Evidence map›Paper›PMID 34361773›Full record

ArticleMolecules (Basel, Switzerland)2021

Structural and Binding Effects of Chemical Modifications on Thrombin Binding Aptamer (TBA).

Vibhav Valsangkar, Sweta Vangaveti, Goh Woon Lee, Walid M Fahssi, Waqas S Awan, Yicheng Huang, Alan A Chen, Jia Sheng

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 38% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Vibhav ValsangkarDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.
Sweta VangavetiThe RNA Institute, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.
Goh Woon LeeDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.ORCID 0000-0003-4562-1671
Walid M FahssiThe RNA Institute, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.
Waqas S AwanDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.
Yicheng HuangDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.
Alan A ChenDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.ORCID 0000-0001-8246-2935
Jia ShengDepartment of Chemistry, University at Albany, State University of New York, 1400 Washington Avenue, Albany, NY 12222, USA.ORCID 0000-0001-6198-390X
Albany State University · US

Funding

Thermodynamically Calibrated RNA Simulations to Decode Mechanisms of RNAMolecular RecognitionR35GM133469 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI Alan Austin Chen · 2019 to 2026
$2.9M
Environmental Epitranscriptomic Studies and Tools Focused on the Wobble UridineR15GM124627 · NIGMS · STATE UNIVERSITY OF NEW YORK AT ALBANY · PI SHENG, JIA · 2017 to 2017
$443k
NIGMS NIH HHS R15 GM124627NIGMS NIH HHS R35 GM133469NIH HHS R15GM124627 and R35GM133469
6 · The paper itself

Abstract

The thrombin binding aptamer (TBA) is a promising nucleic acid-based anticoagulant. We studied the effects of chemical modifications, such as dendrimer Trebler and NHS carboxy group, on TBA with respect to its structures and thrombin binding affinity. The two dendrimer modifications were incorporated into the TBA at the 5' end and the NHS carboxy group was added into the thymine residues in the thrombin binding site of the TBA G-quadruplex (at T4, T13 and both T4/T13) using solid phase oligonucleotide synthesis. Circular dichroism (CD) spectroscopy confirmed that all of these modified TBA variants fold into a stable G-quadruplex. The binding affinity of TBA variants with thrombin was measured by surface plasmon resonance (SPR). The binding patterns and equilibrium dissociation constants (K

Indexed as

G-QuadruplexesAnticoagulantsAptamers, NucleotideBase SequenceBinding SitesBlood CoagulationDendrimersHumansKineticsMolecular Dynamics SimulationNucleic Acid ConformationOligonucleotidesProtein BindingThermodynamicsThrombinAnticoagulantsAptamers, NucleotideDendrimersOligonucleotidesThrombinthrombin aptamerdendrimersNHS-carboxy Tthrombin binding aptamer (TBA)trebler

Identifiers

PMID34361773
PMCPMC8348300
OpenAlexW3188426966

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.