Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Marianne Schimpl"'
Autor:
Vasiliki Paraskevopoulou, Marianne Schimpl, Ross C. Overman, Snow Stolnik, Yajie Chen, Linh Nguyen, G. Sebastiaan Winkler, Paul Gellert, John S. Klassen, Franco H. Falcone
Publikováno v:
Current Research in Structural Biology, Vol 3, Iss , Pp 19-29 (2021)
Helicobacter pylori (H. pylori) uses several outer membrane proteins for adhering to its host's gastric mucosa, an important step in establishing and preserving colonization. Several adhesins (SabA, BabA, HopQ) have been characterized in terms of the
Externí odkaz:
https://doaj.org/article/8195fe10d9e7491586ad5fba6c9ba824
Autor:
Villo Muha, Ritchie Williamson, Rachel Hills, Alison D. McNeilly, Thomas G. McWilliams, Jana Alonso, Marianne Schimpl, Aneika C. Leney, Albert J. R. Heck, Calum Sutherland, Kevin D. Read, Rory J. McCrimmon, Simon P. Brooks, Daan M. F. van Aalten
Publikováno v:
Open Biology, Vol 9, Iss 11 (2019)
O-GlcNAcylation is an abundant post-translational modification in the nervous system, linked to both neurodevelopmental and neurodegenerative disease. However, the mechanistic links between these phenotypes and site-specific O-GlcNAcylation remain la
Externí odkaz:
https://doaj.org/article/9e64e5af2f29476f9e4eeb84d52a4cc3
Autor:
Lotte van Beek, Éilís McClay, Saleha Patel, Marianne Schimpl, Laura Spagnolo, Taiana Maia de Oliveira
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 10, p 5112 (2021)
Poly (ADP-ribose) polymerases (PARP) 1-3 are well-known multi-domain enzymes, catalysing the covalent modification of proteins, DNA, and themselves. They attach mono- or poly-ADP-ribose to targets using NAD+ as a substrate. Poly-ADP-ribosylation (PAR
Externí odkaz:
https://doaj.org/article/330724b4ce614e97af4b4e2129d27fe4
Autor:
Daniel Mariappa, Xiaowei Zheng, Marianne Schimpl, Olawale Raimi, Andrew T. Ferenbach, H.-Arno J. Müller, Daan M. F. van Aalten
Publikováno v:
Open Biology, Vol 5, Iss 12 (2015)
Post-translational modification of intracellular proteins with O-linked N-acetylglucosamine (O-GlcNAc) catalysed by O-GlcNAc transferase (OGT) has been linked to regulation of diverse cellular functions. OGT possesses a C-terminal glycosyltransferase
Externí odkaz:
https://doaj.org/article/b94e298faec4481fb80bf832bb42dfae
Autor:
Rachael Rutkowski, Robin Dickinson, Graeme Stewart, Ashley Craig, Marianne Schimpl, Stephen M Keyse, Anton Gartner
Publikováno v:
PLoS Genetics, Vol 7, Iss 8, p e1002238 (2011)
Maintaining genome stability in the germline is thought to be an evolutionarily ancient role of the p53 family. The sole Caenorhabditis elegans p53 family member CEP-1 is required for apoptosis induction in meiotic, late-stage pachytene germ cells in
Externí odkaz:
https://doaj.org/article/68ea7534cb0b420ebf86f25c0e65f16c
Autor:
Frederick W, Goldberg, Attilla K T, Ting, David, Beattie, Gillian M, Lamont, Charlene, Fallan, M Raymond V, Finlay, Beth, Williamson, Marianne, Schimpl, Alexander R, Harmer, Oladipupo B, Adeyemi, Pär, Nordell, Anna S, Cronin, Mercedes, Vazquez-Chantada, Derek, Barratt, Antonio, Ramos-Montoya, Elaine B, Cadogan, Barry R, Davies
Publikováno v:
ACS medicinal chemistry letters. 13(8)
The DNA-PK complex is activated by double-strand DNA breaks and regulates the non-homologous end-joining repair pathway; thus, targeting DNA-PK by inhibiting the DNA-PK catalytic subunit (DNA-PKcs) is potentially a useful therapeutic approach for onc
Autor:
Frederick W. Goldberg, Attilla K. T. Ting, David Beattie, Gillian M. Lamont, Charlene Fallan, M. Raymond V. Finlay, Beth Williamson, Marianne Schimpl, Alexander R. Harmer, Oladipupo B. Adeyemi, Pär Nordell, Anna S. Cronin, Mercedes Vazquez-Chantada, Derek Barratt, Antonio Ramos-Montoya, Elaine B. Cadogan, Barry R. Davies
Publikováno v:
ACS Medicinal Chemistry Letters. 13:1295-1301
Autor:
Jeffrey W. Johannes, Fiona Pachl, Amber Balazs, Tieguang Yao, C. Larner, Lisa McWilliams, Marianne Schimpl, Scott W. Martin, Kevin J. Embrey, Tom D. Heightman, Paul Hemsley, Jonathan P. Orme, Derek Barratt, Giuditta Illuzzi, Andrew Madin, Paolo Di Fruscia, Avipsa Ghosh, Martin J. Packer, Scott D. Edmondson, Elisabetta Leo, Xiaolan Zheng, Matthew D. Chuba, Xiaohui Pei, Mark J. O'Connor, Verity Talbot, Ke Zhang, Stephen Fawell, Elizabeth Underwood, Anna Staniszewska, Lina Liu, Lin Xue, Sonja J. Gill, Anders Gunnarsson, Andrew Pike, Susan E. Critchlow, Jeffrey G. Varnes, Andrew X. Zhang, Sébastien L. Degorce, J. Lane, Sudhir M. Hande, Hongyao She, Sabina Cosulich, Michal Bista
Publikováno v:
Journal of Medicinal Chemistry. 64:14498-14512
Poly-ADP-ribose-polymerase (PARP) inhibitors have achieved regulatory approval in oncology for homologous recombination repair deficient tumors including BRCA mutation. However, some have failed in combination with first-line chemotherapies, usually
Autor:
Edward J. Hennessy, Marianne Schimpl, Emma Rivers, Paul D. Smith, Elizabeth Hardaker, Ann T. Doherty, Nichola L. Davies, Jon Travers, Qianxiu Zhu, Beth Williamson, Graham Smith, Lorraine Mooney, Helen Musgrove, Kristin Goldberg, Muireann Coen, Anne-Laure Lainé, Xiefeng Jiang, Philip Hopcroft, Yuting Zheng, Robert I Troup, George Hodgson, Nicola Lindsay, Lindsay McMurray, Olga Collingwood, Stephen D. Wilkinson, Sharon Tentarelli, Guang He, Philip B. Rawlins, Roshini Markandu, Jon Winter-Holt, Josephine Walton, Ankur Karmokar, J. Willem M. Nissink, Yumeng Mao, Dejian Yang, Alexander Pflug, Gary Fairley, Scott Boyd, Cheng Wang, Anne Jackson, Martin R. Brown, William McCoull, Neville McLean, Venkatesh Pilla Reddy
Publikováno v:
Journal of Medicinal Chemistry. 64:13524-13539
Inhibition of Mer and Axl kinases has been implicated as a potential way to improve the efficacy of current immuno-oncology therapeutics by restoring the innate immune response in the tumor microenvironment. Highly selective dual Mer/Axl kinase inhib
Author Correction: The active site of O-GlcNAc transferase imposes constraints on substrate sequence
Autor:
Shalini Pathak, Jana Alonso, Marianne Schimpl, Karim Rafie, David E. Blair, Vladimir S. Borodkin, Alexander W. Schüttelkopf, Osama Albarbarawi, Daan M. F. van Aalten
Publikováno v:
Nature Structural & Molecular Biology. 30:564-564