OpenAlex Citation Counts

OpenAlex Citations Logo

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:

The structure of human CST reveals a decameric assembly bound to telomeric DNA
Ci Ji Lim, Alexandra T. Barbour, Arthur J. Zaug, et al.
Science (2020) Vol. 368, Iss. 6495, pp. 1081-1085
Open Access | Times Cited: 101

Showing 1-25 of 101 citing articles:

Highly accurate protein structure prediction with AlphaFold
John Jumper, Richard Evans, Alexander Pritzel, et al.
Nature (2021) Vol. 596, Iss. 7873, pp. 583-589
Open Access | Times Cited: 29615

Shaping human telomeres: from shelterin and CST complexes to telomeric chromatin organization
Ci Ji Lim, Thomas R. Cech
Nature Reviews Molecular Cell Biology (2021) Vol. 22, Iss. 4, pp. 283-298
Open Access | Times Cited: 195

The regulations of telomerase reverse transcriptase (TERT) in cancer
Mingdi Liu, Yuning Zhang, Yong‐Ping Jian, et al.
Cell Death and Disease (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 22

CST–polymerase α-primase solves a second telomere end-replication problem
Hiroyuki Takai, Valentina Aria, Pamela Borges, et al.
Nature (2024) Vol. 627, Iss. 8004, pp. 664-670
Open Access | Times Cited: 21

Molecular mechanisms of telomere biology disorders
Sherilyn Grill, Jayakrishnan Nandakumar
Journal of Biological Chemistry (2020) Vol. 296, pp. 100064-100064
Open Access | Times Cited: 90

Telomere Replication: Solving Multiple End Replication Problems
Erin Bonnell, Emeline Pasquier, Raymund J. Wellinger
Frontiers in Cell and Developmental Biology (2021) Vol. 9
Open Access | Times Cited: 86

Structures of the human CST-Polα–primase complex bound to telomere templates
He Q, Xiuhua Lin, Bianca L. Chavez, et al.
Nature (2022) Vol. 608, Iss. 7924, pp. 826-832
Open Access | Times Cited: 64

G4-quadruplex-binding proteins: review and insights into selectivity
Vanessa Meier‐Stephenson
Biophysical Reviews (2022) Vol. 14, Iss. 3, pp. 635-654
Open Access | Times Cited: 54

Cryo-EM structure of the human CST–Polα/primase complex in a recruitment state
Sarah W. Cai, John C. Zinder, Vladimir Svetlov, et al.
Nature Structural & Molecular Biology (2022) Vol. 29, Iss. 8, pp. 813-819
Open Access | Times Cited: 54

G-Quadruplex-Binding Proteins: Promising Targets for Drug Design
Huiling Shu, Rongxin Zhang, Ke Xiao, et al.
Biomolecules (2022) Vol. 12, Iss. 5, pp. 648-648
Open Access | Times Cited: 49

Immediate-Early, Early, and Late Responses to DNA Double Stranded Breaks
Shaylee R. Kieffer, Noel F. Lowndes
Frontiers in Genetics (2022) Vol. 13
Open Access | Times Cited: 47

Reconstitution of a telomeric replicon organized by CST
Arthur J. Zaug, Karen J. Goodrich, Jessica J. Song, et al.
Nature (2022) Vol. 608, Iss. 7924, pp. 819-825
Open Access | Times Cited: 38

Structure of Tetrahymena telomerase-bound CST with polymerase α-primase
Yao He, He Song, Henry Chan, et al.
Nature (2022) Vol. 608, Iss. 7924, pp. 813-818
Open Access | Times Cited: 37

CST–Polα/Primase: the second telomere maintenance machine
Sarah W. Cai, Titia de Lange
Genes & Development (2023) Vol. 37, Iss. 13-14, pp. 555-569
Open Access | Times Cited: 23

POT1 recruits and regulates CST-Polα/primase at human telomeres
Sarah W. Cai, Hiroyuki Takai, Arthur J. Zaug, et al.
Cell (2024) Vol. 187, Iss. 14, pp. 3638-3651.e18
Open Access | Times Cited: 7

Cold-Shock Domains—Abundance, Structure, Properties, and Nucleic-Acid Binding
Udo Heinemann, Yvette Roske
Cancers (2021) Vol. 13, Iss. 2, pp. 190-190
Open Access | Times Cited: 44

RPA-like single-stranded DNA-binding protein complexes including CST serve as specialized processivity factors for polymerases
Alexandra T. Barbour, Deborah S. Wuttke
Current Opinion in Structural Biology (2023) Vol. 81, pp. 102611-102611
Open Access | Times Cited: 15

Structural Motifs at the Telomeres and Their Role in Regulatory Pathways
Abeer F. R. Alanazi, Gary N. Parkinson, Shozeb Haider
Biochemistry (2024) Vol. 63, Iss. 7, pp. 827-842
Open Access | Times Cited: 6

A mechanistic model of primer synthesis from catalytic structures of DNA polymerase α–primase
E.A. Mullins, Lauren E. Salay, Clarissa L. Durie, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 5, pp. 777-790
Open Access | Times Cited: 6

Human CST complex protects stalled replication forks by directly blocking MRE11 degradation of nascent‐strand DNA
Xinxing Lyu, Kai‐Hang Lei, Pau Biak Sang, et al.
The EMBO Journal (2020) Vol. 40, Iss. 2
Open Access | Times Cited: 41

The evolution of metazoan shelterin
Logan R. Myler, Charles G. Kinzig, Nanda Kumar Sasi, et al.
Genes & Development (2021) Vol. 35, Iss. 23-24, pp. 1625-1641
Open Access | Times Cited: 39

DNA-binding mechanism and evolution of replication protein A
Clément Madru, Markel Martínez‐Carranza, Sébastien Laurent, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 14

An AlphaFold2 map of the 53BP1 pathway identifies a direct SHLD3–RIF1 interaction critical for shieldin activity
Chérine Sifri, Lisa Hoeg, Daniel Durocher, et al.
EMBO Reports (2023) Vol. 24, Iss. 8
Open Access | Times Cited: 14

RPA engages telomeric G-quadruplexes more effectively than CST
Conner L. Olson, Alexandra T. Barbour, Thomas A. Wieser, et al.
Nucleic Acids Research (2023) Vol. 51, Iss. 10, pp. 5073-5086
Open Access | Times Cited: 13

Page 1 - Next Page

Scroll to top