Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ranajoy Majumdar"'
Autor:
Anjul Khadria, Chad D. Paavola, Konstantin Maslov, Francisco A. Valenzuela, Andrea E. Sperry, Amy L. Cox, Rui Cao, Junhui Shi, Patricia L. Brown-Augsburger, Emmanuel Lozano, Ross L. Blankenship, Ranajoy Majumdar, Scott A. Bradley, John M. Beals, Sunday S. Oladipupo, Lihong V. Wang
Publikováno v:
Molecular Metabolism, Vol 62, Iss , Pp 101522- (2022)
Objective: Ultra-rapid insulin formulations control postprandial hyperglycemia; however, inadequate understanding of injection site absorption mechanisms is limiting further advancement. We used photoacoustic imaging to investigate the injection site
Externí odkaz:
https://doaj.org/article/4e686fb7d1214da195f3ad2aa1b7871d
Autor:
Amjad A. Chowdhury, Neha Manohar, Marta A. Witek, Mahlet A. Woldeyes, Ranajoy Majumdar, Ken K. Qian, William D. Kimball, Shifeng Xu, Alfredo Lanzaro, Thomas M. Truskett, Keith P. Johnston
Publikováno v:
Molecular Pharmaceutics.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a31c515821aaef29e3bc232ece18943d
https://doi.org/10.1021/acs.molpharmaceut.3c00023
https://doi.org/10.1021/acs.molpharmaceut.3c00023
Autor:
George M. Bou-Assaf, Ivan L. Budyak, Michael Brenowitz, Eric S. Day, David Hayes, John Hill, Ranajoy Majumdar, Paola Ringhieri, Peter Schuck, Jasper C. Lin
Publikováno v:
J Pharm Sci
Analytical ultracentrifugation (AUC) is a critical analytical tool supporting the development and manufacture of protein therapeutics. AUC is routinely used as an assay orthogonal to size exclusion chromatography for aggregate quantitation. This arti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e43b967f463b00c953dcfcd1b5533d9
https://europepmc.org/articles/PMC9232890/
https://europepmc.org/articles/PMC9232890/
Publikováno v:
Journal of Pharmaceutical Sciences. 107:1498-1511
This work compares the conformational stability, backbone flexibility, and aggregation propensity of monomer and dimer fractions of an IgG1 monoclonal antibody (mAb) generated on UVA light exposure for up to 72 h collected by preparative size-exclusi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7709500af859c4de1d55e83863d3aeae
https://doi.org/10.1016/j.xphs.2018.01.017
https://doi.org/10.1016/j.xphs.2018.01.017
Publikováno v:
Hydrogen Exchange Mass Spectrometry of Proteins
The dynamic nature of the structure of monoclonal antibodies (mAbs) can be probed at a resolution of 5-20 residues using hydrogen-deuterium exchange mass spectrometry (H/D-MS). Recent studies using H/D-MS have shown that distinct regions of IgG1 mAbs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ac9695a2b7c0b1b31b50b9f54b2e8f3
https://doi.org/10.1002/jps.24224
https://doi.org/10.1002/jps.24224
Autor:
Jae Hyun Kim, Ranajoy Majumdar, Sangeeta B. Joshi, C. Russell Middaugh, David D. Weis, Thomas J. Tolbert, David B. Volkin, Mohammad A. Alsenaidy
Publikováno v:
Journal of Pharmaceutical Sciences. 102:3942-3956
The structural integrity and conformational stability of an IgG1 monoclonal antibody (mAb), after partial or complete enzymatic removal of the N-linked Fc glycan, were compared with the untreated mAb over a wide range of temperature (10°C-90°C) and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17d2b995066df8704de3ecb38b8f3024
https://doi.org/10.1002/jps.23730
https://doi.org/10.1002/jps.23730
Autor:
C. Russell Middaugh, David D. Weis, Jayant Arora, David B. Volkin, Ranajoy Majumdar, Steven M. Bishop, Hardeep S. Samra, John M. Hickey, Reza Esfandiary
Publikováno v:
mAbs
There is a need for new analytical approaches to better characterize the nature of the concentration-dependent, reversible self-association (RSA) of monoclonal antibodies (mAbs) directly, and with high resolution, when these proteins are formulated a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c52aad2d8d67ce6ce181771eb78d441f
https://pubmed.ncbi.nlm.nih.gov/25875351
https://pubmed.ncbi.nlm.nih.gov/25875351
Autor:
Hardeep S. Samra, Prakash Manikwar, Hasige A. Sathish, John M. Hickey, David D. Weis, C. Russell Middaugh, Santosh V. Thakkar, Ranajoy Majumdar, David B. Volkin, Steven M. Bishop
Publikováno v:
Journal of pharmaceutical sciences. 102(7)
The effects of sucrose and arginine on the conformational and storage stability of an IgG1 monoclonal antibody (mAb) were monitored by differential scanning calorimetry (DSC) and size-exclusion chromatography (SEC), respectively. Excipient effects on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cca82f35f0f13facbff32c6163ce800
https://pubmed.ncbi.nlm.nih.gov/23620222
https://pubmed.ncbi.nlm.nih.gov/23620222
Autor:
David D. Weis, Ranajoy Majumdar, Jayant Arora, C. Russell Middaugh, David B. Volkin, Prakash Manikwar, John M. Hickey
Publikováno v:
Journal of the American Society for Mass Spectrometry. 23(12)
Chromatographic carry-over can severely distort measurements of amide H/D exchange in proteins analyzed by LC/MS. In this work, we explored the origin of carry-over in the online digestion of an IgG1 monoclonal antibody using an immobilized pepsin co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3feae29a25d4fc498a6027a0bcb6c8b0
https://pubmed.ncbi.nlm.nih.gov/22993047
https://pubmed.ncbi.nlm.nih.gov/22993047