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:

Structural basis of TRAPPIII‐mediated Rab1 activation
Aaron M.N. Joiner, Ben P. Phillips, Kumar Yugandhar, et al.
The EMBO Journal (2021) Vol. 40, Iss. 12
Open Access | Times Cited: 33

Showing 1-25 of 33 citing articles:

Who’s in control? Principles of Rab GTPase activation in endolysosomal membrane trafficking and beyond
Ann-Christin Borchers, Lars Langemeyer, Christian Ungermann
The Journal of Cell Biology (2021) Vol. 220, Iss. 9
Open Access | Times Cited: 131

Insights into the role of the membranes in Rab GTPase regulation
Stephan Wilmes, Daniel Kümmel
Current Opinion in Cell Biology (2023) Vol. 83, pp. 102177-102177
Open Access | Times Cited: 17

Targeting of the Mon1-Ccz1 Rab guanine nucleotide exchange factor to distinct organelles by a synergistic protein and lipid code
Eric Herrmann, Lars Langemeyer, Kathrin Auffarth, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 3, pp. 102915-102915
Open Access | Times Cited: 16

Structure of a TRAPPII-Rab11 activation intermediate reveals GTPase substrate selection mechanisms
Saket R. Bagde, J. Christopher Fromme
Science Advances (2022) Vol. 8, Iss. 19
Open Access | Times Cited: 20

Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation
B.U. Klink, Eric Herrmann, Claudia Antoni, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 6
Open Access | Times Cited: 19

Structural basis for assembly of TRAPPII complex and specific activation of GTPase Ypt31/32
Chenchen Mi, Li Zhang, Guoqiang Huang, et al.
Science Advances (2022) Vol. 8, Iss. 4
Open Access | Times Cited: 19

Molecular insights into endolysosomal microcompartment formation and maintenance
Daniel Kümmel, Eric Herrmann, Lars Langemeyer, et al.
Biological Chemistry (2022) Vol. 404, Iss. 5, pp. 441-454
Closed Access | Times Cited: 17

Structure of the metazoan Rab7 GEF complex Mon1–Ccz1–Bulli
Eric Herrmann, Jan-Hannes Schäfer, Stephan Wilmes, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 20
Open Access | Times Cited: 10

The TRAPPC8/TRS85 subunit of the Arabidopsis TRAPPIII tethering complex regulates endoplasmic reticulum function and autophagy
Marta Hoffman‐Sommer, Natalia Piłka, Anna Anielska-Mazur, et al.
PLANT PHYSIOLOGY (2025) Vol. 197, Iss. 3
Open Access

Structural insights into traffic through the Golgi complex
Bryce A Brownfield, J. Christopher Fromme
Current Opinion in Cell Biology (2025) Vol. 94, pp. 102505-102505
Closed Access

The flow of proteins through the mammalian secretory pathway described by a phenomenological-based semi-physical model
Santiago Benavides-López, Laura M. Muñoz-Echeverri, Mauricio A. Trujillo‐Roldán, et al.
Biochemical Engineering Journal (2025), pp. 109759-109759
Open Access

The TRAPPIII subunit, Trs85, has a dual role in the trafficking of cellulose synthase complexes in Arabidopsis
Holly Allen, Xiaoyu Zhu, Shundai Li, et al.
The Plant Journal (2024) Vol. 118, Iss. 5, pp. 1475-1485
Open Access | Times Cited: 3

The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11
Antonio Galindo, Sean Munro
FEBS Letters (2022) Vol. 597, Iss. 6, pp. 734-749
Open Access | Times Cited: 14

Focus on the Small GTPase Rab1: A Key Player in the Pathogenesis of Parkinson’s Disease
José A. Martı́nez-Menárguez, Emma Martínez‐Alonso, Mireia Cara‐Esteban, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 21, pp. 12087-12087
Open Access | Times Cited: 16

Biochemical Insight into Novel Rab-GEF Activity of the Mammalian TRAPPIII Complex
Noah J Harris, Meredith L. Jenkins, Udit Dalwadi, et al.
Journal of Molecular Biology (2021) Vol. 433, Iss. 18, pp. 167145-167145
Open Access | Times Cited: 15

The P4‐ATPase Drs2 interacts with and stabilizes the multisubunit tethering complex TRAPPIII in yeast
Irene Pazos, Marta Puig‐Tintó, Laura Betancur, et al.
EMBO Reports (2023) Vol. 24, Iss. 5
Open Access | Times Cited: 6

SP-141 targets Trs85 to inhibit rice blast fungus infection and functions as a potential broad-spectrum antifungal agent
Xi‐Yu Wu, Bo Dong, Xue‐Ming Zhu, et al.
Plant Communications (2023) Vol. 5, Iss. 2, pp. 100724-100724
Open Access | Times Cited: 6

The Small GTPase FgRab1 Plays Indispensable Roles in the Vegetative Growth, Vesicle Fusion, Autophagy and Pathogenicity of Fusarium graminearum
Yanping Yuan, Meiru Zhang, Jingjing Li, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 2, pp. 895-895
Open Access | Times Cited: 9

The Uso1 globular head interacts with SNAREs to maintain viability even in the absence of the coiled-coil domain
Ignacio Bravo-Plaza, Víctor G. Tagua, Herbert N. Arst, et al.
eLife (2023) Vol. 12
Open Access | Times Cited: 5

Structural basis for Rab6 activation by the Ric1-Rgp1 complex
J. Ryan Feathers, Ryan C. Vignogna, J. Christopher Fromme
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 1

The TRAPP complexes: discriminating GTPases in context
Saket R. Bagde, J. Christopher Fromme
FEBS Letters (2022) Vol. 597, Iss. 6, pp. 721-733
Open Access | Times Cited: 6

Structural insights into assembly of TRAPPII and its activation of Rab11/Ypt32
Shan Sun, Sen‐Fang Sui
Current Opinion in Structural Biology (2023) Vol. 80, pp. 102596-102596
Closed Access | Times Cited: 3

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