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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:

UPR transducer BBF2H7 allows export of type II collagen in a cargo- and developmental stage–specific manner
Tokiro Ishikawa, Takuya Toyama, Yuki Nakamura, et al.
The Journal of Cell Biology (2017) Vol. 216, Iss. 6, pp. 1761-1774
Open Access | Times Cited: 59

Showing 1-25 of 59 citing articles:

The Unfolded Protein Response and Cell Fate Control
Claudio Hetz, Feroz R. Papa
Molecular Cell (2017) Vol. 69, Iss. 2, pp. 169-181
Open Access | Times Cited: 1228
Principles of Ubiquitin-Dependent Signaling
Eugene Oh, David Akopian, Michael Rapé
Annual Review of Cell and Developmental Biology (2018) Vol. 34, Iss. 1, pp. 137-162
Closed Access | Times Cited: 296
ROS signaling and ER stress in cardiovascular disease
Cristhiaan D. Ochoa, Ru Feng Wu, Lance S. Terada
Molecular Aspects of Medicine (2018) Vol. 63, pp. 18-29
Open Access | Times Cited: 277
Early Events in the Endoplasmic Reticulum Unfolded Protein Response
Steffen Preißler, David Ron
Cold Spring Harbor Perspectives in Biology (2018) Vol. 11, Iss. 4, pp. a033894-a033894
Open Access | Times Cited: 165
Interactome Screening Identifies the ER Luminal Chaperone Hsp47 as a Regulator of the Unfolded Protein Response Transducer IRE1α
Denisse Sepúlveda, Diego Rojas‐Rivera, Diego A. Rodríguez, et al.
Molecular Cell (2018) Vol. 69, Iss. 2, pp. 238-252.e7
Open Access | Times Cited: 152
Roles of the endoplasmic reticulum–resident, collagen-specific molecular chaperone Hsp47 in vertebrate cells and human disease
Shinya Ito, Kazuhiro Nagata
Journal of Biological Chemistry (2018) Vol. 294, Iss. 6, pp. 2133-2141
Open Access | Times Cited: 131
CREB3 Transcription Factors: ER-Golgi Stress Transducers as Hubs for Cellular Homeostasis
Luciana Sampieri, Pablo Di Giusto, Cecilia Álvarez
Frontiers in Cell and Developmental Biology (2019) Vol. 7
Open Access | Times Cited: 115
The endoplasmic reticulum unfolded protein response – homeostasis, cell death and evolution in virus infections
Vibhu Prasad, Urs F. Greber
FEMS Microbiology Reviews (2021) Vol. 45, Iss. 5
Open Access | Times Cited: 72
Tunnels for Protein Export from the Endoplasmic Reticulum
I. Raote, V. Malhotra
Annual Review of Biochemistry (2021) Vol. 90, Iss. 1, pp. 605-630
Open Access | Times Cited: 69
TANGO1 inhibitors reduce collagen secretion and limit tissue scarring
Ishier Raote, Ann-Helen Rosendahl, Hanna-Maria Häkkinen, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 9
ER-to-Golgi Transport: A Sizeable Problem
Janine McCaughey, David Stephens
Trends in Cell Biology (2019) Vol. 29, Iss. 12, pp. 940-953
Open Access | Times Cited: 71
A review of behavioural issues contribution to motorcycle safety
Mustafa Talib Yousif, Ahmad Farhan Mohd Sadullah, Khairil Anwar Abu Kassim
IATSS Research (2019) Vol. 44, Iss. 2, pp. 142-154
Open Access | Times Cited: 70
A molecular signature associated with prolonged survival in glioblastoma patients treated with regorafenib
Alessandra Santangelo, Marzia Rossato, Giuseppe Lombardi, et al.
Neuro-Oncology (2020) Vol. 23, Iss. 2, pp. 264-276
Open Access | Times Cited: 65
Proteostasis governs differential temperature sensitivity across embryonic cell types
Michael W. Dorrity, Lauren M. Saunders, Madeleine Duran, et al.
Cell (2023) Vol. 186, Iss. 23, pp. 5015-5027.e12
Open Access | Times Cited: 21
COPII-dependent ER export in animal cells: adaptation and control for diverse cargo
Janine McCaughey, David Stephens
Histochemistry and Cell Biology (2018) Vol. 150, Iss. 2, pp. 119-131
Open Access | Times Cited: 56
TANGO1 and SEC12 are copackaged with procollagen I to facilitate the generation of large COPII carriers
Lin Yuan, Samuel J. Kenny, Juliet Hemmati, et al.
Proceedings of the National Academy of Sciences (2018) Vol. 115, Iss. 52
Open Access | Times Cited: 56
Site-1 protease deficiency causes human skeletal dysplasia due to defective inter-organelle protein trafficking
Yuji Kondo, Jianxin Fu, Hua Wang, et al.
JCI Insight (2018) Vol. 3, Iss. 14
Open Access | Times Cited: 50
COPII gets in shape: Lessons derived from morphological aspects of early secretion
Meir Aridor
Traffic (2018) Vol. 19, Iss. 11, pp. 823-839
Open Access | Times Cited: 43
Sorting and Export of Proteins at the Endoplasmic Reticulum
Ishier Raote, Sonashree Saxena, Vivek Malhotra
Cold Spring Harbor Perspectives in Biology (2022) Vol. 15, Iss. 5, pp. a041258-a041258
Open Access | Times Cited: 22
Regulatory mechanisms of the cAMP-responsive element binding protein 3 (CREB3) family in cancers
Yu-Xiong Wang, Faping Li, Bin Liu, et al.
Biomedicine & Pharmacotherapy (2023) Vol. 166, pp. 115335-115335
Open Access | Times Cited: 12
Not just a cargo receptor for large cargoes; an emerging role of TANGO1 as an organizer of ER exit sites
Kota Saito, Miharu Maeda
The Journal of Biochemistry (2019) Vol. 166, Iss. 2, pp. 115-119
Open Access | Times Cited: 27
Transcription factors activated through RIP (regulated intramembrane proteolysis) and RAT (regulated alternative translocation)
Jin Ye
Journal of Biological Chemistry (2020) Vol. 295, Iss. 30, pp. 10271-10280
Open Access | Times Cited: 27
CREB3L2-mediated expression of Sec23A/Sec24D is involved in hepatic stellate cell activation through ER-Golgi transport
Shotaro Tomoishi, Shinichi Fukushima, Kentaro Shinohara, et al.
Scientific Reports (2017) Vol. 7, Iss. 1
Open Access | Times Cited: 28
The Role of Mammalian Creb3-Like Transcription Factors in Response to Nutrients
Haris Ali Khan, Carla Margulies
Frontiers in Genetics (2019) Vol. 10
Open Access | Times Cited: 25
CrebA increases secretory capacity through direct transcriptional regulation of the secretory machinery, a subset of secretory cargo, and other key regulators
Dorothy M. Johnson, Michael B. Wells, Rebecca Fox, et al.
Traffic (2020) Vol. 21, Iss. 9, pp. 560-577
Open Access | Times Cited: 23
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