نتائج البحث - "Rens M J M de Vries"

المصدر: Journal of Medicinal Chemistry, 63(1), 241-259. American Chemical Society
Journal of Medicinal Chemistry
Journal of medicinal chemistry 63(1), 241-259 (2020). doi:10.1021/acs.jmedchem.9b01372

مصطلحات موضوعية: Drug Inverse Agonism, Allosteric regulation, Retinoic acid, Ligands, 01 natural sciences, Article, Mice, Structure-Activity Relationship, 03 medical and health sciences, chemistry.chemical_compound, RAR-related orphan receptor gamma, Cell Line, Tumor, Drug Discovery, Coactivator, Animals, Inverse agonist, ddc:610, 030304 developmental biology, Orphan receptor, 0303 health sciences, Binding Sites, Cycloaddition Reaction, Molecular Structure, Isoxazoles, Nuclear Receptor Subfamily 1, Group F, Member 3, 0104 chemical sciences, 3. Good health, Cell biology, Molecular Docking Simulation, 010404 medicinal & biomolecular chemistry, Retinoic acid receptor, Nuclear receptor, chemistry, Drug Design, Microsomes, Liver, Molecular Medicine

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4ae8e57733404f4158688fc9f7a2155Test
https://doi.org/10.1021/acs.jmedchem.9b01372Test

4

Cooperativity between the orthosteric and allosteric ligand binding sites of RORγt

المؤلفون: Rens M J M de Vries, Femke A. Meijer, Luc Brunsveld, Richard G. Doveston, Iris A. Leijten-van de Gevel

المساهمون: Chemical Biology, ICMS Core

المصدر: Proceedings of the National Academy of Sciences of the United States of America (PNAS), 118(6):e2021287118. National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America

مصطلحات موضوعية: genetic structures, Protein Conformation, Allosteric regulation, Molecular Conformation, nuclear receptors, Cooperativity, Molecular Dynamics Simulation, Crystallography, X-Ray, Ligands, Biochemistry, Biophysical Phenomena, drug discovery, 03 medical and health sciences, 0302 clinical medicine, Allosteric Regulation, Humans, 030304 developmental biology, 0303 health sciences, Multidisciplinary, Binding Sites, Drug discovery, Chemistry, structure elucidation, Cooperative binding, ROR gamma t, Nuclear Receptor Subfamily 1, Group F, Member 3, Biological Sciences, Ligand (biochemistry), Förster resonance energy transfer, Nuclear receptor, 030220 oncology & carcinogenesis, Helix, Physical Sciences, Biophysics, RORγt, allosteric modulators, Allosteric Site, Protein Binding

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4af3aeb1394211469396b3c50ee1046cTest
https://doi.org/10.1073/pnas.2021287118Test

5

Allosteric small molecule modulators of nuclear receptors

المؤلفون: Femke A. Meijer, Rens M J M de Vries, Luc Brunsveld, Iris A. Leijten-van de Gevel

المصدر: Molecular and Cellular Endocrinology. 485:20-34

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dfc3b346802c4fe646566a26a7f4c5aTest
https://doi.org/10.1016Test/j.mce.2019.01.022

6

Structural interface between LRRK2 and 14-3-3 protein

المؤلفون: Luc Brunsveld, Richard G. Doveston, Loes M. Stevers, Christian Ottmann, Rens M J M de Vries, Lech-Gustav Milroy

المساهمون: Chemical Biology

المصدر: Biochemical Journal, 474(7), 1273-1287. Portland Press Ltd.

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Secondary, Peptides/chemical synthesis, Gene Expression, Sequence Homology, Plasma protein binding, Crystallography, X-Ray, Biochemistry, Inclusion bodies, Protein Structure, Secondary, 0302 clinical medicine, Models, Cloning, Molecular, Crystallography, Leucine-Rich Repeat Serine-Threonine Protein Kinase-2/chemistry, Recombinant Fusion Proteins/chemistry, LRRK2, Cell biology, Amino Acid, Protein Binding, Protein Structure, Neurite, Recombinant Fusion Proteins, Chemie, Biology, Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Protein–protein interaction, 03 medical and health sciences, Escherichia coli, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Kinase activity, Protein kinase A, Molecular Biology, 14-3-3 protein, Binding Sites, Sequence Homology, Amino Acid, Molecular, Cell Biology, nervous system diseases, Escherichia coli/genetics, Kinetics, 030104 developmental biology, 14-3-3 Proteins, Mutation, X-Ray, Peptides, 14-3-3 Proteins/chemistry, Sequence Alignment, 030217 neurology & neurosurgery, Cloning

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23dd3716e8903b1553d6d6886612596fTest
http://www.scopus.com/inward/record.url?scp=85016451496&partnerID=8YFLogxKTest

7

Ligand Dependent Switch from RXR Homo- to RXR-NURR1 Heterodimerization

المؤلفون: Marcel Scheepstra, Christian Ottmann, Jian-Nong Ma, Femke A. Meijer, Roger Olsson, Ethan S. Burstein, Rens M J M de Vries, Luc Brunsveld, Sebastian A. Andrei, Lech-Gustav Milroy

المساهمون: Chemical Biology

المصدر: ACS Chemical Neuroscience
ACS Chemical Neuroscience, 8(9), 2065-2077. American Chemical Society
ACS chemical neuroscience 8(9), 2065-2077 (2017). doi:10.1021/acschemneuro.7b00216

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Physiology, Plasma protein binding, Ligands, Biochemistry, 0302 clinical medicine, Models, Nuclear receptors, Nuclear Receptor Subfamily 4, Group A, Member 2, retinoid X receptor, Receptor, Ethers/chemistry, Esters/chemistry, Group A, Nuclear Receptor Subfamily 4, Group A, Member 2/agonists, Molecular Structure, Esters, General Medicine, Ligand (biochemistry), Small molecule, 3. Good health, ddc:540, Small heterodimer partner, Retinoid X Receptor alpha/agonists, Member 2/agonists, ligand binding domain, Ethers, Protein Binding, Research Article, Nuclear Receptor Subfamily 4, Cognitive Neuroscience, Biology, Retinoid X receptor, 03 medical and health sciences, Two-Hybrid System Techniques, Journal Article, Escherichia coli, Humans, nuclear receptor related 1, Retinoid X Receptor alpha, Retinoid X receptor alpha, heterodimerization, Molecular, Hydrogen Bonding, Cell Biology, 030104 developmental biology, Nuclear receptor, Drug Design, Biophysics, Protein Multimerization, 030217 neurology & neurosurgery

وصف الملف: application/pdf

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96b3fbe2538f4b6de28283ad946d8051Test
https://pubmed.ncbi.nlm.nih.gov/28691794Test

8

Characterization and small-molecule stabilization of the multisite tandem binding between 14-3-3 and the R domain of CFTR

المؤلفون: Loes M. Stevers, Luc Brunsveld, Daphne S. van Scheppingen, L.G. Milroy, Rens M J M de Vries, David Y. Thomas, Graeme W. Carlile, Chan Vinh Lam, Seppe Leysen, Christian Ottmann, Femke A. Meijer

المساهمون: Chemical Biology, Biomedical Engineering

المصدر: Proceedings of the National Academy of Sciences of the United States of America (PNAS), 113(9), E1152-E1161. National Academy of Sciences

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, congenital, hereditary, and neonatal diseases and abnormalities, Molecular Sequence Data, Mutant, Druggability, Chemie, Cystic Fibrosis Transmembrane Conductance Regulator, Calorimetry, 010402 general chemistry, 01 natural sciences, Protein–protein interaction, protein-protein interaction, 03 medical and health sciences, Mutant protein, disordered protein, Amino Acid Sequence, Binding site, Binding Sites, Multidisciplinary, biology, Endoplasmic reticulum, multivalency, Small molecule, Cystic fibrosis transmembrane conductance regulator, 0104 chemical sciences, Cell biology, 030104 developmental biology, PNAS Plus, 14-3-3 Proteins, Biochemistry, biology.protein

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34481df6ce559b07be53fe3007d4ad2dTest
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=84959472285Test

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