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Bravo-Plaza, I., Hernández‐González, M., Pinar, M., Díaz, J. F., & Peñalva, M. A. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118551 · Cited by 19 · see citing works

The Versatility of Collagen in Pharmacology: Targeting Collagen, Targeting with Collagen

Revert‐Ros, F., Ventura, I., Prieto-Ruiz, J. Á., Hernández‐Andreu, J. M., & Revert, F. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126523 · Cited by 17 · see citing works

Biophysical forces in membrane bending and traffic

Day, K. J., & Stachowiak, J. C. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.02.017 · Cited by 17 · see citing works

ER exit in physiology and disease

Robinson, C. M., Duggan, A., & Forrester, A. R. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1352970 · Cited by 15 · see citing works

Tales of the ER-Golgi Frontier: Drosophila-Centric Considerations on Tango1 Function

Feng, Z. J., Yang, K. L., & Pastor-Pareja, J. C. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.619022 · Cited by 16 · see citing works

STING COPII ER Export Trafficking and Signaling Primed by Phosphorylation Switches

Nan, Y., Cui, D., Guo, J., Ma, X., Wang, J., Guo, L., Li, T., Yang, M., Huang, G., Xu, A., et al. (2025) · Advanced Science · doi:10.1002/advs.202503660 · Cited by 14 · see citing works

TANGO1 interacts with NRTN to promote hepatocellular carcinoma progression by regulating the PI3K/AKT/mTOR signaling pathway

Man, J., Zhou, W., Zuo, S., Zhao, X., Wang, Q., Ma, H., & Li, H. (2023) · Biochemical Pharmacology · doi:10.1016/j.bcp.2023.115615 · Cited by 14 · see citing works

Ubiquitin-specific protease 8 deubiquitinates Sec31A and decreases large COPII carriers and collagen IV secretion

Kawaguchi, K., Endo, A., Fukushima, T., Madoka, Y., Tanaka, T., & Komada, M. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.03.202 · Cited by 14 · see citing works

DYRK3-Controlled Phase Separation Organizes the Early Secretory PathwayPreprint

Gallo, R., Rai, A., & Pelkmans, L. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.10.941757 · Cited by 14 · see citing works

Collagen IV biosynthesis: Intracellular choreography of post-translational modifications

Ishikawa, Y., Lennon, R., Forneris, F., Myllyharju, J., & Salo, A. M. (2025) · Matrix Biology · doi:10.1016/j.matbio.2025.07.002 · Cited by 13 · see citing works

Endoplasmic reticulum–to–Golgi trafficking of procollagen III via conventional vesicular and tubular carriers

Hirata, Y., Matsui, Y., Wada, I., & Hosokawa, N. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e21-07-0372 · Cited by 13 · see citing works

Ultrastructure of COPII vesicle formation in yeast characterized by correlative light and electron microscopy

Melero, A., Jérôme Boulanger, A., Kukulski, W., & Miller, E. A. (2022) · Molecular Biology of the Cell · doi:10.1091/mbc.e22-03-0103 · Cited by 13 · see citing works

A cargo sorting receptor mediates chloroplast protein trafficking through the secretory pathway

Liu, J., Chen, H., Liu, L. X., Meng, X., Liu, Q., Ye, Q., Wen, J., Wang, T., & Dong, J. (2024) · The Plant Cell · doi:10.1093/plcell/koae197 · Cited by 10 · see citing works

Organizing principles underlying COPII-mediated transport

Flood, J. R., Mendina, C. A., & Audhya, A. (2025) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2025.102492 · Cited by 9 · see citing works

Cryo-electron tomography reveals how COPII assembles on cargo-containing membranesPreprint

Pyle, E., Miller, E. A., & Zanetti, G. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.17.576008 · Cited by 9 · see citing works

In situ cryo-ET defines the ultrastructure of ER exit sites in human cells

Downes, K. W., Flood, J. R., Nans, A., der Verren, S. E. V., Audhya, A., & Zanetti, G. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-01964-2 · Cited by 8 · see citing works

Nutrient deprivation alters the rate of COPII subunit recruitment at ER subdomains to tune secretory protein transport

Kasberg, W., Luong, P., Swift, K. A., & Audhya, A. (2023) · Nature Communications · doi:10.1038/s41467-023-44002-7 · Cited by 8 · see citing works

Caspase 1 Enhances Transport and Golgi Organization Protein 1 Expression to Promote Procollagen Export From the Endoplasmic Reticulum in Systemic Sclerosis Contributing to Fibrosis

Connolly, L. M., McFalls, C. M., McMahon, I. G., Bhat, A. M., & Artlett, C. M. (2023) · Arthritis & Rheumatology · doi:10.1002/art.42535 · Cited by 8 · see citing works

TFG regulates inner COPII coat recruitment to facilitate anterograde secretory protein transport

Kasberg, W., Luong, P., Minushkin, K., Pustova, I., Swift, K. A., Zhao, M., & Audhya, A. (2024) · Molecular Biology of the Cell · doi:10.1091/mbc.e24-06-0282 · Cited by 7 · see citing works

Secretory defects in pediatric osteosarcoma result from downregulation of selective COPII coatomer proteins

Wood, R. K., Flory, A. R., Mann, M. J., Talbot, L. J., & Hendershot, L. M. (2022) · iScience · doi:10.1016/j.isci.2022.104100 · Cited by 7 · see citing works

Visualizing membrane trafficking through the electron microscope: cryo-tomography of coat complexes

Markova, E. A., & Zanetti, G. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319005011 · Cited by 7 · see citing works

Hanging the coat on a collar: Same function but different localization and mechanism for COPII

Malis, Y., Hirschberg, K., & Kaether, C. (2022) · BioEssays · doi:10.1002/bies.202200064 · Cited by 7 · see citing works

Unveiling Sec31: The regulator of COPII vesicle-dependent secretion and beyond

Nie, J., & Ma, J. (2025) · iScience · doi:10.1016/j.isci.2025.113612 · Cited by 5 · see citing works

Defects in early secretory pathway transport machinery components and neurodevelopmental disorders

Tang, B. L. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2021-0020 · Cited by 5 · see citing works

Protein networking: nicotinic acetylcholine receptors and their protein–protein-associations

Brockmöller, S., Worek, F., & Rothmiller, S. (2024) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-024-05032-x · Cited by 5 · see citing works

A distant TANGO1 family member promotes vitellogenin export from the ER in C. elegans

Mo, J. H., Zhai, C., Jung, K., Li, Y., Yan, Y., Dong, M., & Mak, H. Y. (2025) · iScience · doi:10.1016/j.isci.2025.111860 · Cited by 5 · see citing works

Molecular mechanisms underlying cTAGE5/MEA6-mediated cargo transport and biological functions

Ma, T., Zhang, F., Wang, Y., & Xu, Z. (2022) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2022.04.001 · Cited by 5 · see citing works

cTAGE5 acts as a Sar1 GTPase regulator for collagen exportPreprint

Sasaki, N., Shiraiwa, M., Maeda, M., Yorimitsu, T., Sato, K., Katada, T., & Saito, K. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/452904 · Cited by 5 · see citing works

TANGO1 Dances to Export of Procollagen from the Endoplasmic Reticulum

Artlett, C. M., & Connolly, L. M. (2023) · Fibrosis · doi:10.35534/fibrosis.2023.10008 · Cited by 3 · see citing works

Conventional and Unconventional Protein Secretion in Yeast and Animal Cells

Tang, X., & Guo, Y. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4059-3_1 · Cited by 3 · see citing works

A general role for MIA3/TANGO1 in secretory pathway organization and functionPreprint

McCaughey, J., Stevenson, N. L., Mantell, J., Neal, C., Paterson, A. R., Heesom, K. J., & Stephens, D. J. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.24.432632 · Cited by 3 · see citing works

p125A (Sec23ip) couples COPII coat assembly with donor-acceptor membrane organization to facilitate tunnel-based trafficPreprint

Long, K. R., Singh, G., Villemeur, M., Brouwers, N., Malhotra, V., Raote, I., & Aridor, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.07.652703 · Cited by 3 · see citing works

Research progress on collagen secretion mechanisms in scarring

Wenkai, Y. E., Xinan, M. E. N. G., & Suhong, X. U. (2025) · Journal of Zhejiang University (Medical Sciences) · doi:10.3724/zdxbyxb-2024-0535 · Cited by 2 · see citing works

Unraveling Chylomicron Retention Disease Enhances Insight into SAR1B GTPase Functions and Mechanisms of Actions, While Shedding Light of Intracellular Chylomicron Trafficking

Levy, E. H., Fallet‐Bianco, C., Auclair, N., Patey, N., Marcil, V., Sané, A. T., & Spahis, S. (2024) · Biomedicines · doi:10.3390/biomedicines12071548 · Cited by 2 · see citing works

New insights into protein secretion: TANGO1 runs rings around the COPII coat

Glick, B. S. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701142 · Cited by 2 · see citing works

Ultrastructure of COPII vesicle formation characterised by correlative light and electron microscopyPreprint

Melero, A., Jérôme Boulanger, A., Kukulski, W., & Miller, E. A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.13.484130 · Cited by 2 · see citing works

A Tubules-First Model for the Origin of Eukaryotic Membrane Traffic

Thattai, M. (2026) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-021424-013933 · Cited by 1 · see citing works

Biomolecular Condensates in and Around the ER–Golgi Interface

Ruiz, M., Bogus, S. M., & Ernst, A. M. (2025) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-032-06936-8_9 · Cited by 1 · see citing works

Beyond Vesicular Traffic: The ERES as the Gateway for Biosynthetic Secretion

Aridor, M. (2026) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-032-16833-7_1 · Cited by 1 · see citing works

Emerging mechanisms of COPII adaptation for large cargo ER export

Phillips, P. M., & Zanetti, G. (2026) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2026.102645 · Cited by 1 · see citing works

SAR1 paralogs differ biochemically in assembly of the COPII coatPreprint

Melville, D. B., Studer, S., & Schekman, R. W. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.09.940833 · Cited by 1 · see citing works

Unconventional COPII-mediated secretory protein trafficking continues in the absence of the Sar1 GTPasePreprint

Kasberg, W., Luong, P., Hanna, M., Minushkin, K., Tsao, A., Lee, H. H., Engin, F., Shankar, R., Block, S., & Audhya, A. (2021) · Research Square · doi:10.21203/rs.3.rs-1168612/v1 · Cited by 1 · see citing works

Mechanical View on the Endoplasmatic Reticulum and Golgi

Mierke, C. T. (2020) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-030-58532-7_7

Linton Mark Traub (1962–2020)

Aridor, M., & Owen, D. J. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202011169

Identifying the Molecular Cause of Extreme Endoplasmic Reticulum Dilation in Pediatric Osteosarcoma and Its Relationship to the Disease

Wood, R. K. (2021) · doi:10.21007/etd.cghs.2021.0555

TANGO1 and SEC12 are copackaged with procollagen I to facilitate the generation of large COPII carriers

Yuan, L., Kenny, S. J., Hemmati, J., Xu, K., & Schekman, R. W. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814810115 · Cited by 55 · see citing works

TANGO1 assembles into rings around COPII coats at ER exit sites

Raote, I., Bellido, M. O., Pirozzi, M., Zhang, C., Melville, D., Parashuraman, S., Zimmermann, T., & Malhotra, V. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201608080 · Cited by 90 · see citing works

New insights into protein secretion: TANGO1 runs rings around the COPII coat

Glick, B. S. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701142 · Cited by 2 · see citing works

Cargo control of bulky carrier formation during collagen export

Chabanon, M., Walani, N., Arroyo, M., & Campelo, F. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2022.11.349

p125A (Sec23ip) couples COPII coat assembly with donor-acceptor membrane organization to facilitate tunnel-based trafficPreprint

Long, K. R., Singh, G., Villemeur, M., Brouwers, N., Malhotra, V., Raote, I., & Aridor, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.07.652703 · Cited by 3 · see citing works