Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Sander S. van Berkel"'
Autor:
Marloes A. Wijdeven, Remon van Geel, Jorin H. Hoogenboom, Jorge M. M. Verkade, Brian M. G. Janssen, Inge Hurkmans, Laureen de Bever, Sander S. van Berkel, Floris L. van Delft
Publikováno v:
mAbs, Vol 14, Iss 1 (2022)
Antibody-drug conjugates (ADCs) are increasingly powerful medicines for targeted cancer therapy. Inspired by the trend to further improve their therapeutic index by generation of homogenous ADCs, we report here how the clinical-stage GlycoConnect™
Externí odkaz:
https://doaj.org/article/848d309b246a42aca0115d74462db631
Autor:
Jorge M. M. Verkade, Marloes A. Wijdeven, Remon van Geel, Brian M. G. Janssen, Sander S. van Berkel, Floris L. van Delft, Antibodies Editorial Office
Publikováno v:
Antibodies, Vol 7, Iss 3, p 34 (2018)
The conflict of interest section of the published paper [1] has been updated as follows[...]
Externí odkaz:
https://doaj.org/article/fb2f870787b6466e95da8a6ea1543a7a
Autor:
Jorge M. M. Verkade, Marloes A. Wijdeven, Remon van Geel, Brian M. G. Janssen, Sander S. van Berkel, Floris L. van Delft
Publikováno v:
Antibodies, Vol 7, Iss 1, p 12 (2018)
Despite tremendous efforts in the field of targeted cancer therapy with antibody–drug conjugates (ADCs), attrition rates have been high. Historically, the priority in ADC development has been the selection of target, antibody, and toxin, with littl
Externí odkaz:
https://doaj.org/article/3467b0204f6846e79773a9ba2403fa4a
Autor:
Laureen de Bever, Sorraya Popal, Jord van Schaik, Baron Rubahamya, Floris L. van Delft, Greg M. Thurber, Sander S. van Berkel
Publikováno v:
Bioconjugate Chemistry. 34:538-548
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a226ada7c59d0b8e04a021b37862ac2d
https://doi.org/10.1021/acs.bioconjchem.2c00611
https://doi.org/10.1021/acs.bioconjchem.2c00611
Publikováno v:
Drug Discovery Today: Technologies, 30, 3-10
Drug Discovery Today: Technologies 30 (2018)
Drug Discovery Today: Technologies 30 (2018)
Target-specific killing of tumor cells with antibody-drug conjugates (ADCs) is an elegant concept in the continued fight against cancer. However, despite more than 20 years of clinical development, only four ADC have reached market approval, while at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e2da5df7a9f7336b7adeea00e930f8b
https://pubmed.ncbi.nlm.nih.gov/30553518
https://pubmed.ncbi.nlm.nih.gov/30553518
Autor:
Raymond J. Owens, Sander S. van Berkel, Philip Hinchliffe, Timothy R. Walsh, Ramya Salimraj, Magda Kosmopoulou, Michael A. McDonough, James Spencer, Anil Verma, Jürgen Brem, Christopher J. Schofield, Jonathan M. Tyrrell
Publikováno v:
The Febs Journal
Salimraj, R, Hinchliffe, P, Kosmopoulou, M, Tyrrell, J M, Brem, J, van Berkel, S S, Verma, A, Owens, R J, McDonough, M A, Walsh, T R, Schofield, C J & Spencer, J 2019, ' Crystal structures of VIM-1 complexes explain active site heterogeneity in VIM-class metallo-β-lactamases ', FEBS Journal, vol. 286, no. 1, pp. 169-183 . https://doi.org/10.1111/febs.14695
Salimraj, R, Hinchliffe, P, Kosmopoulou, M, Tyrrell, J M, Brem, J, van Berkel, S S, Verma, A, Owens, R J, McDonough, M A, Walsh, T R, Schofield, C J & Spencer, J 2019, ' Crystal structures of VIM-1 complexes explain active site heterogeneity in VIM-class metallo-β-lactamases ', FEBS Journal, vol. 286, no. 1, pp. 169-183 . https://doi.org/10.1111/febs.14695
Metallo-β-Lactamases (MBLs) protect bacteria from almost all β-lactam antibiotics. Verona integron-encoded MBL (VIM) enzymes are among the most clinically important MBLs, with VIM-1 increasing in carbapenem-resistant Enterobacteriaceae (Escherichia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b47eabebd91278b76a1eb701b466b8a
https://pubmed.ncbi.nlm.nih.gov/30430727
https://pubmed.ncbi.nlm.nih.gov/30430727
Autor:
Jürgen Brem, Michael A. McDonough, Sander S. van Berkel, Justin L. P. Benesch, Timothy D. W. Claridge, Christopher J. Schofield, Emily Flashman, Hanna Tarhonskaya, Inga Pfeffer, Anna M. Rydzik, Weston B. Struwe, James Spencer
Publikováno v:
Chemical Science. 6:956-963
Metallo-β-lactamases (MBLs) catalyse the hydrolysis of almost all β-lactam antibiotics. We report biophysical and kinetic studies on the Sao Paulo MBL (SPM-1), which reveal its Zn(II) ion usage and mechanism as characteristic of the clinically impo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a66ce0b6a12644bd1602a63adb8d5e2
https://doi.org/10.1039/c4sc01752h
https://doi.org/10.1039/c4sc01752h
Autor:
Sander S. van Berkel, Christopher J. Schofield, Klaus-Daniel Umland, Wei Shen Aik, Jürgen Brem, Michael A. McDonough, Timothy D. W. Claridge, Anna M. Rydzik, Akane Kawamura, Matthew B. Avison, Ilaria Pettinati, James Spencer
Publikováno v:
Nature Chemistry. 6:1084-1090
The use of β-lactam antibiotics is compromised by resistance, which is provided by β-lactamases belonging to both metallo (MBL)- and serine (SBL)-β-lactamase subfamilies. The rhodanines are one of very few compound classes that inhibit penicillin-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04c25700eb3403476e748b43079cc44b
https://doi.org/10.1038/nchem.2110
https://doi.org/10.1038/nchem.2110
Autor:
Joanne E. Nettleship, Christopher J. Schofield, Jürgen Brem, Jingshan Ren, Sander S. van Berkel, Michael A. McDonough, Timothy D. W. Claridge, Ivanhoe K. H. Leung, Raymond J. Owens, David I. Stuart, Hwanho Choi
Publikováno v:
ACS Chemical Biology. 8:2112-2116
β-Lactam antibiotics react with penicillin binding proteins (PBPs) to form relatively stable acyl-enzyme complexes. We describe structures derived from the reaction of piperacillin with PBP3 (Pseudomonas aeruginosa) including not only the anticipate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb11237e89edd78796e18d74b90c287e
https://doi.org/10.1021/cb400200h
https://doi.org/10.1021/cb400200h
Autor:
Anne Makena, Sander S. van Berkel, Jürgen Brem, Timothy D. W. Claridge, Anna M. Rydzik, Christopher J. Schofield, Inga Pfeffer
Publikováno v:
Angewandte Chemie (International Ed. in English)
The New Delhi metallo-β-lactamase (NDM-1) is involved in the emerging antibiotic resistance problem. Development of metallo-β-lactamases (MBLs) inhibitors has proven challenging, due to their conformational flexibility. Here we report site-selectiv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a58caae2a3f5a41a9fc5d3393e3fc59
https://doi.org/10.1002/anie.201310866
https://doi.org/10.1002/anie.201310866
