Zobrazeno 1 - 10
of 24
pro vyhledávání: '"SUBHABRATA MAJUMDER"'
Autor:
Teshome Aboye, Christopher J. Meeks, Subhabrata Majumder, Alexander Shekhtman, Kathleen Rodgers, Julio A. Camarero
Publikováno v:
Molecules, Vol 21, Iss 2, p 152 (2016)
We report for the first time the design and synthesis of a novel cyclotide able to activate the unique receptor of angiotensin (1-7) (AT1-7), the MAS1 receptor. This was accomplished by grafting an AT1-7 peptide analog onto loop 6 of cyclotide MCoTI-
Externí odkaz:
https://doaj.org/article/18520d2f54c948ac8c5a905d2ff52d2d
Publikováno v:
Journal of the American Chemical Society. 145:10826-10838
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a4005a7469d86a965dbfbf836ca7578
https://doi.org/10.1021/jacs.3c02154
https://doi.org/10.1021/jacs.3c02154
Publikováno v:
Drug Metabolism Handbook. :923-966
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fdf20ad37a64b2c6453f5e7ce61c54a5
https://doi.org/10.1002/9781119851042.ch27
https://doi.org/10.1002/9781119851042.ch27
Publikováno v:
Pharmaceutical research. 39(3)
The viscosity of highly concentrated therapeutic monoclonal antibody (mAb) formulations at concentrations ≥ 100 mg/mL can significantly affect the stability, processing, and drug product development for subcutaneous delivery. An early identificatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c639aad2f0dc4631f39bb081b319dafd
https://pubmed.ncbi.nlm.nih.gov/35174433
https://pubmed.ncbi.nlm.nih.gov/35174433
Autor:
Sergey Reverdatto, Christopher M. DeMott, Alexander Shekhtman, David S. Burz, Subhabrata Majumder
Publikováno v:
Biochemistry. 56:4117-4126
Ribosomes are present inside bacterial cells at micromolar concentrations and occupy up to 20% of the cell volume. Under these conditions, even weak quinary interactions between ribosomes and cytosolic proteins can affect protein activity. By using i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::716cb70e1b554777b1f420fd3df5e47d
https://doi.org/10.1021/acs.biochem.7b00613
https://doi.org/10.1021/acs.biochem.7b00613
Autor:
Shibu Philip, Subhabrata Majumder, Andrew Saati, Elaine Stephens, Arun Alphonse Ignatius, Lucy L. Liu, Jason C. Rouse
Publikováno v:
Pharmaceutical research. 36(9)
An understanding of higher order structure (HOS) of monoclonal antibodies (mAbs) could be critical to predicting its function. Amongst the various factors that can potentially affect HOS of mAbs, chemical modifications that are routinely encountered
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85ab5935051c9da90dea1242200ae40f
https://pubmed.ncbi.nlm.nih.gov/31264003
https://pubmed.ncbi.nlm.nih.gov/31264003
Autor:
Christopher M. DeMott, David S. Burz, Sergey Reverdatto, Subhabrata Majumder, Alexander Shekhtman
Publikováno v:
Biochemistry. 55:4568-4573
RNA constitutes up to 20% of a cell’s dry weight, corresponding to ~20 mg/mL. This high concentration of RNA facilitates low-affinity protein–RNA quinary interactions, which may play an important role in facilitating and regulating biological pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bed32ba9bc869bb88f62d100a88e02c
https://doi.org/10.1021/acs.biochem.6b00330
https://doi.org/10.1021/acs.biochem.6b00330
Publikováno v:
Pharmaceutical Research. 35
Fc domains are an integral component of monoclonal antibodies (mAbs) and Fc-based fusion proteins. Engineering mutations in the Fc domain is a common approach to achieve desired effector function and clinical efficacy of therapeutic mAbs. It remains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85b8fe80bd760c963958d66bc0e0cb20
https://doi.org/10.1007/s11095-018-2500-8
https://doi.org/10.1007/s11095-018-2500-8
Publikováno v:
Journal of pharmaceutical sciences. 108(3)
Bispecific antibodies represent a promising avenue whereby 2 different binding specificities of a single-chain antibody can be grafted into a common Fc fragment to generate one antibody-like molecule. Despite the promising efficacy of such modalities
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13dbb285ffd7064f7b2f2f5bf9d30383
https://pubmed.ncbi.nlm.nih.gov/30391414
https://pubmed.ncbi.nlm.nih.gov/30391414
Publikováno v:
ChemBioChem. 15:929-933
Distinct differences between how model proteins interact in-cell and in vitro suggest that the cytosol might have a profound effect in modulating protein-protein and/or protein-ligand interactions that are not observed in vitro. Analyses of in-cell N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be10671e65b66a07fddfd743db74e959
https://doi.org/10.1002/cbic.201400030
https://doi.org/10.1002/cbic.201400030