Výsledky vyhledávání - "Loria, J Patrick"

Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases

Autoři: Shen, Ruidan Crean, Rory M. Olsen, Keith J. a další

Zdroj: Chemical Science. 13(45):13524-13540

Popis souboru: electronic

Přístupová URL adresa: https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-490545
https://doi.org/10.1039/d2sc04135a

Conformational Dynamics and Catalytic Backups in a Hyper-thermostable Engineered Archaeal Protein Tyrosine Phosphatase

Autoři: Yehorova, Dariia Alansson, Nikolas Shen, Ruidan a další

Přispěvatelé: Yehorova, Dariia Alansson, Nikolas Shen, Ruidan a další

Zdroj: JACS Au ; ISSN 2691-3704 2691-3704

Dostupnost: https://doi.org/10.1021/jacsau.5c00756
https://pubs.acs.org/doi/pdf/10.1021/jacsau.5c00756

Eigenvector centrality for characterization of protein allosteric pathways

Autoři: Negre, Christian F. A. Morzan, Uriel N. Hendrickson, Heidi P. a další

Zdroj: Proceedings of the National Academy of Sciences of the United States of America, 2018 Dec . 115(52), E12201-E12208.

Přístupová URL adresa: https://www.jstor.org/stable/26573957

Distal Mutations Rewire Allosteric Networks to Control Substrate Specificity in PTP1B.

Autoři: Wang, Xiaoyuan Anderson, Ryan M. Liu, Jinchan a další

Zdroj: Biochemistry. 12/16/2025, Vol. 64 Issue 24, p4661-4674. 14p.

Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activity

Autoři: Lisi, George P. East, Kyle W. Batista, Victor S. a další

Zdroj: Proceedings of the National Academy of Sciences of the United States of America, 2017 Apr . 114(17), E3414-E3423.

Přístupová URL adresa: https://www.jstor.org/stable/26480788

Turning up the heat mimics allosteric signaling in imidazole-glycerol phosphate synthase

Autoři: Maschietto, Federica Morzan, Uriel N Tofoleanu, Florentina a další

Přispěvatelé: Maschietto, Federica Morzan, Uriel N Tofoleanu, Florentina a další

Zdroj: ISSN: 2041-1723.

Témata: [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]

Relation: info:eu-repo/semantics/altIdentifier/pmid/37076500; PUBMED: 37076500

Dostupnost: https://hal.science/hal-05006523
https://hal.science/hal-05006523v1/document
https://hal.science/hal-05006523v1/file/s41467-023-37956-1.pdf
https://doi.org/10.1038/s41467-023-37956-1

Author Correction: Turning up the heat mimics allosteric signaling in imidazole-glycerol phosphate synthase

Autoři: Maschietto, Federica Morzan, Uriel N. Tofoleanu, Florentina a další

Zdroj: Nature Communications ; volume 14, issue 1 ; ISSN 2041-1723

Dostupnost: https://doi.org/10.1038/s41467-023-38370-3
https://www.nature.com/articles/s41467-023-38370-3.pdf
https://www.nature.com/articles/s41467-023-38370-3

Conformational Motions Regulate Phosphoryl Transfer in Related Protein Tyrosine Phosphatases

Autoři: Whittier, Sean K. Hengge, Alvan C. Loria, J. Patrick

Zdroj: Science, 2013 Aug . 341(6148), 899-903.

Přístupová URL adresa: https://www.jstor.org/stable/23491261

MIF intersubunit disulfide mutant antagonist supports activation of CD74 by endogenous MIF trimer at physiologic concentrations

Autoři: Fan, Chengpeng Rajasekaran, Deepa Syed, Mansoor Ali a další

Zdroj: Proceedings of the National Academy of Sciences of the United States of America, 2013 Jul 01. 110(27), 10994-10999.

Přístupová URL adresa: https://www.jstor.org/stable/42706363

A simple method to determine changes in the affinity between HisF and HisH in the Imidazole Glycerol Phosphate Synthase heterodimer

Autoři: Almeida, Vitor M. Loria, J. Patrick Marana, Sandro R. a další

Přispěvatelé: Almeida, Vitor M. Loria, J. Patrick Marana, Sandro R. a další

Zdroj: PLOS ONE ; volume 17, issue 4, page e0267536 ; ISSN 1932-6203

Dostupnost: https://doi.org/10.1371/journal.pone.0267536
https://dx.plos.org/10.1371/journal.pone.0267536

Unified total synthesis of the limonoid alkaloids: Strategies for the de novo synthesis of highly substituted pyridine scaffolds

Autoři: Schuppe, Alexander W. Liu, Yannan Gonzalez-Hurtado, Elsie a další

Zdroj: Chem ; volume 8, issue 10, page 2856-2887 ; ISSN 2451-9294

Dostupnost: http://dx.doi.org/10.1016/j.chempr.2022.09.012
https://api.elsevier.com/content/article/PII:S2451929422004855?httpAccept=text/xml
https://api.elsevier.com/content/article/PII:S2451929422004855?httpAccept=text/plain

The Mechanism of Rate-Limiting Motions in Enzyme Function

Autoři: Watt, Eric D. Shimada, Hiroko Kovrigin, Evgenii L. a další

Zdroj: Proceedings of the National Academy of Sciences of the United States of America, 2007 Jul . 104(29), 11981-11986.

Přístupová URL adresa: https://www.jstor.org/stable/25436235

Supplementary Simulation Data for Insights into the Importance of WPD-Loop Sequence for Activity and Structure in Protein Tyrosine Phosphatases

Autoři: Shen, Ruidan orcid:0000-0003-4709- Crean, Rory M. a další

Témata: Protein Tyrosine Phosphatases, PTP1B, YopH, Conformational Plasticitiy, Loop Dynamics, Molecular Dynamics, Molecular Simulation Data

Relation: https://zenodo.org/records/5500670; oai:zenodo.org:5500670; https://doi.org/10.5281/zenodo.5500670

Dostupnost: https://doi.org/10.5281/zenodo.5500670
https://zenodo.org/records/5500670

Updated Supplementary Simulation Data for Insights into the Importance of WPD-Loop Sequence for Activity and Structure in Protein Tyrosine Phosphatases

Autoři: Shen, Ruidan orcid:0000-0003-4709- Crean, Rory M. a další

Témata: Protein Tyrosine Phosphatases, PTP1B, YopH, Conformational Plasticitiy, Loop Dynamics, Molecular Dynamics, Molecular Simulation Data

Relation: https://zenodo.org/records/6525328; oai:zenodo.org:6525328; https://doi.org/10.5281/zenodo.6525328

Dostupnost: https://doi.org/10.5281/zenodo.6525328
https://zenodo.org/records/6525328

Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality

Autoři: Pinkston, Justin Jo, Jihye Olsen, Keith J. a další

Přispěvatelé: Pinkston, Justin Jo, Jihye Olsen, Keith J. a další

Zdroj: Biochemistry ; volume 60, issue 38, page 2888-2901 ; ISSN 0006-2960 1520-4995

Dostupnost: https://doi.org/10.1021/acs.biochem.1c00365
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.1c00365

Phosphorylation of a Human Microprotein Promotes Dissociation of Biomolecular Condensates

Autoři: Na, Zhenkun Luo, Yang Cui, Danica S. a další

Přispěvatelé: Na, Zhenkun Luo, Yang Cui, Danica S. a další

Zdroj: Journal of the American Chemical Society ; volume 143, issue 32, page 12675-12687 ; ISSN 0002-7863 1520-5126

Dostupnost: https://doi.org/10.1021/jacs.1c05386
https://pubs.acs.org/doi/pdf/10.1021/jacs.1c05386

Exploring Protein Structure and Dynamics through a Project-Oriented Biochemistry Laboratory Module

Autoři: Lipchock, James M. Ginther, Patrick S. Douglas, Bonnie B. a další

Zdroj: Biochemistry and Molecular Biology Education. Sep-Oct 2017 45(5):403-410.

Peer Reviewed: Y

Page Count: 8

Sponsoring Agency: National Science Foundation (NSF)

Descriptors: Biochemistry, Undergraduate Students, Student Research, Genetics, Kinetics, Laboratory Experiments, Molecular Structure, Active Learning, Student Projects

Allosteric Communication Disrupted by a Small Molecule Binding to the Imidazole Glycerol Phosphate Synthase Protein–Protein Interface

Autoři: Rivalta, Ivan Lisi, George P. Snoeberger, Ning-Shiuan a další

Přispěvatelé: Rivalta, Ivan Lisi, George P. Snoeberger, Ning-Shiuan a další

Zdroj: Biochemistry. 55:6484-6494

Témata: 0301 basic medicine, 0303 health sciences, Binding Sites, Magnetic Resonance Spectroscopy, Imidazoles, Allosteric Site, Aminohydrolases, Bacterial Proteins, Biocatalysis, Calorimetry, Catalytic Domain, Crystallography, X-Ray, Ligands, Molecular Dynamics Simulation, Protein Binding, Protein Domains, Protein Subunits, Ribonucleotides, Small Molecule Libraries, Thermotoga maritima, Allosteric Regulation, Biochemistry, 03 medical and health sciences, [CHIM] Chemical Sciences

Přístupová URL adresa: https://europepmc.org/articles/pmc5283573?pdf=render
https://pubmed.ncbi.nlm.nih.gov/27797506
http://pubs.acs.org/doi/abs/10.1021/acs.biochem.6b00859
https://pubs.acs.org/doi/abs/10.1021/acs.biochem.6b00859
https://pubs.acs.org/doi/full/10.1021/acs.biochem.6b00859
https://pubmed.ncbi.nlm.nih.gov/27797506/
https://www.ncbi.nlm.nih.gov/pubmed/27797506
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5283573/
https://hal.science/hal-01639041v1
https://doi.org/10.1021/acs.biochem.6b00859
https://hdl.handle.net/11585/669328
http://pubs.acs.org/journal/bichaw
https://doi.org/10.1021/acs.biochem.6b00859

Dissecting Dynamic Allosteric Pathways Using Chemically Related Small-Molecule Activators

Autoři: Lisi, George P. Manley, Gregory A. Hendrickson, Heidi a další

Přispěvatelé: Lisi, George P. Manley, Gregory A. Hendrickson, Heidi a další

Zdroj: Structure. 24:1155-1166

Témata: Molecular Docking Simulation, 0301 basic medicine, 0303 health sciences, 03 medical and health sciences, Allosteric Regulation, Aminohydrolases, Aminoimidazole Carboxamide, Isoxazoles, Ligands, Ribonucleotides, Allosteric Site, Structural Biology, Molecular Biology, [CHIM] Chemical Sciences

Přístupová URL adresa: http://www.cell.com/article/S0969212616300715/pdf
https://pubmed.ncbi.nlm.nih.gov/27238967
https://www.cell.com/structure/fulltext/S0969-2126(16)30071-5
http://www.cell.com/structure/comments/S0969-2126(16)30071-5
https://www.ncbi.nlm.nih.gov/pubmed/27238967
https://www.sciencedirect.com/science/article/pii/S0969212616300715
http://www.sciencedirect.com/science/article/pii/S0969212616300715
https://pubmed.ncbi.nlm.nih.gov/27238967/
https://hal.science/hal-01639042v1
https://doi.org/10.1016/j.str.2016.04.010
http://www.journals.elsevier.com/structure/
https://doi.org/10.1016/j.str.2016.04.010
https://hdl.handle.net/11585/669334

A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi

Autoři: Berk, Jason M. Lim, Christopher Ronau, Judith A. a další

Přispěvatelé: Berk, Jason M. Lim, Christopher Ronau, Judith A. a další

Zdroj: Nature Communications ; volume 11, issue 1 ; ISSN 2041-1723

Dostupnost: https://doi.org/10.1038/s41467-020-15985-4
https://www.nature.com/articles/s41467-020-15985-4.pdf
https://www.nature.com/articles/s41467-020-15985-4