Drug interaction mapping with proximity dependent enzyme recruiting chimeras

Autor: John D Venable, Ajay A Vashisht, Shima Rayatpisheh, James P Lajiness, Dean P Phillips, Ansgar Brock

Proximity dependent labeling using engineered enzymes has been used extensively to identify protein-protein interactions, and map protein complexes in-vitro and in-vivo. Here, we extend the use of engineered promiscuous biotin ligases to the identifi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::11521c45e325bcdb46153b2a8649dbe5
https://doi.org/10.1101/2022.09.26.509259

Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb

Autor: Tyler S. Hageman, Ulrike Leurs, John D. Lambris, Michael J. Chalmers, Ratnesh Pandey, Malvina Papanastasiou, James J. Filliben, Ioannis Karageorgos, Jeffrey W. Hudgens, Guodong Chen, Sarah Urata, Xiaojun Lu, Arun Chandramohan, Sheng Li, George M. Bou-Assaf, Mohammed A. Al-Naqshabandi, Alfonso Espada, Daniel Deredge, Ganesh S. Anand, Ansgar Brock, Sasidhar N. Nirudodhi, Caitlin Steckler, Patrick L. Wintrode, Eduardo Harguindey, Justin B. Sperry, Jennifer Zhang, Kyle Anderson, Kasper D. Rand, David D. Weis, Jason C. Rouse, James A. Carroll, Benjamin T. Walters, John D. Venable, Elyssia S. Gallagher, Hui-Min Zhang, Richard Y.-C. Huang, In-Hee Park

Publikováno v: Hudgens, J W, Gallagher, E S, Karageorgos, I, Anderson, K W, Filliben, J J, Huang, R Y-C, Chen, G, Bou-Assaf, G M, Espada, A, Chalmers, M J, Harguindey, E, Zhang, H-M, Walters, B T, Zhang, J, Venable, J D, Steckler, C, Park, I, Brock, A, Lu, X, Pandey, R K, Chandramohan, A, Anand, G S, Nirudodhi, S N, Sperry, J B, Rouse, J C, Carroll, J A, Rand, K D, Leurs, U, Weis, D D, Al-Naqshabandi, M A, Hageman, T S, Deredge, D, Wintrode, P L, Papanastasiou, M, Lambris, J D, Li, S & Urata, S 2019, ' Interlaboratory Comparison of Hydrogen-Deuterium Exchange Mass Spectrometry Measurements of the Fab fragment of NISTmAb ', Analytical Chemistry, vol. 91, no. 11, pp. 7336-7345 . https://doi.org/10.1021/acs.analchem.9b01100
Anal Chem

Hydrogen-deuterium exchange mass spectrometry (HDX-MS) is an established, powerful tool for investigating protein-ligand interactions, protein folding, and protein dynamics. However, HDX-MS is still an emergent tool for quality control of biopharmace

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5296a6097f668348bab5767e63adbfa6
https://curis.ku.dk/portal/da/publications/interlaboratory-comparison-of-hydrogendeuterium-exchange-mass-spectrometry-measurements-of-the-fab-fragment-of-nistmab(681700fb-de3a-485d-8fe7-fe3921794d20).html

Feature Based Retention Time Alignment for Improved HDX MS Analysis

Autor: John D. Venable, William Scuba, Ansgar Brock

Publikováno v: Journal of the American Society for Mass Spectrometry. 24:642-645

An algorithm for retention time alignment of mass shifted hydrogen-deuterium exchange (HDX) data based on an iterative distance minimization procedure is described. The algorithm performs pairwise comparisons in an iterative fashion between a list of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::194b4377589dd47306edbd275c7dece5
https://doi.org/10.1007/s13361-012-0566-9

Improving Protein Identification Sensitivity by Combining MS and MS/MS Information for Shotgun Proteomics Using LTQ-Orbitrap High Mass Accuracy Data

Autor: John D. Venable, John R. Yates, Cristian I. Ruse, Bingwen Lu, Akira Motoyama

Publikováno v: Analytical Chemistry. 80:2018-2025

We investigated and compared three approaches for shotgun protein identification by combining MS and MS/MS information using LTQ-Orbitrap high mass accuracy data. In the first approach, we employed a unique mass identifier method where MS peaks match

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e7714aff537db1355930375c4ba5f22
https://doi.org/10.1021/ac701697w

Estimation of Hydrogen-Exchange Protection Factors from MD Simulation Based on Amide Hydrogen Bonding Analysis

Autor: Susan E. Cellitti, Ansgar Brock, Glen Spraggon, In-Hee Park, John D. Venable, Scott A. Lesley, Caitlin Steckler

Publikováno v: Journal of chemical information and modeling. 55(9)

Hydrogen exchange (HX) studies have provided critical insight into our understanding of protein folding, structure and dynamics. More recently, Hydrogen Exchange Mass Spectrometry (HX-MS) has become a widely applicable tool for HX studies. The interp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eaac8e49049723e7b1cc59b9ff629ec9
https://pubmed.ncbi.nlm.nih.gov/26241692