Supplemental material
Journal of Biomolecular Structure and Dynamics
Volume 39, 2021 - Issue 6
Research Articles
Molecular dynamics simulations of human α-thrombin in different structural contexts: evidence for an aptamer-guided cooperation between the two exosites
Romualdo Troisia Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant’Angelo, Naples, Italy
https://orcid.org/0000-0002-3484-3589
https://orcid.org/0000-0002-3484-3589, Nicole Balascob Institute of Biostructures and Bioimaging, CNR, Naples, Italyhttps://orcid.org/0000-0001-7862-9448
https://orcid.org/0000-0001-7862-9448, Luigi Vitaglianob Institute of Biostructures and Bioimaging, CNR, Naples, Italyhttps://orcid.org/0000-0002-3032-3375
https://orcid.org/0000-0002-3032-3375 & Filomena Sicaa Department of Chemical Sciences, University of Naples Federico II, Complesso Universitario di Monte Sant’Angelo, Naples, ItalyCorrespondence[email protected]
https://orcid.org/0000-0003-4501-4476
https://orcid.org/0000-0003-4501-4476Reprints and Corporate Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
To request a reprint or corporate permissions for this article, please click on the relevant link below:
Academic Permissions
Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?
Obtain permissions instantly via Rightslink by clicking on the button below:
If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.
Related Research Data
Polymorphic transitions in single crystals: A new molecular dynamics method
Source:
AIP Publishing
Aptamers as therapeutics.
Source:
Springer Science and Business Media LLC
Targeting the GPIbα Binding Site of Thrombin To Simultaneously Induce Dual Anticoagulant and Antiplatelet Effects
Source:
American Chemical Society (ACS)
Amide H/2H exchange reveals a mechanism of thrombin activation.
Source:
American Chemical Society (ACS)
Accurate Prediction of Amide Exchange in the Fast Limit Reveals Thrombin Allostery.
Source:
Elsevier BV
Aptamers as therapeutics.
Source:
Springer Science and Business Media LLC
Molecular assembly for high-performance bivalent nucleic acid inhibitor
Source:
Proceedings of the National Academy of Sciences
Measurement of aptamer-protein interactions with back-scattering interferometry.
Source:
American Chemical Society (ACS)
NMR reveals a dynamic allosteric pathway in thrombin.
Source:
Springer Science and Business Media LLC
Thrombin as an anticoagulant.
Source:
Elsevier
Structural identification of the pathway of long-range communication in an allosteric enzyme
Source:
Proceedings of the National Academy of Sciences
Duplex–quadruplex motifs in a peculiar structural organization cooperatively contribute to thrombin binding of a DNA aptamer
Source:
International Union of Crystallography (IUCr)
Probing light chain mutation effects on thrombin via molecular dynamics simulations and machine learning
Source:
Informa UK Limited
DNA Aptamers for Human Thrombin with High Anticoagulant Activity Demonstrate Target- and Species-Specificity
Source:
Bentham Science Publishers Ltd.
Conformational analysis of γ′ peptide (410-427) interactions with thrombin anion binding exosite II
Source:
American Chemical Society (ACS)
Aptamers as targeted therapeutics: current potential and challenges
Source:
Springer Science and Business Media LLC
Exosites in blood coagulation
Source:
Wiley
Why ser and not thr brokers catalysis in the trypsin fold.
Source:
American Chemical Society (ACS)
Thrombin Exosite Maturation and Ligand Binding at ABE II Help Stabilize PAR-Binding Competent Conformation at ABE I
Source:
American Chemical Society (ACS)
Ligand Binding to Anion Binding Exosites Regulates Conformational Properties of Thrombin
Source:
Elsevier BV
Synergistic effect of aptamers that inhibit exosites 1 and 2 on thrombin.
Source:
Cold Spring Harbor Laboratory
Binding of Exosite Ligands to Human Thrombin: RE-EVALUATION OF ALLOSTERIC LINKAGE BETWEEN THROMBIN EXOSITES I AND II *
Source:
Elsevier BV
High-resolution structures of two complexes between thrombin and thrombin-binding aptamer shed light on the role of cations in the aptamer inhibitory activity
Source:
Oxford University Press (OUP)
Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems
Source:
AIP Publishing
Crystallization and preliminary X-ray analysis of the complex of human α-thrombin with a modified thrombin-binding aptamer
Source:
International Union of Crystallography (IUCr)
Investigation of the interaction between a bivalent aptamer and thrombin by AFM.
Source:
American Chemical Society (ACS)
Thrombin Specificity
Source:
Georg Thieme Verlag KG
Structural transitions during prothrombin activation: On the importance of fragment 2
Source:
Elsevier BV
Exosite 2-Directed Ligands Attenuate Protein C Activation by the Thrombin-Thrombomodulin Complex.
Source:
American Chemical Society (ACS)
Selection of single-stranded DNA molecules that bind and inhibit human thrombin.
Source:
Springer Science and Business Media LLC
Linking provided by
