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pro vyhledávání: '"E. Neil Cagle"'
Synthetic Erythropoietic Proteins: Tuning Biological Performance by Site-Specific Polymer Attachment
Autor:
E. Neil Cagle, Maia Carnevali, John W. Adamson, Vincent Gueriguian, Carlos E. Bozzini, Gerd G. Kochendoerfer, Sonya Cressman, James A. Bradburne, Ada Kung, M. Con Wiedeke, Heather Porter, Laura Savatski, Stephen M. Stratton, Feng Mao, Haiyan Shao, Donald W. Low, Stephen B. H. Kent, Shiah-Yun Chen, Peter J. Keogh, Hal S. Beilan
Publikováno v:
Chemistry & Biology. 12(3):371-383
SummaryChemical synthesis in combination with precision polymer modification allows the systematic exploration of the effect of protein properties, such as charge and hydrodynamic radius, on potency using defined, homogeneous conjugates. A series of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9455f5c2578524928fd3f5cbf800ce2c
Autor:
Jeffrey S. Nelson, Karen L. Fearon, Annette M. Raible, Vicky Boyd, Michael F. Foy, Andrzej Okruszek, Jeff E. Frediani, Lawrence A. DeDionisio, Sarah N. McCurdy, Mark Q. Nguyen, E. Neil Cagle, Bernard L. Hirschbein
Publikováno v:
Nucleic Acids Research. 26:3813-3824
Oligodeoxynucleotide N3'-->P5' phosphoramidates are promising candidates for antisense therapeutics, as well as for diagnostic applications. We recently reported a new method for the synthesis of these oligonucleotide analogs which makes use of a pho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fe81ede51584566783eab06febd86a2
https://doi.org/10.1093/nar/26.16.3813
https://doi.org/10.1093/nar/26.16.3813
Autor:
Les P. Miranda, Ada Kung, Xavier Paliard, Yvonne Chinn, Rod Garcia, Maia Carnevali, Bill O'dwyer, Di Song, Jill Wilken, Donald E. Low, Ting Kong, Gerd G. Kochendoerfer, Jay Ye, Shiah-Yun Chen, James A. Bradburne, Alex Taekyung Lee, Jason Williams, Haiyan Shao, E. Neil Cagle, Nathalie Fraud
Publikováno v:
Journal of the American Chemical Society. 129(43)
Chemical protein synthesis is important for dissecting the molecular basis of protein function. Here we advance its scope by demonstrating the significant improvement of the multifaceted pharmaceutical profile of small proteins exclusively via a chem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c25beaef3234beabb2cc4151e03a4ad
https://pubmed.ncbi.nlm.nih.gov/17915868
https://pubmed.ncbi.nlm.nih.gov/17915868
Autor:
Vincent Gueriguian, Gerd G. Kochendoerfer, Shiah-Yun Chen, Maia Carnevali, Ting Kong, Jason M. Williams, James A. Bradburne, Xavier Paliard, Haiyan Shao, Janette M. Tack, E. Neil Cagle, Milan M. Crnogorac, Les P. Miranda, David Tumelty
Publikováno v:
Journal of the American Chemical Society. 127(5)
A synthetic strategy that allows for the site-specific attachment of polymers such as poly(ethylene glycol) (PEG) to protein pharmaceuticals is described. PEG was attached to a 67-amino acid fully synthetic CCL-5 (RANTES) analogue at its GAG binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c25e29ae93d555a5302a6ffeeb8f343
https://pubmed.ncbi.nlm.nih.gov/15686348
https://pubmed.ncbi.nlm.nih.gov/15686348
Autor:
Haiyan Shao, Sonya Cressman, John W. Adamson, Vincent Gueriguian, Paolo Botti, Suresh Kalbag, Peter J. Keogh, Laura Savatski, Janice Schindler-Horvat, James A. Bradburne, Donald W. Low, Les P. Miranda, Stephen B. H. Kent, Stacey Traviglia, Feng Mao, Christie L. Hunter, Jay J. Levy, Milan M. Crnogorac, Jill Wilken, Gerd G. Kochendoerfer, Heather Porter, E. Neil Cagle, Ada Kung, Stephen M. Stratton, Shiah-Yun Chen, Maia Carnevali, Jie Tang, M. Con Wiedeke
Publikováno v:
Science (New York, N.Y.). 299(5608)
We report the design and total chemical synthesis of “synthetic erythropoiesis protein” (SEP), a 51-kilodalton protein-polymer construct consisting of a 166-amino–acid polypeptide chain and two covalently attached, branched, and monodisperse po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24473ee266ab5a0bf2ce5d7d6753ca51
https://pubmed.ncbi.nlm.nih.gov/12574628
https://pubmed.ncbi.nlm.nih.gov/12574628
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