Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Patrick Dennler"'
Publikováno v:
Antibodies, Vol 4, Iss 3, Pp 197-224 (2015)
Monoclonal antibodies (mAbs) and their derivatives are currently the fastest growing class of therapeutics. Even if naked antibodies have proven their value as successful biopharmaceuticals, they suffer from some limitations. To overcome suboptimal t
Externí odkaz:
https://doaj.org/article/a308793d9c864f05960d8a1ed18357f0
Autor:
Jürgen Grünberg, Simone Jeger, Dikran Sarko, Patrick Dennler, Kurt Zimmermann, Walter Mier, Roger Schibli
Publikováno v:
PLoS ONE, Vol 8, Iss 4, p e60350 (2013)
Site-specific enzymatic reactions with microbial transglutaminase (mTGase) lead to a homogenous species of immunoconjugates with a defined ligand/antibody ratio. In the present study, we have investigated the influence of different numbers of 1,4,7,1
Externí odkaz:
https://doaj.org/article/d4184795e8a54b6cb345f953962a847c
Autor:
Selena Milicevic Sephton, Patrick Dennler, Dominique S. Leutwiler, Linjing Mu, Roger Schibli, Stefanie D. Krämer, Simon M. Ametamey
Publikováno v:
CHIMIA, Vol 66, Iss 4 (2012)
Involvement of metabotropic glutamate receptor subtype 5 (mGluR5) in physiological and pathophysiological processes in the brain has been demonstrated, and hence mGluR5 has emerged as an important drug target. [11C]-ABP688 is clinically the most succ
Externí odkaz:
https://doaj.org/article/de6c5f8757e646eebffcefc55dcb1dd0
Publikováno v:
Antibodies, 4 (3)
Antibodies, Vol 4, Iss 3, Pp 197-224 (2015)
Antibodies, Vol 4, Iss 3, Pp 197-224 (2015)
Monoclonal antibodies (mAbs) and their derivatives are currently the fastest growing class of therapeutics. Even if naked antibodies have proven their value as successful biopharmaceuticals, they suffer from some limitations. To overcome suboptimal t
Publikováno v:
Chembiochem : a European journal of chemical biology
Antibody-like proteins selected from discovery platforms are preferentially functionalized by site-specific modification as this approach preserves the binding abilities and allows a side-by-side comparison of multiple conjugates. Here we present an
Autor:
C. Delcambre, Christian Belmant, M. Sapet, N. Viaud, C. Bonnafous, N. Schneider, Eliane Fischer, Angelique Boedec, Florence Lhospice, Patrick Dennler, Roger Schibli, H. Rispaud, S. Savard-Chambard, François Romagné, Agnès Represa, C. Paturel, Laurent Gauthier, S. Ingoure, Aristeidis Chiotellis, Delphine Bregeon
Publikováno v:
Molecular pharmaceutics
Antibody-drug conjugates (ADCs) have demonstrated clinical benefits that have led to the recent FDA approval of KADCYLA and ADCETRIS. Most ADCs that are currently in clinical use or development, including ADCETRIS, are produced by chemical conjugatio
Autor:
Patrick Dennler, Aristeidis Chiotellis, Laurent Gauthier, Florence Lhospice, François Romagné, Eliane Fischer, Delphine Bregeon, Christian Belmant, Roger Schibli
Publikováno v:
Schibli Roger
Most chemical techniques used to produce antibody-drug conjugates (ADCs) result in a heterogeneous mixture of species with variable drug-to-antibody ratios (DAR) which will potentially display different pharmacokinetics, stability, and safety profile
Autor:
Romana, Meletta, Adrienne, Müller Herde, Patrick, Dennler, Eliane, Fischer, Roger, Schibli, Stefanie D, Krämer
Publikováno v:
EJNMMI Research
Background The inflammatory nature of atherosclerosis provides a broad range of potential molecular targets for atherosclerosis imaging. Growing interest is focused on targets related to plaque vulnerability such as the co-stimulatory molecules CD80
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1045
Enzymatic posttranslational modification of proteins permits more precise control over conjugation site than chemical modification of reactive amino acid side chains. Ideally, protein modification by an enzyme yields completely homogeneous conjugates
Publikováno v:
Methods in Molecular Biology ISBN: 9781627035408
Enzymatic posttranslational modification of proteins permits more precise control over conjugation site than chemical modification of reactive amino acid side chains. Ideally, protein modification by an enzyme yields completely homogeneous conjugates
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e9d9afe9ed4fa6032ab3e469a365f06
https://doi.org/10.1007/978-1-62703-541-5_12
https://doi.org/10.1007/978-1-62703-541-5_12