Please use this identifier to cite or link to this item: https://doi.org/10.21256/zhaw-19484
Full metadata record
DC FieldValueLanguage
dc.contributor.authorFischer, Thomas-
dc.contributor.authorRiedl, Rainer-
dc.date.accessioned2020-02-19T14:23:33Z-
dc.date.available2020-02-19T14:23:33Z-
dc.date.issued2019-
dc.identifier.issn1420-3049de_CH
dc.identifier.issn1433-1373de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/19484-
dc.description.abstractThe family of matrix metalloproteinases (MMPs) consists of a set of biological targets that are involved in a multitude of severe pathogenic events such as different forms of cancers or arthritis. Modulation of the target class with small molecule drugs has not led to the anticipated success until present, as all clinical trials failed due to unacceptable side effects or a lack of therapeutic outcome. Monoclonal antibodies offer a tremendous therapeutic potential given their high target selectivity and good pharmacokinetic profiles. For the treatment of a variety of diseases there are already antibody therapies available and the number is increasing. Recently, several antibodies were developed for the selective inhibition of single MMPs that showed high potency and were therefore investigated in in vivo studies with promising results. In this review, we highlight the progress that has been achieved toward the design of inhibitory antibodies that successfully modulate MMP-9 and MMP-14.de_CH
dc.language.isoende_CH
dc.publisherMDPIde_CH
dc.relation.ispartofMoleculesde_CH
dc.rightshttp://creativecommons.org/licenses/by/4.0/de_CH
dc.subjectDrug designde_CH
dc.subjectInhibitory antibodyde_CH
dc.subjectMatrix metalloproteinasede_CH
dc.subjectSelectivityde_CH
dc.subjectTissue inhibitors of metalloproteinasede_CH
dc.subjectAmino acid sequencede_CH
dc.subjectAnimalde_CH
dc.subjectMonoclonal antibodyde_CH
dc.subjectBinding sitede_CH
dc.subjectHumande_CH
dc.subjectMatrix metalloproteinase inhibitorsde_CH
dc.subjectMolecular conformationde_CH
dc.subjectMolecular docking simulationde_CH
dc.subjectMolecular dynamics simulationde_CH
dc.subjectProtein bindingde_CH
dc.subjectStructure-activity relationshipde_CH
dc.subject.ddc571: Physiologie und verwandte Themende_CH
dc.titleInhibitory antibodies designed for matrix metalloproteinase modulationde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementLife Sciences und Facility Managementde_CH
dc.identifier.doi10.3390/molecules24122265de_CH
dc.identifier.doi10.21256/zhaw-19484-
dc.identifier.pmid31216704de_CH
zhaw.funding.euNode_CH
zhaw.issue12de_CH
zhaw.originated.zhawYesde_CH
zhaw.pages.start2265de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume24de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
zhaw.webfeedCC Drug Discoveryde_CH
zhaw.author.additionalNode_CH
Appears in collections:Publikationen Life Sciences und Facility Management

Files in This Item:
File Description SizeFormat 
2019_Fischer_Inhibitory-antibodies.pdf2.82 MBAdobe PDFThumbnail
View/Open
Show simple item record
Fischer, T., & Riedl, R. (2019). Inhibitory antibodies designed for matrix metalloproteinase modulation. Molecules, 24(12), 2265. https://doi.org/10.3390/molecules24122265
Fischer, T. and Riedl, R. (2019) ‘Inhibitory antibodies designed for matrix metalloproteinase modulation’, Molecules, 24(12), p. 2265. Available at: https://doi.org/10.3390/molecules24122265.
T. Fischer and R. Riedl, “Inhibitory antibodies designed for matrix metalloproteinase modulation,” Molecules, vol. 24, no. 12, p. 2265, 2019, doi: 10.3390/molecules24122265.
FISCHER, Thomas und Rainer RIEDL, 2019. Inhibitory antibodies designed for matrix metalloproteinase modulation. Molecules. 2019. Bd. 24, Nr. 12, S. 2265. DOI 10.3390/molecules24122265
Fischer, Thomas, and Rainer Riedl. 2019. “Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation.” Molecules 24 (12): 2265. https://doi.org/10.3390/molecules24122265.
Fischer, Thomas, and Rainer Riedl. “Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation.” Molecules, vol. 24, no. 12, 2019, p. 2265, https://doi.org/10.3390/molecules24122265.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.