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Search Publications by: Robert Brinson (Fed)

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Displaying 26 - 50 of 72

Characterization of the internal translation initiation region in monoclonal antibodies expressed in Escherichia coli

October 11, 2019
Author(s)
Erik M. Leith, William Brad O'Dell, Na Ke, Colleen McClung, Mehmet Berkmen, Christina Bergonzo, Robert G. Brinson, Zvi Kelman
Monoclonal antibodies (mAbs) represent an important platform for the development of biotherapeutic products. While most mAbs are produced in mammalian cells, there are several examples of mAbs made in Escherichia coli, including therapeutic fragments. When

Structural Insights into DNA-Stabilized Silver Clusters

May 10, 2019
Author(s)
Danielle Schultz, Robert G. Brinson, Fahriye N. Sari, Jeffrey Fagan, Christina Bergonzo, Nancy Lin, Joy Dunkers
The structure and dynamics of Ag complexes derived from single stranded DNA (ssDNA) is less understood than their double stranded (dsDNA) counterparts despite their great promise as fluorescent biological probes and sensors. In this work, we seek new

Enabling adoption of 2D-NMR for the higher order structure assessment of monoclonal antibody therapeutics

January 1, 2019
Author(s)
Robert G. Brinson, John P. Marino, Frank Delaglio, Luke W. Arbogast, Ryan M. Evans, Anthony J. Kearsley, Yves Aubin, Gregory Pierens, Xinying Jia, David Keizer, Jonas Stahle, Goran Widmalm, Chad Lawrence, Patrick Reardon, John Cort, Koichi Kato, Stuart Parnham, Andreas Blomgren, Torgny Rundlof, Kang Chen, David Keire, Thea Suter-Stahel, Gerhard Wider, Donna Baldisseri, Julie Wu, Mats Wikstrom, Medhi Mobli
Of the top ten drugs on the global market in 2016, seven of them are biologics with a combined market value of over US$60 billion. Moreover, around 2,800 biopharmaceuticals, many of them monoclonal antibodies (mAbs), are in some stage of clinical

Platform development for expression and purification of stable isotope labeled monoclonal antibodies in Escherichia coli

October 1, 2018
Author(s)
Prasad T. Reddy, Robert G. Brinson, James T. Hoopes, Colleen McClung, Na Ke, Lila Kashi, Mehmet Berkmen
Proteins labeled with stable isotopes play an important role in structural and biophysical studies including nuclear magnetic resonance, small angle neutron scattering, neutron reflectometry, quantitative mass spec and more. The most common and cost

Platform development for expression and purification of stable isotope labeled monoclonal antibodies in Escherichia coli

October 1, 2018
Author(s)
Robert Brinson, James T. Hoopes, Colleen McClung, Na Ke, Lila Kashi, Mehmet Berkmen, Zvi Kelman, Prasad T. Reddy
Proteins labeled with stable isotopes play an important role in structural and biophysical studies including nuclear magnetic resonance, small angle neutron scattering, neutron reflectometry, quantitative mass spec and more. The most common and cost

Tissue Inhibitor of Metalloprotease-2: bioprocess development, physicochemical, biochemical and biological characterization of highly expressed recombinant protein

December 1, 2017
Author(s)
Ananda Chowdhury, Robert G. Brinson, Beiyang Wei, William G. Stetler-Stevenson
Tissue Inhibitor of Metalloprotease -2 (TIMP-2) is a secreted, 21 kDa, multifunctional protein. It was first described as an endogenous inhibitor of matrix metalloproteases (MMPs) that prevents protease-mediated breakdown of the extracellular matrix often

Non-Uniform Sampling for All: More Spectral Quality, Less Measurement Time

June 30, 2017
Author(s)
Frank Delaglio, Gregory S. Walker, Kathleen A. Farley, Raman Sharma, Jeffrey C. Hoch, Luke Arbogast, Robert Brinson, John Marino
Nuclear Magnetic Resonance (NMR) spectroscopy is an indispensable tool in pharmaceutical science, with uses in drug discovery, development, and manufacturing. Non-Uniform Sampling (NUS) is an acquisition method for NMR experiments with two or more

Application of 2D-NMR with Room Temperature NMR Probes for the Assessment of the Higher Order Structure of Filgrastim

January 15, 2017
Author(s)
Robert G. Brinson, Houman Ghasriani, Derek Hodgson, Adams Kristie, Ian McEwen, Kang Chen, Yves Aubin, John P. Marino
The higher order structure (HOS) of biotherapeutics is a critical quality attribute that can be evaluated by nuclear magnetic resonance (NMR) spectroscopy at atomic resolution. NMR spectral mapping of HOS can be used to establish HOS consistency of a