Ubiquitin-dependent regulation of COPII coat size and function

Metastasis: from dissemination to organ-specific colonization

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Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome

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Control of the Embryonic Stem Cell State

Young, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.01.032 · Cited by 1,246

Genome-wide association of early-onset myocardial infarction with single nucleotide polymorphisms and copy number variants

Myocardial Infarction Genetics Consortium (2009) · Nature Genetics · doi:10.1038/ng.327 · Cited by 1,088

Cancer as an overhealing wound: an old hypothesis revisited

Schäfer, M., & Werner, S. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2455 · Cited by 974

BTB Protein Keap1 Targets Antioxidant Transcription Factor Nrf2 for Ubiquitination by the Cullin 3-Roc1 Ligase

Furukawa, M., & Xiong, Y. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.25.1.162-171.2005 · Cited by 759

Latent Bone Metastasis in Breast Cancer Tied to Src-Dependent Survival Signals

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Activation of Phosphoinositide 3-OH Kinase by the α6β4 Integrin Promotes Carcinoma Invasion

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Deletion of beta 1 integrins in mice results in inner cell mass failure and peri-implantation lethality.Preprint

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BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3

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Regulation of blood pressure and renal electrolyte balance by Cullin-RING ligases

Uchida, S. (2014) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0000000000000049 · Cited by 16

Inhibition of cargo export at ER exit sites and the trans-Golgi network by the secretion inhibitor FLI-06

Yonemura, Y., Li, X., Müller, K., Krämer, A., Atigbire, P., Mentrup, T., Feuerhake, T., Kroll, T. C., Shomron, O., Nohl, R., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.186163 · Cited by 16

Identification of Cysteine Ubiquitylation Sites on the Sec23A Protein of the COPII Complex Required for Vesicle Formation from the ER

Amodio, G., Margarucci, L., Moltedo, O., Casapullo, A., & Remondelli, P. (2017) · The Open Biochemistry Journal · doi:10.2174/1874091x01711010036 · Cited by 16

Can modulators of apolipoproteinB biogenesis serve as an alternate target for cholesterol-lowering drugs?

Doonan, L. M., Fisher, E. A. A., & Brodsky, J. L. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.03.010 · Cited by 17

Kelch-like protein 5-mediated ubiquitination of lysine 183 promotes proteasomal degradation of sphingosine kinase 1

Powell, J. A., Pitman, M. R., Zebol, J. R., Moretti, P. A. B., Neubauer, H. A., Davies, L. T., Lewis, A. C., Dagley, L. F., Webb, A. I., Costabile, M., et al. (2019) · Biochemical Journal · doi:10.1042/bcj20190245 · Cited by 16

Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficking and disease susceptibility

Mao, H., Aryal, B., Langenecker, T., Hagmann, J., Geisler, M. M., & Grebe, M. (2017) · Nature Plants · doi:10.1038/s41477-017-0039-z · Cited by 16

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

Diagnostic and Clinical Value of Specific Autoantibodies against Kelch-like 12 Peptide and Nuclear Envelope Proteins in Patients with Primary Biliary Cholangitis

Bauer, A., Habior, A., & Gaweł, D. (2022) · Biomedicines · doi:10.3390/biomedicines10040801 · Cited by 15

Targeting kelch-like (KLHL) proteins: achievements, challenges and perspectives

Zhou, Y., Zhang, Q., Zhao, Z., Hu, X., You, Q., & Jiang, Z. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116270 · Cited by 15

Gene-wide Association Study Reveals RNF122 Ubiquitin Ligase as a Novel Susceptibility Gene for Attention Deficit Hyperactivity Disorder

Iris Garcia-martinez, A., Sánchez‐Mora, C., Artigas, M. S., Rovira, P., Pagerols, M., Montse Corrales, F., Calvo-Sánchez, E., Vanesa Richarte, B., Bustamante, M., Sunyer, J., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05514-7 · Cited by 16

Folded or Degraded in Endoplasmic Reticulum

Li, C., Xia, B., Wang, S., & Xu, J. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-3266-5_12 · Cited by 17

Prospect of divergent roles for the CUL3 system in vascular endothelial cell function and angiogenesis

Sakaue, T., Maekawa, M., Nakayama, H., & Higashiyama, S. (2017) · The Journal of Biochemistry · doi:10.1093/jb/mvx051 · Cited by 14

The roles of KLHL family members in human cancers.

Ye, G., Wang, J., Yang, W., Li, J., Meng, Y., & Jin, X. (2022) · PubMed Central · Cited by 13

Tag Team Ubiquitin Ligases

Kleiger, G., & Deshaies, R. J. (2016) · Cell · doi:10.1016/j.cell.2016.08.014 · Cited by 14

Control of craniofacial and brain development by Cullin3-RING ubiquitin ligases: Lessons from human disease genetics

Asmar, A. J., Beck, D. B., & Werner, A. A. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112300 · Cited by 13

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 16

Cargo Receptor-Mediated ER Export in Lipoprotein Secretion and Lipid HomeostasisPreprint

Wang, X., & Chen, X. (2022) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041260 · Cited by 14

Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex

Zhao, B., Payne, W. G., Sai, J., Lu, Z., Olejniczak, E. T., & Fesik, S. W. (2020) · Biochemistry · doi:10.1021/acs.biochem.9b01073 · Cited by 13

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

Cullin-3 and the endocytic system

Hubner, M., & Peter, M. (2012) · Cellular Logistics · doi:10.4161/cl.20372 · Cited by 13

A ubiquitin-based effector-to-inhibitor switch coordinates early brain, craniofacial, and skin development

Asmar, A. J., Abrams, S. R., Hsin, J., Collins, J. C., Yazejian, R. M., Wu, Y., Cho, J., Doyle, A. D., Cinthala, S., Simon, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40223-y · Cited by 11

C9orf72-Associated Dipeptide Repeat Expansions Perturb ER-Golgi Vesicular Trafficking, Inducing Golgi Fragmentation and ER Stress, in ALS/FTD

Sultana, J., Ragagnin, A., Parakh, S., Saravanabavan, S., Soo, K. Y., Vidal, M., Jagaraj, C. J., Ding, K., Wu, S., Shadfar, S., et al. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04187-4 · Cited by 12

Endoplasmic Reticulum Exit of Golgi-resident Defective for SREBP Cleavage (Dsc) E3 Ligase Complex Requires Its Activity

Raychaudhuri, S., & Espenshade, P. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.630863 · Cited by 12

Transport through the Golgi in Trypanosoma brucei

Warren, G. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1112-y · Cited by 12

Detection of Anti-kelch-like 12 and Anti-hexokinase 1 Antibodies in Primary Biliary Cholangitis Patients in China

Bin, L., Liu, Z., & Xu, L. (2020) · Revista Española de Enfermedades Digestivas · doi:10.17235/reed.2020.7483/2020 · Cited by 12

ALS/FTD-associated mutation in cyclin F inhibits ER-Golgi trafficking, inducing ER stress, ERAD and Golgi fragmentation

Ragagnin, A., Sundaramoorthy, V., Farzana, F., Gautam, S., Saravanabavan, S., Takalloo, Z., Mehta, P. M., Do‐Ha, D., Parakh, S., Shadfar, S., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-46802-9 · Cited by 11

C9orf72 controls hepatic lipid metabolism by regulating SREBP1 transport

Wu, Y., Zheng, W., Xu, G., Zhu, L., Li, Z., Chen, J., Wang, L., & Chen, S. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01312-7 · Cited by 11

Dynamic regulation of the oxidative stress response by the E3 ligase TRIP12

Ingersoll, A. J., McCloud, D. M., Hu, J. G., & Rapé, M. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116262 · Cited by 11

Three-dimensional visualization of tip-vesicles in growing pollen tubes by electron tomography

Liu, Z., Liao, M., Liang, Z., Gao, J., Huang, Y., Xiang, Y., Ni, T., Erdmann, P. S., & Jiang, L. (2025) · Science China Life Sciences · doi:10.1007/s11427-025-3096-x · Cited by 10

Mechanical stress shapes the cancer cell response to neddylation inhibition

Mittler, F., Obeïd, P., Haguet, V., Allier, C. P., Gerbaud, S., Rulina, A. V., Gidrol, X., & Balakirev, M. Y. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-022-02328-y · Cited by 10

Adaptor functions of the Ca2+-binding protein ALG-2 in protein transport from the endoplasmic reticulum

Shibata, H. (2018) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2018.1525274 · Cited by 9

Mutations and chromosomal rearrangements ofJAK2: not only a myeloid issue

Salmoiraghi, S., Montalvo, M. L. G., D’Agostini, E., Amicarelli, G., Minnucci, G., Spinelli, O., & Rambaldi, A. (2013) · Expert Review of Hematology · doi:10.1586/17474086.2013.826910 · Cited by 10

Pancreatic beta cell ER export in health and diabetes

Barrabi, C., Zhang, K., Liu, M. R., & Chen, X. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1155779 · Cited by 9

The administration of exogenous HSP47 as a collagen-specific therapeutic approach

Besio, R., Garibaldi, N., Sala, A., Tonelli, F., Aresi, C., Maffioli, E., Casali, C., Torriani, C., Biggiogera, M., Villani, S., et al. (2025) · JCI Insight · doi:10.1172/jci.insight.181570 · Cited by 9

KLHL12 can form large COPII structures in the absence of CUL3 neddylation

Moretti, T., Kim, K., Tuladhar, A., & Kim, J. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e22-08-0383 · Cited by 9

Morpho-Functional Architecture of the Golgi Complex of Neuroendocrine Cells

Martínez‐Alonso, E., Tomás, M., & Martínez‐Menárguez, J. A. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00041 · Cited by 13

The Ubiquitin Ligase CBLC Maintains the Network Organization of the Golgi Apparatus

Lee, W. Y., Goh, G. Y. L., Chia, J., Boey, A., Gounko, N. V., & Bard, F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0138789 · Cited by 9

Heat shock protein 60 negatively regulates the biological functions of ubiquitin-like protein MNSFβ in macrophages

Nakamura, M., Notsu, K., & Nakagawa, M. (2019) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-018-3487-5 · Cited by 9

The life cycle of type IV collagen

Srinivasan, S., & Sherwood, D. R. (2025) · Matrix Biology · doi:10.1016/j.matbio.2025.04.004 · Cited by 8

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

Cullin' PLK1 from kinetochores

McGourty, C. A., & Rapé, M. (2013) · Nature Cell Biology · doi:10.1038/ncb2722 · Cited by 8

Characterization of the interaction between the dopamine D4 receptor, KLHL12 and β-arrestins

Skieterska, K., Shen, A., Clarisse, D., Rondou, P., Borroto‐Escuela, D. O., Lintermans, B., Fuxé, K., Xiang, Y. K., & Craenenbroeck, K. V. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.05.003 · Cited by 8

Loss-of-function Mutations of CUL3, a High Confidence Gene for Psychiatric Disorders, Lead to Aberrant Neurodevelopment In Human Induced Pluripotent Stem Cells

Fischer, S. E., Schlotthauer, I., Kizner, V., Macartney, T., Dorner‐Ciossek, C., & Gillardon, F. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.08.028 · Cited by 8

Functional Insights from Studies on the Structure of the Nuclear Pore and Coat Protein ComplexesPreprint

Schwartz, T. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013375 · Cited by 8

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

Sequence-based GWAS in 180 000 German Holstein cattle reveals new candidate genes for milk production traitsPreprint

Križanac, A.-M., Reimer, C., Heise, J., Liu, Z., Pryce, J. E., Bennewitz, J., Thaller, G., Falker‐Gieske, C., & Tetens, J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.06.570350 · Cited by 7

The Ubp3/Bre5 deubiquitylation complex modulates COPII vesicle formation

Gómez‐Navarro, N., Jérôme Boulanger, A., & Miller, E. A. (2020) · Traffic · doi:10.1111/tra.12766 · Cited by 6

Defective protein degradation in genetic disorders

Castel, P. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166366 · Cited by 6

Cargo carriers from the Golgi to the cell surface

Pfeffer, S. R. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.249 · Cited by 6

Cullin3-RING ubiquitin ligases are intimately linked to the unfolded protein response of the endoplasmic reticulumPreprint

Kim, K., Moretti, T., Park, S., & Kim, J. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/428136 · Cited by 6

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 6

The dual nature of KLHL proteins: From cellular regulators to disease drivers

Giulio, V. D., Canciello, A., Carletti, E., Luca, A. D., Giordano, A., Morrione, A., Berardinelli, J., Russo, V., Solari, D., Cavallo, L. M., et al. (2025) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2025.151483 · Cited by 5

Kinetically Distinct Sorting Pathways through the Golgi Exhibit Different Requirements for Arf1

Whitt, M. A., Cox, M. E., Kansal, R. G., & Cox, J. V. (2014) · Traffic · doi:10.1111/tra.12248 · Cited by 5

COPII Vesicles Get Supersized by Ubiquitin

Malhotra, V. (2012) · Cell · doi:10.1016/j.cell.2012.03.006 · Cited by 5

Anderson’s Disease/Chylomicron Retention Disease and Mutations in the SAR1B Gene

Sassolas, A., Filippo, M. D., Aggerbeck, L. P., Peretti, N., & Samson-Boum, M. E. (2012) · InTech eBooks · doi:10.5772/45975 · Cited by 5

Degradation for better survival? Role of ubiquitination in epithelial morphogenesis

Cheng, X., Zheng, J., Li, G., Göbel, V., & Zhang, H. (2018) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1111/brv.12404 · Cited by 5

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

IFN-γ-driven UBE2D3 upregulation impairs antigen presentation pathways and anti-tumor immunity in pancreatic cancer

Wang, S., Yang, W., Peng, T., Zhu, C., Dong, J., Wang, Y., Yuan, H., Sun, Q., Luan, X., Guan, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65762-4 · Cited by 4

Altered contractility, Ca 2+ transients, and cell morphology seen in a patient-specific iPSC-CM model of Ebstein’s anomaly with left ventricular noncompaction

Thareja, S. K., Anfinson, M., Cavanaugh, M., Kim, M.-S., Lamberton, P., Radandt, J., Brown, R. J., Liang, H.-L., Stamm, K., Afzal, M. Z., et al. (2023) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00658.2022 · Cited by 4

Studying lipoprotein trafficking in zebrafish, the case of chylomicron retention disease

Schlegel, A. (2015) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1248-9 · Cited by 4

Regulation of Stem Cells by Cullin-RING Ligase

Fu, L., Cui, C., & Zhang, L. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_6 · Cited by 4

Variants in the 3'-untranslated region of CUL3 is associated with risk of esophageal squamous cell carcinoma

Hu, J.-L., Hu, X.-L., Lu, C., Chen, X., Fu, L., Han, Q., & Cang, S. (2018) · Journal of Cancer · doi:10.7150/jca.27052 · Cited by 4

Sec23IP recruits the Cohen syndrome factor VPS13B/COH1 to ER exit site-Golgi interface for tubular ERGIC formationPreprint

Du, Y., Fan, X., Song, C., Xiong, J., & Ji, W.-K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.28.582656 · Cited by 4

Tissue-specific SEC31A alternative splicing is regulated by RBM47 and controls lipid transport

Ostwaldt, F., Plößner, S., Dimos‐Röhl, B., Preußner, M., & Heyd, F. (2025) · RNA · doi:10.1261/rna.080572.125 · Cited by 3

Intestinal KLHL12 is dispensable for lipid absorption and chylomicron metabolism

Zhao, Z., Lu, W., Li, C., Xu, M., & Wang, B. (2025) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00219.2025 · Cited by 3

Autoantibodies in Primary Biliary Cholangitis: From Classical Markers to Emerging Targets

Mimura, S., Morishita, A., Oura, K., Yano, R., Nakahara, M., Tadokoro, T., Fujita, K., Tani, J., Tatsuta, M., Himoto, T., et al. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14238503 · Cited by 4

Ubiquitin Dynamics in Stem Cell Biology: Current Challenges and Perspectives

de Dieuleveult, M., & Miotto, B. (2020) · BioEssays · doi:10.1002/bies.201900129 · Cited by 2

Activation of RhoC by regulatory ubiquitination is mediated by LNX1 and suppressed by LIS1

Kholmanskikh, S. S., Singh, S., & Ross, M. E. (2022) · Scientific Reports · doi:10.1038/s41598-022-19740-1 · Cited by 3

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

An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination

Puig-Sàrries, P., Bijlmakers, M.-J., Zuin, A., Bichmann, A., Pons, M., & Crosas, B. (2015) · Biochemical Journal · doi:10.1042/bj20141571 · Cited by 3

Heritable Skeletal Disorders Arising from Defects in Processing and Transport of Type I Procollagen from the ER: Perspectives on Possible Therapeutic Approaches

Cutrona, M. B., Morgan, N. E., & Simpson, J. C. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_67 · Cited by 3

USP9X deubiquitinase couples the pluripotency network and cell metabolism to regulate ESC differentiation potentialPreprint

de Dieuleveult, M., Leduc, M., Salataj, E., Ransy, C., Dairou, J., Homma, K., Gall, M. L., Bossard, P., Lombès, A., Bouillaud, F., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.01.13.904904 · Cited by 3

Loss of hepatic VMP1 trapped VLDL in the bilayer of endoplasmic reticulum membrane

Ni, H., Ding, B., & Chen, A. (2023) · Liver Research · doi:10.1016/j.livres.2023.04.001 · Cited by 2

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

KLHL24 mutation drives intermediate filament degradation, mitochondrial dysfunction and fibrosis in heart failure patients

Ramovš, V., Chen, H. S., Patra, A., Tjokrodirijo, R. T. N., van Veelen, P. A., Mulder, A. A., Koning, R. I., Stöger, J. L., Hubner, C., Ibañez‐Arenas, R., et al. (2025) · Cardiovascular Research · doi:10.1093/cvr/cvaf231 · Cited by 2

Cryo-EM structure of the human COP1-DET1 ubiquitin ligase complex

Wang, S., Teng, F., Stjepanović, G., Rao, F., & Su, M.-Y. (2026) · Nature Communications · doi:10.1038/s41467-026-68375-7 · Cited by 2

In silico analysis of alternative splicing events implicated in intracellular trafficking during B-lymphocyte differentiation

Ostwaldt, F., Los, B., & Heyd, F. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1030409 · Cited by 2

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

Biallelic Loss of Function Variant in SEC31A Is Associated With Lethal Neurodevelopmental Disorder, Dysmorphic Features, and Skeletal Defects

Almontashiri, N. A. M., Mushiba, A. M., Alruqi, H., Alharby, E., & Hashmi, J. A. (2024) · Clinical Genetics · doi:10.1111/cge.14680 · Cited by 2

Managing the Adaptive Proteostatic Landscape: Restoring Resilience in Alpha-1 Antitrypsin Deficiency

Wang, C., & Balch, W. E. (2015) · Respiratory medicine · doi:10.1007/978-3-319-23449-6_4 · Cited by 2

Anticorps anti-hexokinase-1 et anti-kelch-like 12, de nouveaux marqueurs de la cholangite biliaire primitive

Khelifi‐Touhami, D., Johanet, C., Choi, S., & Ballot, E. (2022) · Revue Francophone des Laboratoires · doi:10.1016/s1773-035x(22)00252-0 · Cited by 2

Steady-state regulation of COPII-dependent secretory cargo sorting by inositol trisphosphate receptors, calcium, and penta EF hand proteins

Held, A., Lapka, J., Sargeant, J., Hojanazarova, J., Shaheen, A., Galindo, S., Madreiter‐Sokolowski, C. T., Malli, R., Graier, W. F., & Hay, J. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105471 · Cited by 2

Dynamic regulation of the COPII interactome and collagen trafficking by site-specific glycosylation of Sec24DPreprint

Hirata, T., Choudhary, D., Bisnett, B. J., Soderblom, E. J., Knapik, E. W., & Boyce, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.13.659590 · Cited by 2

cTAGE5 / MEA6 Regulates LBR Localization to Maintain Nuclear Envelope Integrity and Safeguard Against Aging

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Mass spectrometry-based multi-omics analysis elucidates immune microenvironmental characteristics and the risk of distant metastasis in N1c colorectal cancer

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