OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

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Showing 16 citing articles:

A Spectroscopic Overview of Intramolecular Hydrogen Bonds of NH…O,S,N Type
Poul Erik Hansen
Molecules (2021) Vol. 26, Iss. 9, pp. 2409-2409
Open Access | Times Cited: 29

Synthesis of 1‐phenyl‐3‐(quinolin‐8‐ylamino)prop‐2‐en‐1‐one and analysis of its structure by X‐ray crystallography, NMR, UV‐Vis spectroscopy and DFT calculations
M. Yu. Volkov, Alsu R. Sharipova, О. А. Туранова, et al.
ChemistrySelect (2024) Vol. 9, Iss. 8
Closed Access | Times Cited: 3

Experimental and computational studies of tautomerism pyridine carbonyl thiosemicarbazide derivatives
Paweł Kozyra, Agnieszka A. Kaczor, Zbigniew Karczmarzyk, et al.
Structural Chemistry (2023) Vol. 34, Iss. 5, pp. 1973-1984
Open Access | Times Cited: 7

Proposing 5-Steps Rule Is a Notable Milestone for Studying Molecular Biology
Kuo‐Chen Chou
Natural Science (2020) Vol. 12, Iss. 03, pp. 74-79
Open Access | Times Cited: 19

Using Similarity Software to Evaluate Scientific Paper Quality Is a Big Mistake
Kuo‐Chen Chou
Natural Science (2020) Vol. 12, Iss. 03, pp. 42-58
Open Access | Times Cited: 15

Molecular mechanism of amyloidogenicity and neurotoxicity of a pro-aggregated tau mutant in the presence of histidine tautomerism via replica-exchange simulation
Sompriya Chatterjee, Abbas Salimi, Jin Yong Lee
Physical Chemistry Chemical Physics (2021) Vol. 23, Iss. 17, pp. 10475-10486
Closed Access | Times Cited: 13

pLoc_Deep-mHum: Predict Subcellular Localization of Human Proteins by Deep Learning
Yutao Shao, Xinxin Liu, Zhe Lü, et al.
Natural Science (2020) Vol. 12, Iss. 07, pp. 526-551
Open Access | Times Cited: 14

pLoc_Deep-mEuk: Predict Subcellular Localization of Eukaryotic Proteins by Deep Learning
Yutao Shao, Kuo‐Chen Chou
Natural Science (2020) Vol. 12, Iss. 06, pp. 400-428
Open Access | Times Cited: 10

Gordon Life Science Institute and Its Impacts on Computational Biology and Drug Development
Kuo‐Chen Chou
Natural Science (2020) Vol. 12, Iss. 03, pp. 125-161
Open Access | Times Cited: 5

The Chemical Mechanism of Pestilences or Coronavirus Disease 2019 (COVID-19)
Dongdong Zhang, Lin Fang, Li Wang, et al.
Natural Science (2020) Vol. 12, Iss. 11, pp. 717-725
Open Access | Times Cited: 5

The Significant and Profound Impacts of Chou’s 5-Steps Rule
Kuo‐Chen Chou
Natural Science (2020) Vol. 12, Iss. 09, pp. 633-637
Open Access | Times Cited: 4

Synthesis and Structure Identification of 1-[4-(4-pentylcyclohexyl)-phenyl]-3-(quinolin-8-ylamino)prop-2-en-1-one Molecules in Solvents of Different Polarities
M. Yu. Volkov, А. Р. Шарипова, О. А. Туранова
Applied Magnetic Resonance (2024)
Closed Access

Coronavirus and Gordon Life Science Institute
Kuo‐Chen Chou
Natural Science (2020) Vol. 12, Iss. 07, pp. 429-440
Open Access | Times Cited: 3

Showcase to Illustrate How the Web-Server iSulf_Wide-PseAAC Is Working
Kuo‐Chen Chou
Natural Science (2020) Vol. 12, Iss. 08, pp. 620-631
Closed Access | Times Cited: 3

The Topological Entropy Mechanism of Coronavirus Disease 2019 (COVID-19)
Ruomeng Xu, Ludan Lei, Ruihua Qin, et al.
Natural Science (2020) Vol. 12, Iss. 12, pp. 737-742
Open Access | Times Cited: 3

Novel Schiff Bases of C-Methylresorcinarene Derivatives
Albina Y. Ziganshinа, Olga S. Saranova, Rezeda R. Fazleeva, et al.
Molbank (2022) Vol. 2022, Iss. 4, pp. M1505-M1505
Open Access

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