Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Tim J. Kamerzell"'
Autor:
C. Russell Middaugh, Tim J. Kamerzell
Publikováno v:
Journal of Pharmaceutical Sciences. 110:665-681
The rapid growth in technological advances and quantity of scientific data over the past decade has led to several challenges including data storage and analysis. Accurate models of complex datasets were previously difficult to develop and interpret.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49e0336c5cae218be84e153974619af7
https://doi.org/10.1016/j.xphs.2020.11.034
https://doi.org/10.1016/j.xphs.2020.11.034
Autor:
Tim J, Kamerzell, Brittney, Mikell, Lei, Chen, Harold, Elias, Buddhadeb, Dawn, Calum, MacRae, C Russell, Middaugh
Publikováno v:
Advances in protein chemistry and structural biology. 130
Histone modifying enzymes regulate chromatin architecture through covalent modifications and ultimately control multiple aspects of cellular function. Disruption of histone modification leads to changes in gene expression profiles and may lead to dis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e1df1aeb0282ead26630cda3247030f6
https://pubmed.ncbi.nlm.nih.gov/35534108
https://pubmed.ncbi.nlm.nih.gov/35534108
Autor:
Tim J. Kamerzell, Brittney Mikell, Lei Chen, Harold Elias, Buddhadeb Dawn, Calum MacRae, C. Russell Middaugh
Publikováno v:
Protein Design and Structure ISBN: 9780323992299
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9db995eb08e18c929151b3c86f9fb8c5
https://doi.org/10.1016/bs.apcsb.2022.02.004
https://doi.org/10.1016/bs.apcsb.2022.02.004
Autor:
Kai-Chen Yang, Ravi Iyengar, Tim J. Kamerzell, Calum A. MacRae, Jeanne M. Nerbonne, Eric A. Sobie
Genotype-phenotype relationships are determinants of human diseases. Often, we know little about why so many genes are involved in complex common diseases. We hypothesized that this multigene effect arises from the relationship between genes and phys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea6815af368f522bb57ad69c5f01233d
Publikováno v:
Journal of Pharmaceutical Sciences. 100:1341-1349
The physicochemical stability of protein therapeutics is of significant pharmaceutical interest. Immunoglobulin gamma (IgG) hinge region fragmentation has recently garnered attention as an important degradation route of therapeutic monoclonal antibod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb7e9ba38a20d0e09cf73a7b564400ed
https://doi.org/10.1002/jps.22389
https://doi.org/10.1002/jps.22389
Autor:
C. Russell Middaugh, Tim J. Kamerzell
Publikováno v:
Biochemistry. 46:9762-9773
Despite the well-accepted importance of protein flexibility and dynamics in molecular recognition and conformational stability, our understanding of these relationships is incomplete. Immunoglobulin flexibility is essential for antigen binding and ad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60dbb3a94b2d5b4ff43393d97b23e151
https://doi.org/10.1021/bi700645k
https://doi.org/10.1021/bi700645k
Autor:
Damon Papac, Sangeeta B. Joshi, C. Russell Middaugh, Meili Li, Tim J. Kamerzell, Donald McClean, Lori Peplinskie, Karen Toney
Publikováno v:
Protein Science. 16:1193-1203
The interaction of four representative polyanions with parathyroid hormone (PTH) residues 1-84 has been investigated utilizing a variety of spectroscopic and calorimetric techniques. Each of the polyanions employed demonstrate enthalpically driven bi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c170407885af96c068eda1ab2c2dd86
https://doi.org/10.1110/ps.062613807
https://doi.org/10.1110/ps.062613807
Autor:
Sarah J. Pyszczynski, Jay R. Unruh, Brian D. Slaughter, Tim J. Kamerzell, Thaddaus R. Hellwig, Carey K. Johnson, Michael W. Allen
Publikováno v:
The Journal of Physical Chemistry A. 107:5660-5669
This paper presents a detailed description of the fluorescence and photophysical behavior of indoline and indoline-2-carboxylic acid (I2CA). Indoline is an analogue of indole lacking the C2C3 double bond, but unlike indole, indoline possesses well-se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2e683ce8b43f68c99f232205be6882a
https://doi.org/10.1021/jp027813p
https://doi.org/10.1021/jp027813p
Although extensively studied, protein–protein interactions remain highly elusive and are of increasing interest in drug development. We show the assembly of a monoclonal antibody, using multivalent carboxylate ions, into highly-ordered structures.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14894f3fdbf33cdd416a3a5dfc6db44a
https://europepmc.org/articles/PMC3893242/
https://europepmc.org/articles/PMC3893242/
Autor:
Yatin R. Gokarn, Y. John Wang, Amanda L. Pace, Tim J. Kamerzell, Dimitry M. Danilenko, Michelle Mcdowell, Megan Li
Publikováno v:
Journal of pharmaceutical sciences. 102(4)
Low-volume protein dosage forms for subcutaneous injection pose unique challenges to the pharmaceutical scientist. Indeed, high protein concentrations are often required to achieve acceptable bioavailability and efficacy for many indications. Further
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c005ce37ed3aee2ed29fe15dbb15e27
https://pubmed.ncbi.nlm.nih.gov/23359242
https://pubmed.ncbi.nlm.nih.gov/23359242