Zobrazeno 1 - 10
of 238
pro vyhledávání: '"Tim, Edmunds"'
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
Genetic alterations in the protein acid sphingomyelinase (ASM) lead to ASM deficiency and have been associated with Niemann–Pick disease. Here, the authors report the crystal structures of ASM alone and bound to its product, and discuss the catalyt
Externí odkaz:
https://doaj.org/article/eda182e9ef134dd2b69154514ce76ea7
Autor:
Cécile Capdevila, Christophe Loux, Catherine Lawrence, Jean-Piere Marquette, Magali Mathieu, Jacques Dumas, Paul Ferrari, Huawei Qiu, Bruno Dumas, Josiane Le Parc, Clark Pan, Ronnie Wei, Mark Levine, Russell Bigelow, Tim Edmunds, Aaron Moulin, Alexey Rak, Christine Hamel, Julie Bird
Publikováno v:
Protein Science. 23:1698-1707
Various important biological pathways are modulated by TGFβ isoforms; as such they are potential targets for therapeutic intervention. Fresolimumab, also known as GC1008, is a pan-TGFβ neutralizing antibody that has been tested clinically for sever
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59d962602ccf8d97b943d8b22a97f36a
https://doi.org/10.1002/pro.2548
https://doi.org/10.1002/pro.2548
Autor:
Robert J. Mattaliano, Michelle Busch, Nathan Jones, Jesse Keegan, Michael L. Hayes, Mark Plavsic, Kate Zhang, Weichang Zhou, Peng Pan, John M. McPherson, Yongchang Qiu, Tim Edmunds
Publikováno v:
Biotechnology and Bioengineering. 110:1342-1353
The prevention of adventitious agent contamination is a top priority throughout the entire biopharmaceutical production process. For example, although viral contamination of cell banks or cell cultures is rare, it can result in serious consequences (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5345b8db7c30a647248a56192e3318d
https://doi.org/10.1002/bit.24791
https://doi.org/10.1002/bit.24791
Publikováno v:
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
Nature Communications, Vol 7, Iss 1, Pp 1-10 (2016)
Acid sphingomyelinase (ASM) hydrolyzes sphingomyelin to ceramide and phosphocholine, essential components of myelin in neurons. Genetic alterations in ASM lead to ASM deficiency (ASMD) and have been linked to Niemann–Pick disease types A and B. Oli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7acd7b33cd9859b308f3226bddbde0f3
https://doi.org/10.1038/ncomms13082
https://doi.org/10.1038/ncomms13082
Autor:
Emily B. Cohen, Karen Lee, Charles J Morgan, Heather Hughes, Kristen Barranco, Elizabeth Brunyak, Tim Edmunds
Publikováno v:
The AAPS Journal. 11:335-341
In this study, we have investigated sedimentation velocity ultracentrifugation (AUC-SV), size exclusion chromatography (SEC), and circular dichroism (CD) methods for the detection and quantitation of protein aggregates using recombinant acid alpha-gl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::781214d157f91a08f6e83bf889389d5c
https://doi.org/10.1208/s12248-009-9108-1
https://doi.org/10.1208/s12248-009-9108-1
Autor:
Scott M. Van Patten, Tim Edmunds
Publikováno v:
Post-translational Modification of Protein Biopharmaceuticals
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::300dcbd81833b75cb86c0ed318e76359
https://doi.org/10.1002/9783527626601.ch13
https://doi.org/10.1002/9783527626601.ch13
Autor:
Lihui Hou, Denise M. Honey, Qun Zhou, Tim Edmunds, James E. Stefano, Clark Pan, Anna Park, Josephine Kyazike
Publikováno v:
Journal of Controlled Release. 135:113-118
Lysosomal storage diseases arise from a genetic loss-of-function defect in enzymes mediating key catabolic steps resulting in accumulation of substrate within the lysosome. Treatment of several of these disorders has been achieved by enzyme replaceme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d808c4bff8b6498a94bba793d105fd4d
https://doi.org/10.1016/j.jconrel.2008.12.006
https://doi.org/10.1016/j.jconrel.2008.12.006
Autor:
Tim Edmunds, Naho Ohyanagi, Kohji Itoh, Kaori Fujishima, Kobayashi Toshihide, Tadayasu Togawa, Daisuke Tsuji, Masahiko Ikekita, Kanako Sugawara, Ikuo Kawashima, Michiru Yoshimizu, Youichi Tajima, Sei-ichi Aikawa, Fumiko Matsuzawa, Kunihiko Iwamoto, Toshihiro Suzuki, Hitoshi Sakuraba, Kazuki Ohno
Publikováno v:
Clinica Chimica Acta. 391:68-73
Background Recently, enzyme enhancement therapy (EET) for Pompe disease involving imino sugars, which act as potential inhibitors of acid α-glucosidases in vitro , to improve the stability and/or transportation of mutant acid α-glucosidases in cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2293f690368010fe83c4ecfdf0f3f5c
https://doi.org/10.1016/j.cca.2008.02.014
https://doi.org/10.1016/j.cca.2008.02.014
LIMP-2 Is a Receptor for Lysosomal Mannose-6-Phosphate-Independent Targeting of β-Glucocerebrosidase
Autor:
David Reczek, Tim Edmunds, Scott M. Van Patten, Judith Blanz, Paul Saftig, William Brondyk, Heather Hughes, Jenny Schröder, Xiaoying Jin, Michael Schwake
Publikováno v:
Cell. 131:770-783
beta-glucocerebrosidase, the enzyme defective in Gaucher disease, is targeted to the lysosome independently of the mannose-6-phosphate receptor. Affinity-chromatography experiments revealed that the lysosomal integral membrane protein LIMP-2 is a spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc7a8f9650bbfe1a6f60cec75cc89942
https://doi.org/10.1016/j.cell.2007.10.018
https://doi.org/10.1016/j.cell.2007.10.018
Autor:
Tim Edmunds, Scott M. Van Patten, Heather Hughes, Michael R. Huff, Peter A. Piepenhagen, David Reczek, James Waire, Paul V. Ward, Huawei Qiu, Chandrashekar Ganesa, Joseph P. Kutzko
Publikováno v:
Glycobiology. 17:467-478
Recombinant human glucocerebrosidase (imiglucerase, Cerezyme ® ) is used in enzyme replacement therapy for Gaucher disease. Complex oligosaccharides present on Chinese hamster ovary cell-expressed glucocerebrosidase (GCase) are enzymatically remodel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4337bd713ea307e7ea15940d25d6c8bf
https://doi.org/10.1093/glycob/cwm008
https://doi.org/10.1093/glycob/cwm008