Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Joseph D. Eschweiler"'
Autor:
Daniel D. Vallejo, Chae Kyung Jeon, Kristine F. Parson, Hayley R. Herderschee, Joseph D. Eschweiler, Dana I. Filoti, Brandon T. Ruotolo
Publikováno v:
Analytical Chemistry. 94:6745-6753
Stability is a key critical quality attribute monitored throughout the development of monoclonal antibody (mAb) therapeutics. Minor changes in their higher order structure (HOS) caused by stress or environment may alter mAb aggregation, immunogenicit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d30baf8cbb571aa86626d2ebb16cd28d
https://doi.org/10.1021/acs.analchem.2c00160
https://doi.org/10.1021/acs.analchem.2c00160
Autor:
Joseph D. Eschweiler, Daniel A. Polasky, Ruwan T. Kurulugama, Brandon T. Ruotolo, Daniel D. Vallejo, John C. Fjeldsted
Publikováno v:
Analytical Chemistry. 91:8137-8146
Collision-induced unfolding (CIU) of protein ions and their noncovalent complexes offers relatively rapid access to a rich portfolio of biophysical information, without the need to tag or purify proteins prior to analysis. Such assays have been chara
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d252c88554d7d98600761f4ad0e1d319
https://doi.org/10.1021/acs.analchem.9b00427
https://doi.org/10.1021/acs.analchem.9b00427
Autor:
Brandon T. Ruotolo, Somayesadat Badieyan, James C.A. Bardwell, Joseph D. Eschweiler, Ajitha S. Cristie-David, Aaron Sciore, Philipp Koldewey, Min Su, E. Neil G. Marsh
Publikováno v:
ChemBioChem. 18:1888-1892
The organization of proteins into new hierarchical forms is an important challenge in synthetic biology. However, engineering new interactions between protein subunits is technically challenging and typically requires extensive redesign of protein-pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bf5812b35f7f664780ccc20a2afd983
https://doi.org/10.1002/cbic.201700406
https://doi.org/10.1002/cbic.201700406
Publikováno v:
Annual Review of Analytical Chemistry. 10:25-44
Capturing the dynamic interplay between proteins and their myriad interaction partners is critically important for advancing our understanding of almost every biochemical process and human disease. The importance of this general area has spawned many
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4824a7be6e25eefb0ada3fa66423efa8
https://doi.org/10.1146/annurev-anchem-061516-045414
https://doi.org/10.1146/annurev-anchem-061516-045414
Autor:
Sugyan M. Dixit, Brandon T. Ruotolo, Mark A. Farrugia, Robert P. Hausinger, Joseph D. Eschweiler
The synthesis of active Klebsiella aerogenes urease via an 18-subunit enzyme apoprotein-accessory protein pre-activation complex has been well-studied biochemically, but thus far this complex has remained refractory to direct structural characterizat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70ad908d75d3634b32ce4c5627d8ccec
https://europepmc.org/articles/PMC5884726/
https://europepmc.org/articles/PMC5884726/
Publikováno v:
Journal of the American Society for Mass Spectrometry. 27:41-49
Protocols that aim to construct complete models of multiprotein complexes based on ion mobility and mass spectrometry data are becoming an important element of integrative structural biology efforts. However, the usefulness of such data is predicated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36967d7f9e89df140aee7b1ed4bc5315
https://doi.org/10.1007/s13361-015-1250-7
https://doi.org/10.1007/s13361-015-1250-7
Previously, we discovered and structurally characterized a complex between amyloid β 1–40 and the neuropeptide leucine enkephalin. This work identified leucine enkephalin as a potentially useful starting point for the discovery of peptide-related
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef5d6a7b8246a77b4b14360a539947b9
https://europepmc.org/articles/PMC5724361/
https://europepmc.org/articles/PMC5724361/
Despite the growing application of gas-phase measurements in structural biology and drug discovery, the factors that govern protein stabilities and structures in a solvent-free environment are still poorly understood. Here, we examine the solvent-fre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e31f16902766ce667d42f4a95c1f548c
https://europepmc.org/articles/PMC5724362/
https://europepmc.org/articles/PMC5724362/
Autor:
Sang Joon Won, Brandon T. Ruotolo, Sin Ye Hwang, Fei San Chong, Jaimeen D. Majmudar, Brent R. Martin, Joseph D. Eschweiler
Activity-based protein profiling (ABPP) has revolutionized the discovery and optimization of active-site ligands across distinct enzyme families, providing a robust platform for in-class selectivity profiling. Nonetheless, this approach is less strai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12882a8f75018e2aca92b0501dfb7fbc
https://europepmc.org/articles/PMC5304287/
https://europepmc.org/articles/PMC5304287/
Autor:
Joseph D. Eschweiler, Min Su, James C.A. Bardwell, Kelsey Diffley, Aaron Sciore, Philipp Koldewey, Brian M. Linhares, E. Neil G. Marsh, Brandon T. Ruotolo, Georgios Skiniotis
The assembly of individual protein subunits into large-scale symmetrical structures is widespread in nature and confers new biological properties. Engineered protein assemblies have potential applications in nanotechnology and medicine; however, a ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dc3deaa9ac7bd55de1fb924cc6fd334
https://europepmc.org/articles/PMC4978231/
https://europepmc.org/articles/PMC4978231/