A Structural Explanation for the Antithrombotic Activity of ARC1172, a DNA Aptamer that Binds von Willebrand Factor Domain A1 - Wikidata - wikimedia - TriplyDB

A Structural Explanation for the Antithrombotic Activity of ARC1172, a DNA Aptamer that Binds von Willebrand Factor Domain A1

A Structural Explanation for the Antithrombotic Activity of ARC1172, a DNA Aptamer that Binds von Willebrand Factor Domain A1

http://www.wikidata.org/entity/Q27658166

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Structural basis for discriminatory recognition of Plasmodium lactate dehydrogenase by a DNA aptamer Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib Crystal Structure of Interleukin-6 in Complex with a Modified Nucleic Acid Ligand Structure of a complex formed by a protein and a helical aromatic oligoamide foldamer at 2.1 Å resolution Probing the limits of aptamer affinity with a microfluidic SELEX platform Modulation of the Coagulation Cascade Using Aptamers The conservation profile of a protein bears the imprint of the molecule that is evolutionarily coupled to the protein.Mutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor.Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain.Applications of synchrotron-based spectroscopic techniques in studying nucleic acids and nucleic acid-functionalized nanomaterials Nucleic Acid Ligands With Protein-like Side Chains: Modified Aptamers and Their Use as Diagnostic and Therapeutic Agents Porcine and canine von Willebrand factor and von Willebrand disease: hemostasis, thrombosis, and atherosclerosis studies.Translation and Clinical Development of Antithrombotic Aptamers.A mechanism for localized dynamics-driven affinity regulation of the binding of von Willebrand factor to platelet glycoprotein Ibα.Crystal structure of a DNA aptamer bound to PvLDH elucidates novel single-stranded DNA structural elements for folding and recognition.Using modified aptamers for site specific protein-aptamer conjugations.Aptamers as therapeutics in cardiovascular diseases.Characterization of aptamer-protein complexes by X-ray crystallography and alternative approaches.Quantitative and sensitive protein detection strategies based on aptamers.Targeting von Willebrand factor as a novel anti-platelet therapy; application of ARC1779, an Anti-vWF aptamer, against thrombotic risk.Through-bond effects in the ternary complexes of thrombin sandwiched by two DNA aptamers.Nucleic acid aptamers in cancer research, diagnosis and therapy.Aptamers as Therapeutics.Evolving Aptamers with Unnatural Base Pairs.Mismodeled purines: implicit alternates and hidden Hoogsteens.Using Genome Sequence to Enable the Design of Medicines and Chemical Probes.Aptamers and Their Significant Role in Cancer Therapy and Diagnosis.

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P2860

A Structural Explanation for the Antithrombotic Activity of ARC1172, a DNA Aptamer that Binds von Willebrand Factor Domain A1

http://www.wikidata.org/entity/Q27658166

description

2009 nî lūn-bûn

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2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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A Structural Explanation for t ...... on Willebrand Factor Domain A1

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A Structural Explanation for t ...... on Willebrand Factor Domain A1

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A Structural Explanation for t ...... on Willebrand Factor Domain A1

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Daved H Fremont

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John L Diener

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Ren-Huai Huang

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Robert G Schaub

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P2860

Biochemistry and genetics of von Willebrand factor

Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain

Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations

Electrostatics of nanosystems: application to microtubules and the ribosome

Crystal structure of an RNA aptamer bound to thrombin

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Structural basis of von Willebrand factor activation by the snake toxin botrocetin

Sheared-type G(anti).C(syn) base-pair: a unique d(GXC) loop closure motif

Crystal structure of von Willebrand factor A1 domain complexed with snake venom, bitiscetin: insight into glycoprotein Ibalpha binding mechanism induced by snake venom proteins

Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab

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1476-84

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3048765

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10.1016/J.STR.2009.09.011

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11

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19913482

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structural biology

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3845234

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