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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:

Proteomics, phylogenetics, and coexpression analyses indicate novel interactions in the plastid CLP chaperone-protease system
Jui‐Yun Rei Liao, Giulia Friso, Evan S. Forsythe, et al.
Journal of Biological Chemistry (2022) Vol. 298, Iss. 3, pp. 101609-101609
Open Access | Times Cited: 15

Showing 15 citing articles:

Chloroplast proteostasis: A story of birth, life, and death
Linlin Gao, Zheng-Hui Hong, Yinsong Wang, et al.
Plant Communications (2022) Vol. 4, Iss. 1, pp. 100424-100424
Open Access | Times Cited: 32
Protein degrons and degradation: Exploring substrate recognition and pathway selection in plants
Erika Isono, Jianming Li, Pablo Pulido, et al.
The Plant Cell (2024) Vol. 36, Iss. 9, pp. 3074-3098
Closed Access | Times Cited: 6
Intra-chloroplast proteases: A holistic network view of chloroplast proteolysis
Klaas J. van Wijk
The Plant Cell (2024) Vol. 36, Iss. 9, pp. 3116-3130
Closed Access | Times Cited: 5
The lowdown on breakdown: Open questions in plant proteolysis
Nancy A. Eckardt, Tamar Avin‐Wittenberg, Diane C. Bassham, et al.
The Plant Cell (2024) Vol. 36, Iss. 9, pp. 2931-2975
Open Access | Times Cited: 5
Mutant noxy8 exposes functional specificities between the chloroplast chaperones CLPC1 and CLPC2 in the response to organelle stress and plant defence
Bran López, Yovanny Izquierdo, Tomás Cascón, et al.
Plant Cell & Environment (2024) Vol. 47, Iss. 7, pp. 2334-2348
Open Access | Times Cited: 2
A proteostasis network safeguards the chloroplast proteome
Ernesto Llamas, Pablo Pulido
Essays in Biochemistry (2022) Vol. 66, Iss. 2, pp. 219-228
Open Access | Times Cited: 12
Stromal DUF760-1 and DUF760-2 proteins are degraded by the chloroplast Clp protease system but have very different half-lives
Bingjian Yuan, Klaas J. van Wijk
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
Phylogenomic prediction of interaction networks in the presence of gene duplication
Tony C Gatts, Chris deRoux, Linnea E Lane, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
The chloroplast protease system degrades stromal DUF760-1 and DUF-2 domain-containing proteins at different rates
Bingjian Yuan, Klaas J. van Wijk
PLANT PHYSIOLOGY (2024) Vol. 196, Iss. 3, pp. 1788-1801
Closed Access | Times Cited: 1
Molecular determinants of protein half-life in chloroplasts with focus on the Clp protease system
Lioba Inken Winckler, Nico Dißmeyer
Biological Chemistry (2023) Vol. 404, Iss. 5, pp. 499-511
Closed Access | Times Cited: 2
Competition co‐immunoprecipitation reveals the interactors of the chloroplast CPN60 chaperonin machinery
Fabian Ries, Heinrich Lukas Weil, Claudia Herkt, et al.
Plant Cell & Environment (2023) Vol. 46, Iss. 11, pp. 3371-3391
Open Access | Times Cited: 2
Genome-Wide Identification and Expression Analysis of <i>DUF</i>760 Gene Family in Wheat
政 李
Open Journal of Natural Science (2024) Vol. 12, Iss. 03, pp. 510-518
Closed Access
Correlated evolutionary rates reveal novel components and cross-compartment connectivity in plant proteostasis systems
Tony C Gatts, Elizabeth A Rehmann, Daniel B. Sloan, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access
Uvr motifs regulate the chloroplast Clp chaperone–protease system
Marissa Y Annis, Claire M. Ravenburg, Klaas J. van Wijk
Trends in Plant Science (2024) Vol. 30, Iss. 3, pp. 269-282
Closed Access
Competition co-immunoprecipitation reveals interactors of the chloroplast CPN60 chaperonin machinery
Fabian Ries, Heinrich Lukas Weil, Claudia Herkt, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access
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