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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:

Phosphorylation of RabGTPasesin the regulation of membrane trafficking
Dieter Waschbüsch, Amir R. Khan
Traffic (2020) Vol. 21, Iss. 11, pp. 712-719
Open Access | Times Cited: 32

Showing 1-25 of 32 citing articles:

Lysosome damage triggers acute formation of ER to lysosomes membrane tethers mediated by the bridge-like lipid transport protein VPS13C
Xinbo Wang, Peng Xu, Amanda Bentley‐DeSousa, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 13
A RAB7A phosphoswitch coordinates Rubicon Homology protein regulation of Parkin-dependent mitophagy
Dan Tudorica, Bishal Basak, Alexia S. Puerta Cordova, et al.
The Journal of Cell Biology (2024) Vol. 223, Iss. 7
Open Access | Times Cited: 10
Tunneling nanotubes: The transport highway for astrocyte-neuron communication in the central nervous system
Cuixiang Zhou, Min Huang, Shasha Wang, et al.
Brain Research Bulletin (2024) Vol. 209, pp. 110921-110921
Open Access | Times Cited: 5
Targeting Small GTPases and Their Prenylation in Diabetes Mellitus
Edyta Gendaszewska‐Darmach, Malgorzata Garstka, K. M. Błażewska
Journal of Medicinal Chemistry (2021) Vol. 64, Iss. 14, pp. 9677-9710
Open Access | Times Cited: 27
Evidence for Rab7b and Its Splice Isoforms Having Distinct Biological Functions from Rab7a
Wah Y. Wong, Shiyuan Liu, Annie Shi Ru Li, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 6, pp. 2610-2610
Open Access
The bridge-like lipid transport protein VPS13C/PARK23 mediates ER–lysosome contacts following lysosome damage
X.F. Wang, Peng Xu, Amanda Bentley‐DeSousa, et al.
Nature Cell Biology (2025)
Open Access
Phosphorylation of Rab29 at Ser185 regulates its localization and role in the lysosomal stress response in concert with LRRK2
Tadayuki Komori, Tomoki Kuwahara, Tetta Fujimoto, et al.
Journal of Cell Science (2023) Vol. 136, Iss. 14
Open Access | Times Cited: 9
Aurora kinase A-mediated phosphorylation triggers structural alteration of Rab1A to enhance ER complexity during mitosis
Wei Zhang, Zijian Zhang, Yun Xiang, et al.
Nature Structural & Molecular Biology (2024) Vol. 31, Iss. 2, pp. 219-231
Closed Access | Times Cited: 3
Food-Derived Peptides: Beneficial CNS Effects and Cross-BBB Transmission Strategies
Zehui Li, Qiao Dang, Peng Wang, et al.
Journal of Agricultural and Food Chemistry (2023) Vol. 71, Iss. 51, pp. 20453-20478
Closed Access | Times Cited: 8
The impact of VPS35 D620N mutation on alternative autophagy and its reversal by estrogen in Parkinson's disease
Tomotaka Shiraishi, Keiko Bono, Hiromi Hiraki, et al.
Cellular and Molecular Life Sciences (2024) Vol. 81, Iss. 1
Open Access | Times Cited: 2
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
Large Rab GTPases: Novel Membrane Trafficking Regulators with a Calcium Sensor and Functional Domains
Takayuki Tsukuba, Yu Yamaguchi, Tomoko Kadowaki
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 14, pp. 7691-7691
Open Access | Times Cited: 13
Rab GTPases as Modulators of Vascular Function
Somasundaram Raghavan, Masuma Akter Brishti, M. Dennis Leo
Cells (2022) Vol. 11, Iss. 19, pp. 3061-3061
Open Access | Times Cited: 9
Molecular basis for the recruitment of the Rab effector protein WDR44 by the GTPase Rab11
Matthew C. Thibodeau, Noah J Harris, Meredith L. Jenkins, et al.
Journal of Biological Chemistry (2022) Vol. 299, Iss. 1, pp. 102764-102764
Open Access | Times Cited: 8
Dual arginine recognition of LRRK2 phosphorylated Rab GTPases
Dieter Waschbüsch, Elena Purlyte, Amir R. Khan
Biophysical Journal (2021) Vol. 120, Iss. 9, pp. 1846-1855
Open Access | Times Cited: 11
Mice with the Rab10 T73V mutation exhibit anxiety-like behavior and alteration of neuronal functions in the striatum
Jing Zhang, Jie Li, Pan You, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2023) Vol. 1869, Iss. 4, pp. 166641-166641
Open Access | Times Cited: 4
Vesicular Trafficking, a Mechanism Controlled by Cascade Activation of Rab Proteins: Focus on Rab27
Camille Menaceur, Océane Dusailly, Fabien Gosselet, et al.
Biology (2023) Vol. 12, Iss. 12, pp. 1530-1530
Open Access | Times Cited: 4
Molecular mechanisms of saliva secretion and hyposecretion
Eun‐Ah Christine Song, Sul‐Hee Chung, Jeong Hee Kim
European Journal Of Oral Sciences (2024) Vol. 132, Iss. 2
Closed Access | Times Cited: 1
Pathogenic LRRK2 causes age-dependent and region-specific deficits in ciliation, innervation and viability of cholinergic neurons
Besma Brahmia, Yahaira Naaldijk, Pallabi Sarkar, et al.
(2024)
Open Access | Times Cited: 1
Construction of Two Independent RAB Family-Based Scoring Systems Based on Machine Learning Algorithms and Definition of RAB13 as a Novel Therapeutic Target for Hepatocellular Carcinoma
Chenhao Jiang, Zijian Liu, Jingsheng Yuan, et al.
International Journal of Molecular Sciences (2023) Vol. 24, Iss. 5, pp. 4335-4335
Open Access | Times Cited: 3
Aberrant Patterns of Sensory-Evoked Activity in the Olfactory Bulb of LRRK2 Knockout Mice
Andrea Maset, Marica Albanesi, Antonio di Soccio, et al.
Cells (2021) Vol. 10, Iss. 11, pp. 3212-3212
Open Access | Times Cited: 4
Cholesterol uptake in the intestine is regulated by the LASP1-AKT-NPC1L1 signaling pathway
Elke Butt, Thorsten Günder, Paulina Stürzebecher, et al.
AJP Gastrointestinal and Liver Physiology (2024) Vol. 327, Iss. 1, pp. G25-G35
Closed Access
Pathogenic LRRK2 causes age-dependent and region-specific deficits in ciliation, innervation and viability of cholinergic neurons
Besma Brahmia, Yahaira Naaldijk, Pallabi Sarkar, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Closed Access
Pathogenic LRRK2 causes age-dependent and region-specific deficits in ciliation, innervation and viability of cholinergic neurons
Besma Brahmia, Yahaira Naaldijk, Pallabi Sarkar, et al.
(2024)
Open Access
Rab3B Proteins: Cellular Functions, Regulatory Mechanisms, and Potential as a Cancer Therapy Target
Jiayi Xu, Huhu Zhang, Lina Yang
Cell Biochemistry and Biophysics (2024)
Closed Access
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