Evidence map›Paper›PMID 30149624›Full record

ArticleMolecules (Basel, Switzerland)2018

Comparative Studies of the Dynamics Effects of BAY60-2770 and BAY58-2667 Binding with Human and Bacterial H-NOX Domains.

Rana Rehan Khalid, Muhammad Tahir Ul Qamar, Arooma Maryam, Ayesha Ashique, Farooq Anwar, Mohammed H Geesi, Abdul Rauf Siddiqi

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

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  5. Structural and Dynamic Insights into the W68L, L85P, and T87A Mutations ofInternational journal of environmental research and public health · 2022
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  6. Determination of Novel Anti-Cancer Agents by Targeting OGG1 Enzyme Using Integrated Bioinformatics Methods.International journal of environmental research and public health · 2021
    Article
  7. Article
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  9. In Silico Core Proteomics and Molecular Docking Approaches for the Identification of Novel Inhibitors againstInternational journal of environmental research and public health · 2021
    Article
  10. Article
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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

7 authors at 4 institutions in 3 countries.

Rana Rehan KhalidDepartment of Biosciences, COMSATS University Islamabad (CUI), Islamabad 45550, Pakistan. ray.binm@gmail.com.
Muhammad Tahir Ul QamarCollege of Informatics, Huazhong Agricultural University (HZAU), Wuhan 430070, China. m.tahirulqamar@webmail.hzau.edu.cn.ORCID 0000-0003-4832-4250
Arooma MaryamDepartment of Biosciences, COMSATS University Islamabad (CUI), Islamabad 45550, Pakistan. aroomabinm@yahoo.com.
Ayesha AshiqueDepartment of Biosciences, COMSATS University Islamabad (CUI), Islamabad 45550, Pakistan. ayeshaashiq28@yahoo.com.
Farooq AnwarDepartment of Chemistry, University of Sargodha, Sargodha 40100, Pakistan. fqanwar@yahoo.com.
Mohammed H GeesiDepartment of Chemistry, College of Sciences and Humanities, Prince Sattam Bin Abdulaziz University, Al Kharj 11942, Saudi Arabia. m.geesi@psau.edu.sa.
Abdul Rauf SiddiqiDepartment of Biosciences, COMSATS University Islamabad (CUI), Islamabad 45550, Pakistan. abdulraufsher@gmail.com.
COMSATS University Islamabad · PKHuazhong Agricultural University · CNPrince Sattam Bin Abdulaziz University · SAUniversity of Sargodha · PK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Soluble guanylate cyclase (sGC) is a key enzyme implicated in various physiological processes such as vasodilation, thrombosis and platelet aggregation. The enzyme's Heme-Nitric oxide/Oxygen (H-NOX) binding domain is the only sensor of nitric oxide (NO) in humans, which on binding with NO activates sGC to produce the second messenger cGMP. H-NOX is thus a hot target for drug design programs. BAY60-2770 and BAY58-2667 are two widely studied activators of sGC. Here we present comparative molecular dynamics studies to understand the molecular details characterizing the binding of BAY60-2770 and BAY58-2667 with the human H-NOX (

Indexed as

Protein Interaction Domains and MotifsBacterial ProteinsEnzyme InhibitorsHemeHumansHydrogen BondingMolecular ConformationMolecular Docking SimulationMolecular Dynamics SimulationNitric OxideOxygenProtein BindingSoluble Guanylyl CyclaseBacterial ProteinsEnzyme InhibitorsHemeNitric OxideOxygenSoluble Guanylyl Cyclasemolecular dynamics simulationquantum calculationsGC activator compoundssoluble guanylate cyclase

Identifiers

PMID30149624
PMCPMC6225106
OpenAlexW2888486261

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.