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Designing an improved T-cell mobilising CXCL10 mutant through enhanced GAG binding affinity.

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Title: Designing an improved T-cell mobilising CXCL10 mutant through enhanced GAG binding affinity.
Authors: Gerlza T; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria., Nagele M; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria., Gschwandtner M; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria., Winkler S; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria., Kungl A; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria.; Antagonis Biotherapeutics GmbH, Strasserhofweg 77a, Graz A-8045, Austria.
Source: Protein engineering, design & selection : PEDS [Protein Eng Des Sel] 2019 Dec 31; Vol. 32 (8), pp. 367-373.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Oxford University Press Country of Publication: England NLM ID: 101186484 Publication Model: Print Cited Medium: Internet ISSN: 1741-0134 (Electronic) Linking ISSN: 17410126 NLM ISO Abbreviation: Protein Eng Des Sel Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Designing an improved T-cell mobilising CXCL10 mutant through enhanced GAG binding affinity.
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  Data: <searchLink fieldCode="AU" term="%22Gerlza+T%22">Gerlza T</searchLink>; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria.<br /><searchLink fieldCode="AU" term="%22Nagele+M%22">Nagele M</searchLink>; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria.<br /><searchLink fieldCode="AU" term="%22Gschwandtner+M%22">Gschwandtner M</searchLink>; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria.<br /><searchLink fieldCode="AU" term="%22Winkler+S%22">Winkler S</searchLink>; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria.<br /><searchLink fieldCode="AU" term="%22Kungl+A%22">Kungl A</searchLink>; Institute of Pharmaceutical Sciences, Department of pharmaceutical chemistry, Karl-Franzens-University Graz, Universitätsplatz 1, Graz A-8010, Austria.; Antagonis Biotherapeutics GmbH, Strasserhofweg 77a, Graz A-8045, Austria.
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  Data: <searchLink fieldCode="JN" term="%22101186484%22">Protein engineering, design & selection : PEDS</searchLink> [Protein Eng Des Sel] 2019 Dec 31; Vol. 32 (8), pp. 367-373.
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  Data: Journal Article; Research Support, Non-U.S. Gov't
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Oxford+University+Press%22">Oxford University Press </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>101186484 <i>Publication Model: </i>Print <i>Cited Medium: </i>Internet <i>ISSN: </i>1741-0134 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2217410126%22">17410126 </searchLink><i>NLM ISO Abbreviation: </i>Protein Eng Des Sel <i>Subsets: </i>MEDLINE
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        Value: 10.1093/protein/gzz043
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      – Code: eng
        Text: English
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        StartPage: 367
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      – TitleFull: Designing an improved T-cell mobilising CXCL10 mutant through enhanced GAG binding affinity.
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            NameFull: Gerlza T
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            NameFull: Nagele M
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            NameFull: Gschwandtner M
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            NameFull: Winkler S
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            – D: 31
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              Text: 2019 Dec 31
              Type: published
              Y: 2019
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              Value: 32
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              Value: 8
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            – TitleFull: Protein engineering, design & selection : PEDS
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