{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nguyen HA"],"funding":["U.S. Department of Veterans Affairs (VA)","BLRD VA","NIBIB NIH HHS","Fonds Wetenschappelijk Onderzoek (FWO)","Vlaamse Liga Tegen Kanker (VLK)","European Hematology Association","Stichting Tegen Kanker (Fondation Contre le Cancer)","HHS | NIH | National Institute of Biomedical Imaging and Bioengineering (NIBIB)"],"pagination":["1549-1560"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5856643"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["78(6)"],"pubmed_abstract":["Acute lymphoblastic leukemia (ALL) is the most common type of pediatric cancer, although about 4 of every 10 cases occur in adults. The enzyme drug l-asparaginase serves as a cornerstone of ALL therapy and exploits the asparagine dependency of ALL cells. In addition to hydrolyzing the amino acid l-asparagine, all FDA-approved l-asparaginases also have significant l-glutaminase coactivity. Since several reports suggest that l-glutamine depletion correlates with many of the side effects of these drugs, enzyme variants with reduced l-glutaminase coactivity might be clinically beneficial if their antileukemic activity would be preserved. Here we show that novel low l-glutaminase variants developed on the backbone of the FDA-approved <i>Erwinia chrysanthemi</i> l-asparaginase were highly effica"],"journal":["Cancer research"],"pubmed_title":["A Novel l-Asparaginase with low l-Glutaminase Coactivity Is Highly Efficacious against Both T- and B-cell Acute Lymphoblastic Leukemias &lt;i&gt;In Vivo&lt;/i&gt;."],"pmcid":["PMC5856643"],"funding_grant_id":["I01 BX001919","365Y9115W","365W3415W","FWO17/PDO/111","TRTH104","I01BX001919","3G0C4713","RO1 EB013685","R01 EB013685"],"pubmed_authors":["Bosland MC","Peirs S","Liu L","Lammens T","Merrill BJ","De Moerloose B","Schlicht MJ","Lyubimov AV","Saunthararajah Y","Kabirov KK","Caffrey M","Mahmud DL","Goossens S","Schalk AM","Lavie A","Antanasijevic A","Van Vlierberghe P","Zhang JY","Nguyen HA","Rondelli D","Kajdacsy-Balla A","Su Y","Mondelaers V","Oh A"],"additional_accession":[]},"is_claimable":false,"name":"A Novel l-Asparaginase with low l-Glutaminase Coactivity Is Highly Efficacious against Both T- and B-cell Acute Lymphoblastic Leukemias &lt;i&gt;In Vivo&lt;/i&gt;.","description":"Acute lymphoblastic leukemia (ALL) is the most common type of pediatric cancer, although about 4 of every 10 cases occur in adults. The enzyme drug l-asparaginase serves as a cornerstone of ALL therapy and exploits the asparagine dependency of ALL cells. In addition to hydrolyzing the amino acid l-asparagine, all FDA-approved l-asparaginases also have significant l-glutaminase coactivity. Since several reports suggest that l-glutamine depletion correlates with many of the side effects of these drugs, enzyme variants with reduced l-glutaminase coactivity might be clinically beneficial if their antileukemic activity would be preserved. Here we show that novel low l-glutaminase variants developed on the backbone of the FDA-approved <i>Erwinia chrysanthemi</i> l-asparaginase were highly effica","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Mar","modification":"2026-06-04T06:45:09.615Z","creation":"2019-08-04T07:03:08Z"},"accession":"S-EPMC5856643","cross_references":{"pubmed":["29343523"],"doi":["10.1158/0008-5472.CAN-17-2106","10.1158/0008-5472.can-17-2106"]}}