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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.

Requested Article:

Recent advances in structural studies of 14-3-3 protein complexes
Nikolai N. Sluchanko
Advances in protein chemistry and structural biology (2022), pp. 289-324
Closed Access | Times Cited: 19

Showing 19 citing articles:

Structural insights into the functional roles of 14-3-3 proteins
Veronika Obšilová, Tomáš Obšil
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 59
Autonomous Synthesis of Functional, Permanently Phosphorylated Proteins for Defining the Interactome of Monomeric 14-3-3ζ
Phillip Zhu, Stanislau Stanisheuski, Rachel Franklin, et al.
ACS Central Science (2023) Vol. 9, Iss. 4, pp. 816-835
Open Access | Times Cited: 23
Genome-wide analysis of 14-3-3 genes in sugarcane and functional analysis of SsGF2.1 in response to chilling stress
Huili Zhang, Lilan Chen, Yao-Yao Duan, et al.
Industrial Crops and Products (2024) Vol. 209, pp. 118004-118004
Closed Access | Times Cited: 3
Phosphorylation Code of Human Nucleophosmin Includes Four Cryptic Sites for Hierarchical Binding of 14-3-3 Proteins
Anna A. Kapitonova, Kristina V. Perfilova, Richard B. Cooley, et al.
Journal of Molecular Biology (2024) Vol. 436, Iss. 12, pp. 168592-168592
Open Access | Times Cited: 2
Genetic encoding of 3‐nitro‐tyrosine reveals the impacts of 14‐3‐3 nitration on client binding and dephosphorylation
Phillip Zhu, K.T. Nguyen, Aidan Estelle, et al.
Protein Science (2023) Vol. 32, Iss. 3
Open Access | Times Cited: 5
Phosphorylation code of human nucleophosmin includes four cryptic sites for hierarchical binding of 14-3-3 proteins
Anna A. Kapitonova, Kristina V. Perfilova, Richard B. Cooley, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Crystal structure and ligandability of the 14-3-3/pyrin interface
Roxanne Lau, Michael M. Hann, Christian Ottmann
Biochemical and Biophysical Research Communications (2023) Vol. 651, pp. 1-7
Open Access | Times Cited: 4
Myeloid leukemia factor 1: A “double-edged sword” in health and disease
Zixuan Li, Yuanyuan Yang, Kun Wu, et al.
Frontiers in Oncology (2023) Vol. 13
Open Access | Times Cited: 3
Crystal structure reveals canonical recognition of the phosphorylated cytoplasmic loop of human alpha7 nicotinic acetylcholine receptor by 14-3-3 protein
Nikolai N. Sluchanko, Anna A. Kapitonova, Mikhail A. Shulepko, et al.
Biochemical and Biophysical Research Communications (2023) Vol. 682, pp. 91-96
Closed Access | Times Cited: 3
Contemporary biophysical approaches for studying 14-3-3 protein-protein interactions
Bethany Thurairajah, Andrew J. Hudson, Richard G. Doveston
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 5
Rex1BD and the 14-3-3 protein control heterochromatin organization at tandem repeats by linking RNAi and HDAC
Jinxin Gao, Wenqi Sun, Jie Li, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 50
Open Access | Times Cited: 2
Fragment-Based Interrogation of the 14–3–3/TAZ Protein–Protein Interaction
Blaž Andlovic, Dario Valenti, Federica Centorrino, et al.
Biochemistry (2024) Vol. 63, Iss. 17, pp. 2196-2206
Open Access
Neutrophil-specific interactome of ARHGAP25 reveals novel partners and regulatory insights
Péter Sasvári, Aladár Pettkó‐Szandtner, Éva Wisniewski, et al.
Scientific Reports (2024) Vol. 14, Iss. 1
Open Access
Structural basis for the recognition by 14-3-3 proteins of a conditional binding site within the oligomerization domain of human nucleophosmin
Anna A. Kapitonova, Kristina V. Tugaeva, Larisa A. Varfolomeeva, et al.
Biochemical and Biophysical Research Communications (2022) Vol. 627, pp. 176-183
Closed Access | Times Cited: 3
Recent Developments in Islet Biology: A Review With Patient Perspectives
Lahari Basu, Vriti Bhagat, Ma. Enrica Angela Ching, et al.
Canadian Journal of Diabetes (2022) Vol. 47, Iss. 2, pp. 207-221
Open Access | Times Cited: 1
14-3-3 proteins regulate cullin 7-mediated Eag1 degradation
Chang-Heng Hsieh, Chia‐Cheng Chou, Ya-Ching Fang, et al.
Cell & Bioscience (2023) Vol. 13, Iss. 1
Open Access
Ser149 is another potential 14-3-3 ε binding site of Cdc25B in the G2/M transition of mouse fertilized eggs
Wenning He, Hai-Yao Pang, Yanjun Hou, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
Genetic encoding of 3-nitro-tyrosine reveals the impacts of 14-3-3 nitration on client binding and dephosphorylation
Phillip Zhu, K.T. Nguyen, Aidan Estelle, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2022)
Open Access
Novel diagnostic, therapeutic, and prognostic biomarkers for nonalcoholic steatohepatitis-derived hepatocellular carcinoma: Capable to overcome the heterogeneity-specific barrier
Ruyi Qi, Zhiming Huang
Research Square (Research Square) (2022)
Open Access
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