Zobrazeno 1 - 10 of 11 pro vyhledávání: '"Daniel G. Greene"'
1
Nanocrystalline protein domains via salting-out
Autor: Norman J. Wagner, Abraham M. Lenhoff, Daniel G. Greene, Stanley I. Sandler, Shannon Modla
Publikováno v: Acta Crystallogr F Struct Biol Commun
Protein salting-out is a well established phenomenon that in many cases leads to amorphous structures and protein gels, which are usually not considered to be useful for protein structure determination. Here, microstructural measurements of several d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d2339acb138409753e58f26c59e7b1c
https://europepmc.org/articles/PMC8561819/
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3
Structural characterization and developability assessment of sustained release hydrogels for rapid implementation during preclinical studies
Autor: Daniel G. Greene, Kaitlyn Wendl, Hyunsoo Park, Scott Sherman, Roman Shimanovich, Darren L. Reid, Prashant Agarwal, Leonela Vega
Publikováno v: European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences. 158
Sustained-release formulations are important tools to convert efficacious molecules into therapeutic products. Hydrogels enable the rapid assessment of sustained-release strategies, which are important during preclinical development where drug quanti
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f87e6649e55ffd81d909043e13380b32
https://pubmed.ncbi.nlm.nih.gov/33359482
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5
A critical examination of the decoupling approximation for small-angle scattering from hard ellipsoids of revolution
Autor: Abraham M. Lenhoff, Daniel V. Ferraro, Daniel G. Greene, Norman J. Wagner
Publikováno v: Journal of Applied Crystallography. 49:1734-1739
The decoupling approximation, proposed by Kotlarchyk & Chen [J. Chem. Phys. (1983), 79, 2461–2469], is a first-order correction to the experimentally determined apparent structure factor that is necessary because of concentration effects in polydis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9b5e011dee00214d0a595e81ae58834a
https://doi.org/10.1107/s1600576716012929
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6
Mechanisms of precipitate formation during the purification of an Fc-fusion protein
Autor: Zheng Jian Li, Norman J. Wagner, Sanchayita Ghose, Jing Guo, Xuankuo Xu, Nripen Singh, Kelvin H. Lee, Abraham M. Lenhoff, Leila H. Choe, Steven J. Traylor, Lye Lin Lock, Shannon Modla, Daniel G. Greene
Publikováno v: Biotechnology and Bioengineering
Protein precipitates that arise during bioprocessing can cause manufacturing challenges, but they can also aid in clearance of host-cell protein (HCP) and DNA impurities. Such precipitates differ from many protein precipitates that have been studied
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d42f3b45f3b35a8e0cc3ecbfac4fdfa8
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7
Local Crystalline Structure in an Amorphous Protein Dense Phase
Autor: Shannon Modla, Stanley I. Sandler, Norman J. Wagner, Abraham M. Lenhoff, Daniel G. Greene
Publikováno v: Biophysical Journal. 109(8):1716-1723
Proteins exhibit a variety of dense phases ranging from gels, aggregates, and precipitates to crystalline phases and dense liquids. Although the structure of the crystalline phase is known in atomistic detail, little attention has been paid to noncry
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2a8af27aafc1d6219ff0755ddddb208
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8
Impact of polymer geometry on the interactions of protein-PEG conjugates
Autor: Nikhil Peer, Whitney Shatz, Daniel G. Greene, Isidro E. Zarraga, Jonathan Zarzar, Brian McGarry, Yun Liu, Rosalynn Taing
Publikováno v: Biophysical chemistry. 236
The conjugation of high molecular weight polyethylene glycol (PEG) to an active pharmaceutical ingredient (API) is an attractive strategy for the modification of biophysical and biodistribution properties of the API. Indeed, several therapeutic prote
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87465eced778ec53f4c91aed79043bcd
https://pubmed.ncbi.nlm.nih.gov/29331201
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