</subject><subject>Human protozoal diseases</subject><subject>Immunofluorescence</subject><subject>Infectious diseases</subject><subject>insects</subject><subject>Life cycle. Host-agent relationship. Pathogenesis</subject><subject>Life Sciences</subject><subject>Locomotion</subject><subject>Medical sciences</subject><subject>Metabolites</subject><subject>Microbiology and Parasitology</subject><subject>microbodies</subject><subject>Microbodies - chemistry</subject><subject>Microbodies - enzymology</subject><subject>Organelles</subject><subject>parasites</subject><subject>Parasitic diseases</subject><subject>Phosphorylation</subject><subject>polypeptides</subject><subject>Protozoa</subject><subject>Protozoal diseases</subject><subject>recombinant proteins</subject><subject>Trypanosoma brucei</subject><subject>Trypanosoma brucei brucei - chemistry</subject><subject>Trypanosoma brucei brucei - enzymology</subject><subject>Trypanosoma brucei brucei - genetics</subject><subject>Trypanosoma brucei brucei - physiology</subject><subject>Trypanosomiasis</subject><subject>viability</subject><issn>0020-7519</issn><issn>1879-0135</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kV1v0zAUhi0EYmXwDxDkBgkuUnz8mdwgpmkwpEpcsF1bjnPSuqRxsdNq_fe4pGzABbItS_Zz3vPxEvIS6BwoqPfruV9vbbRzRoHNad60ekRmUOm6pMDlYzKjlNFSS6jPyLOU1pSC5EI8JWeMKai1VDPy8epujLZc9gcXUtjYvuiDs71PdvRhKEJX3MTD1g6_Posm7hz6YoV34bsfbMKCPSdPOtsnfHG6z8ntp6uby-ty8fXzl8uLRelkJcZSNhqqirmq7nRdK9k1VT7OAkdaNxzASV6zSiKAEIgKmRPoFIqWdhRazc_Jh0l3u2s22Docct292Ua_sfFggvXm75_Br8wy7A3XQDUXWeDdJLD6J-z6YmGOb5TxvIDuIbNvT8li-LHDNJqNTw773g4YdslkA4ABr7TKqJhQF0NKEbt7baBHTpm1mYwyR6NyFpONymGv_mznPui3Mxl4cwJsyoZ00Q7OpwcuT1WCOrb1euI6G4xdxszcfsuZRHZb58bhYXKY7dl7jCY5j4PD1kd0o2mD_3-tPwHC2bvk</recordid><startdate>20120401</startdate><enddate>20120401</enddate><creator>Joice, April C.</creator><creator>Lyda, Todd L.</creator><creator>Sayce, Andrew C.</creator><creator>Verplaetse, Emilie</creator><creator>Morris, Meredith T.</creator><creator>Michels, Paul A.M.</creator><creator>Robinson, Derrick R.</creator><creator>Morris, James C.</creator><general>Elsevier Ltd</general><general>Elsevier</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>M7N</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-8200-140X</orcidid><orcidid>https://orcid.org/0000-0001-5572-4127</orcidid></search><sort><creationdate>20120401</creationdate><title>Extra-glycosomal localisation of Trypanosoma brucei hexokinase 2</title><author>Joice, April C. ; Lyda, Todd L. ; Sayce, Andrew C. ; Verplaetse, Emilie ; Morris, Meredith T. ; Michels, Paul A.M. ; Robinson, Derrick R. ; Morris, James C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c584t-5b71882c89f79965fb85fbca13e09b311c539285e1144ee6e2c4ec6e4d0f01d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Antisera</topic><topic>antiserum</topic><topic>Basal bodies</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological and medical sciences</topic><topic>bloodstream forms</topic><topic>Cell migration</topic><topic>cell motility</topic><topic>Enzymes</topic><topic>Flagella</topic><topic>Flagella - chemistry</topic><topic>Flagella - enzymology</topic><topic>Flagellum</topic><topic>fluorescent antibody technique</topic><topic>fractionation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Deletion</topic><topic>Glycolysis</topic><topic>Glycosome</topic><topic>Glycosomes</topic><topic>Hexokinase</topic><topic>Hexokinase - analysis</topic><topic>Hexokinase - genetics</topic><topic>Human protozoal diseases</topic><topic>Immunofluorescence</topic><topic>Infectious diseases</topic><topic>insects</topic><topic>Life cycle. Host-agent relationship. Pathogenesis</topic><topic>Life Sciences</topic><topic>Locomotion</topic><topic>Medical sciences</topic><topic>Metabolites</topic><topic>Microbiology and Parasitology</topic><topic>microbodies</topic><topic>Microbodies - chemistry</topic><topic>Microbodies - enzymology</topic><topic>Organelles</topic><topic>parasites</topic><topic>Parasitic diseases</topic><topic>Phosphorylation</topic><topic>polypeptides</topic><topic>Protozoa</topic><topic>Protozoal diseases</topic><topic>recombinant proteins</topic><topic>Trypanosoma brucei</topic><topic>Trypanosoma brucei brucei - chemistry</topic><topic>Trypanosoma brucei brucei - enzymology</topic><topic>Trypanosoma brucei brucei - genetics</topic><topic>Trypanosoma brucei brucei - physiology</topic><topic>Trypanosomiasis</topic><topic>viability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Joice, April C.</creatorcontrib><creatorcontrib>Lyda, Todd L.</creatorcontrib><creatorcontrib>Sayce, Andrew C.</creatorcontrib><creatorcontrib>Verplaetse, Emilie</creatorcontrib><creatorcontrib>Morris, Meredith T.</creatorcontrib><creatorcontrib>Michels, Paul A.M.</creatorcontrib><creatorcontrib>Robinson, Derrick R.</creatorcontrib><creatorcontrib>Morris, James C.</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>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal for parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joice, April C.</au><au>Lyda, Todd L.</au><au>Sayce, Andrew C.</au><au>Verplaetse, Emilie</au><au>Morris, Meredith T.</au><au>Michels, Paul A.M.</au><au>Robinson, Derrick R.</au><au>Morris, James C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Extra-glycosomal localisation of Trypanosoma brucei hexokinase 2</atitle><jtitle>International journal for parasitology</jtitle><addtitle>Int J Parasitol</addtitle><date>2012-04-01</date><risdate>2012</risdate><volume>42</volume><issue>4</issue><spage>401</spage><epage>409</epage><pages>401-409</pages><issn>0020-7519</issn><eissn>1879-0135</eissn><coden>IJPYBT</coden><abstract>[Display omitted]
► Trypanosoma brucei hexokinase 2 (TbHK2) localisation is lifecycle stage-dependent. ► TbHK2 localises to glycosomes and the flagellum in blood stage parasites. ► In insect stage parasites, distribution is different. ► TbHK2 knockout and parental parasites have similar speed and direction of motion.
The majority of the glycolytic enzymes in the African trypanosome are compartmentalised within peroxisome-like organelles, the glycosomes. Polypeptides harbouring peroxisomal targeting sequences (PTS type 1 or 2) are targeted to these organelles. This targeting is essential to parasite viability, as compartmentalisation of glycolytic enzymes prevents unregulated ATP-dependent phosphorylation of intermediate metabolites. Here, we report the surprising extra-glycosomal localisation of a PTS-2 bearing trypanosomal hexokinase, TbHK2. In bloodstream form parasites, the protein localises to both glycosomes and to the flagellum. Evidence for this includes fractionation and immunofluorescence studies using antisera generated against the authentic protein as well as detection of epitope-tagged recombinant versions of the protein. In the insect stage parasite, distribution is different, with the polypeptide localised to glycosomes and proximal to the basal bodies. The function of the extra-glycosomal protein remains unclear. While its association with the basal body suggests that it may have a role in locomotion in the insect stage parasite, no detectable defect in directional motility or velocity of cell movement were observed for TbHK2-deficient cells, suggesting that the protein may have a different function in the cell.</abstract><cop>Kidlington</cop><pub>Elsevier Ltd</pub><pmid>22619756</pmid><doi>10.1016/j.ijpara.2012.02.008</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0001-8200-140X</orcidid><orcidid>https://orcid.org/0000-0001-5572-4127</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | International journal for parasitology, 2012-04, Vol.42 (4), p.401-409 |
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| subjects | Antisera antiserum Basal bodies Biochemistry, Molecular Biology Biological and medical sciences bloodstream forms Cell migration cell motility Enzymes Flagella Flagella - chemistry Flagella - enzymology Flagellum fluorescent antibody technique fractionation Fundamental and applied biological sciences. Psychology Gene Deletion Glycolysis Glycosome Glycosomes Hexokinase Hexokinase - analysis Hexokinase - genetics Human protozoal diseases Immunofluorescence Infectious diseases insects Life cycle. Host-agent relationship. Pathogenesis Life Sciences Locomotion Medical sciences Metabolites Microbiology and Parasitology microbodies Microbodies - chemistry Microbodies - enzymology Organelles parasites Parasitic diseases Phosphorylation polypeptides Protozoa Protozoal diseases recombinant proteins Trypanosoma brucei Trypanosoma brucei brucei - chemistry Trypanosoma brucei brucei - enzymology Trypanosoma brucei brucei - genetics Trypanosoma brucei brucei - physiology Trypanosomiasis viability |
| title | Extra-glycosomal localisation of Trypanosoma brucei hexokinase 2 |
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