Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Amber D. Rolland"'
Autor:
SM Bargeen Alam Turzo, Justin T. Seffernick, Amber D. Rolland, Micah T. Donor, Sten Heinze, James S. Prell, Vicki H. Wysocki, Steffen Lindert
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
Collision cross sections (CCS) from ion mobility mass spectrometry provide information about protein shape and size. Here, the authors develop an algorithm to predict CCS and integrate experimental ion mobility data into Rosetta-based molecular model
Externí odkaz:
https://doaj.org/article/303314d1bc3e4445821c95a69c584e9a
Autor:
Douglas R. Walker, Kayla A. Jara, Amber D. Rolland, Coban Brooks, Wendy Hare, Andrew K. Swansiger, Patrick N. Reardon, James S. Prell, Elisar J. Barbar
Publikováno v:
Biomolecules, Vol 13, Iss 3, p 404 (2023)
LC8, a ubiquitous and highly conserved hub protein, binds over 100 proteins involved in numerous cellular functions, including cell death, signaling, tumor suppression, and viral infection. LC8 binds intrinsically disordered proteins (IDPs), and alth
Externí odkaz:
https://doaj.org/article/8501563212024d60b3f2005ca59a64c0
Autor:
Amber D. Rolland, James S. Prell
Publikováno v:
Chem Rev
Native mass spectrometry (MS) is aimed at preserving and determining the native structure, composition, and stoichiometry of biomolecules and their complexes from solution after they are transferred into the gas phase. Major improvements in native MS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84ebe5873dcf2267e959ea4e741bc3f2
https://pubmed.ncbi.nlm.nih.gov/34470219
https://pubmed.ncbi.nlm.nih.gov/34470219
Publikováno v:
Journal of the American Society for Mass Spectrometry. 33:369-381
The precise relationship between native gas-phase protein ion structure, charge, desolvation, and activation remains elusive. Much evidence supports the Charge Residue Model for native protein ions formed by electrospray ionization, but scaling laws
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24560553a136af2fcdd7e5a8450471e6
https://doi.org/10.1021/jasms.1c00351
https://doi.org/10.1021/jasms.1c00351
Autor:
Amber D. Rolland, Chad K. Park, Jun Wang, Nancy C. Horton, Julia Alma Townsend, Michael T. Marty, Henry M. Sanders, James S. Prell
Publikováno v:
Anal Chem
Viroporins are small viral ion channels that play important roles in the viral infection cycle and are proven antiviral drug targets. Matrix protein 2 from influenza A (AM2) is the best characterized viroporin, and the current paradigm is that AM2 fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29e5f81f7661a0490afbca2735ea753d
https://doi.org/10.1021/acs.analchem.1c04660
https://doi.org/10.1021/acs.analchem.1c04660
Autor:
James S. Prell, Vicki H. Wysocki, Heinze S, Micah T. Donor, Steffen Lindert, Amber D. Rolland, Justin T Seffernick, Turzo Sba
Publikováno v:
Nature Communications. 13
Among a wide variety of mass spectrometry (MS) methodologies available for structural characterizations of proteins, ion mobility (IM) provides structural information about protein shape and size in the form of an orientationally averaged collision c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75df12c7a73f0753d7fc17af79861580
https://doi.org/10.1038/s41467-022-32075-9
https://doi.org/10.1038/s41467-022-32075-9
Autor:
James S. Prell, Hanh T.M. Hoang, Delaney A. Smith, Kayla A. Jara, Elisar Barbar, Patrick N. Reardon, Amber D. Rolland
Publikováno v:
J Biol Chem
Dynein light chain 8 (LC8) interacts with intrinsically disordered proteins (IDPs) and influences a wide range of biological processes. It is becoming apparent that among the numerous IDPs that interact with LC8, many contain multiple LC8-binding sit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a2b058a46c9c548ffa154a4f5e6cd63
https://doi.org/10.1074/jbc.ra119.011653
https://doi.org/10.1074/jbc.ra119.011653
Autor:
James S. Prell, Amber D. Rolland
Publikováno v:
Trends Analyt Chem
Native ion mobility-mass spectrometry (IM-MS) is a rapidly growing field for studying the composition and structure of biomolecules and biomolecular complexes using gas-phase methods. Typically, ions are formed in native IM-MS using gentle nanoelectr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::407cd4183c48b8d8992fefe8151d8564
https://doi.org/10.1016/j.trac.2019.04.023
https://doi.org/10.1016/j.trac.2019.04.023
Autor:
Joaquin Rodriguez Galvan, Phillip Zhu, Amber D. Rolland, Richard B. Cooley, Elisar Barbar, Zhen Yu, Patrick N. Reardon, Heather M. Forsythe, Seth Pinckney, James S. Prell
Publikováno v:
Biophysical Journal
The nucleocapsid phosphoprotein N plays critical roles in multiple processes of the severe acute respiratory syndrome coronavirus 2 infection cycle: it protects and packages viral RNA in N assembly, interacts with the inner domain of spike protein, b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02c3ec225a36d6da9a291bdb76de60a9
http://europepmc.org/articles/PMC8007181
http://europepmc.org/articles/PMC8007181
Publikováno v:
Anal Chem
Many soluble and membrane proteins form symmetrical homooligomeric complexes. However, determining the oligomeric state of protein complexes can be difficult. Alpha-hemolysin (αHL) from Staphylococcus aureus is a symmetrical homooligomeric protein t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::264f5b4297df09c95e83cbd32c7aee92
https://europepmc.org/articles/PMC8048703/
https://europepmc.org/articles/PMC8048703/
