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l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design
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Zeitschriftentitel: | Molecular BioSystems |
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Personen und Körperschaften: | , , , , |
In: | Molecular BioSystems, 11, 2015, 7, S. 1887-1896 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Royal Society of Chemistry (RSC)
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Schlagwörter: |
author_facet |
Singh, Jasdeep Srivastava, Ankit Jha, Pravin Sinha, Kislay K. Kundu, Bishwajit Singh, Jasdeep Srivastava, Ankit Jha, Pravin Sinha, Kislay K. Kundu, Bishwajit |
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author |
Singh, Jasdeep Srivastava, Ankit Jha, Pravin Sinha, Kislay K. Kundu, Bishwajit |
spellingShingle |
Singh, Jasdeep Srivastava, Ankit Jha, Pravin Sinha, Kislay K. Kundu, Bishwajit Molecular BioSystems l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design Molecular Biology Biotechnology |
author_sort |
singh, jasdeep |
spelling |
Singh, Jasdeep Srivastava, Ankit Jha, Pravin Sinha, Kislay K. Kundu, Bishwajit 1742-206X 1742-2051 Royal Society of Chemistry (RSC) Molecular Biology Biotechnology http://dx.doi.org/10.1039/c5mb00251f <p> <sc>l</sc>-Asparaginases belong to a family of amidohydrolases that catalyze the conversion of <sc>l</sc>-asparagine into <sc>l</sc>-aspartic acid and ammonia.</p> <scp>l</scp>-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design Molecular BioSystems |
doi_str_mv |
10.1039/c5mb00251f |
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Online |
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Biologie Technik |
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Royal Society of Chemistry (RSC), 2015 |
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Royal Society of Chemistry (RSC), 2015 |
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1742-206X 1742-2051 |
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1742-206X 1742-2051 |
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English |
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2015 |
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Royal Society of Chemistry (RSC) |
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Molecular BioSystems |
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49 |
title |
l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_unstemmed |
l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_full |
l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_fullStr |
l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_full_unstemmed |
l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_short |
l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_sort |
<scp>l</scp>-asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
topic |
Molecular Biology Biotechnology |
url |
http://dx.doi.org/10.1039/c5mb00251f |
publishDate |
2015 |
physical |
1887-1896 |
description |
<p>
<sc>l</sc>-Asparaginases belong to a family of amidohydrolases that catalyze the conversion of <sc>l</sc>-asparagine into <sc>l</sc>-aspartic acid and ammonia.</p> |
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Molecular BioSystems |
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author | Singh, Jasdeep, Srivastava, Ankit, Jha, Pravin, Sinha, Kislay K., Kundu, Bishwajit |
author_facet | Singh, Jasdeep, Srivastava, Ankit, Jha, Pravin, Sinha, Kislay K., Kundu, Bishwajit, Singh, Jasdeep, Srivastava, Ankit, Jha, Pravin, Sinha, Kislay K., Kundu, Bishwajit |
author_sort | singh, jasdeep |
container_issue | 7 |
container_start_page | 1887 |
container_title | Molecular BioSystems |
container_volume | 11 |
description | <p> <sc>l</sc>-Asparaginases belong to a family of amidohydrolases that catalyze the conversion of <sc>l</sc>-asparagine into <sc>l</sc>-aspartic acid and ammonia.</p> |
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imprint | Royal Society of Chemistry (RSC), 2015 |
imprint_str_mv | Royal Society of Chemistry (RSC), 2015 |
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language | English |
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match_str | singh2015lasparaginaseasanewmoleculartargetagainstleishmaniasisinsightsintothemechanismofactionandstructurebasedinhibitordesign |
mega_collection | Royal Society of Chemistry (RSC) (CrossRef) |
physical | 1887-1896 |
publishDate | 2015 |
publishDateSort | 2015 |
publisher | Royal Society of Chemistry (RSC) |
record_format | ai |
recordtype | ai |
series | Molecular BioSystems |
source_id | 49 |
spelling | Singh, Jasdeep Srivastava, Ankit Jha, Pravin Sinha, Kislay K. Kundu, Bishwajit 1742-206X 1742-2051 Royal Society of Chemistry (RSC) Molecular Biology Biotechnology http://dx.doi.org/10.1039/c5mb00251f <p> <sc>l</sc>-Asparaginases belong to a family of amidohydrolases that catalyze the conversion of <sc>l</sc>-asparagine into <sc>l</sc>-aspartic acid and ammonia.</p> <scp>l</scp>-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design Molecular BioSystems |
spellingShingle | Singh, Jasdeep, Srivastava, Ankit, Jha, Pravin, Sinha, Kislay K., Kundu, Bishwajit, Molecular BioSystems, l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design, Molecular Biology, Biotechnology |
title | l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_full | l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_fullStr | l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_full_unstemmed | l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_short | l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_sort | <scp>l</scp>-asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
title_unstemmed | l-Asparaginase as a new molecular target against leishmaniasis: insights into the mechanism of action and structure-based inhibitor design |
topic | Molecular Biology, Biotechnology |
url | http://dx.doi.org/10.1039/c5mb00251f |