Regulation of the CUL3 Ubiquitin Ligase by a Calcium-Dependent Co-adaptor

Calcium Signaling

Clapham, D. E. (2007) · Cell · doi:10.1016/j.cell.2007.11.028 · Cited by 4,175 · see citing works

Synaptic, transcriptional and chromatin genes disrupted in autism

Study, T. D., De Rubeis, S., Autism, H. M. C. F., UK10K Consortium, The Autism Sequencing Consortium, He, X., Goldberg, A. P., Poultney, C. S., Samocha, K., Ercument Cicek, A., et al. (2014) · Nature · doi:10.1038/nature13772 · Cited by 2,746 · see citing works

Defining the Human Deubiquitinating Enzyme Interaction Landscape

Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,512 · see citing works

The BioPlex network: a systematic exploration of the human interactome

Huttlin, E. L., Ting, L., Bruckner, R. J., Gebreab, F., Gygi, M. P., Szpyt, J., Tam, S., Zarraga, G., Colby, G., Baltier, K., et al. (2015) · Cell · doi:10.1016/j.cell.2015.06.043 · Cited by 1,425 · cited 2× · see citing works

The impact of the endoplasmic reticulum protein-folding environment on cancer development

Wang, M., & Kaufman, R. (2014) · Nature Reviews. Cancer · doi:10.1038/nrc3800 · Cited by 1,081 · see citing works

Genetic Control of Bone Formation

Karsenty, G., Kronenberg, H. M., & Settembre, C. (2009) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113308 · Cited by 667 · see citing works

TRPA1 is required for histamine-independent, Mas-related G protein–coupled receptor–mediated itch

Wilson, S. R., Gerhold, K. A., Bifolck-Fisher, A., Liu, Q., Patel, K., Dong, X., & Bautista, D. M. (2011) · Nature Neuroscience · doi:10.1038/nn.2789 · Cited by 599 · see citing works

Activation of a Membrane-Bound Transcription Factor by Regulated Ubiquitin/Proteasome-Dependent Processing

Hoppe, T., Matuschewski, K., Rapé, M., Schlenker, S., Ulrich, H. D., & Jentsch, S. (2000) · Cell · doi:10.1016/s0092-8674(00)00080-5 · Cited by 559 · see citing works

Structures of SPOP-Substrate Complexes: Insights into Molecular Architectures of BTB-Cul3 Ubiquitin Ligases

Zhuang, M., Calabrese, M. F., Liu, J., Waddell, M. B., Nourse, A., Hammel, M., Miller, D. J., Walden, H., Duda, D. M., Seyedin, S. N., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.022 · Cited by 486 · see citing works

DHODH modulates transcriptional elongation in the neural crest and melanoma

White, R. M., Cech, J. N., Ratanasirintrawoot, S., Lin, C. Y., Rahl, P. B., Burke, C. J., Langdon, E. M., Tomlinson, M. L., Mosher, J. T., Kaufman, C. K., et al. (2011) · Nature · doi:10.1038/nature09882 · Cited by 452 · see citing works

A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways

Taipale, M., Tucker, G., Peng, J., Krykbaeva, I., Lin, Z., Larsen, B. G., Choi, H., Berger, B., Gingras, A., & Lindquist, S. L. (2014) · Cell · doi:10.1016/j.cell.2014.05.039 · Cited by 388 · see citing works

TANGO1 Facilitates Cargo Loading at Endoplasmic Reticulum Exit Sites

Saito, K., Chen, M., Bard, F., Chen, S., Zhou, H., Woodley, D. T., Polischuk, R., Schekman, R. W., & Malhotra, V. (2009) · Cell · doi:10.1016/j.cell.2008.12.025 · Cited by 379 · see citing works

The KLHL12–Cullin-3 ubiquitin ligase negatively regulates the Wnt–β-catenin pathway by targeting Dishevelled for degradation

Angers, S., Thorpe, C. J., Biechele, T. L., Goldenberg, S. J., Zheng, N., MacCoss, M. J., & Moon, R. T. (2006) · Nature Cell Biology · doi:10.1038/ncb1381 · Cited by 364 · see citing works

KLHL3 mutations cause familial hyperkalemic hypertension by impairing ion transport in the distal nephron

Louis-Dit-Picard, H., Barc, J., Trujillano, D., Miserey‐Lenkei, S., Bouatia‐Naji, N., Pylypenko, O., Beaurain, G., Bonnefond, A., Sand, O., Simian, C., et al. (2012) · Nature Genetics · doi:10.1038/ng.2218 · Cited by 337 · see citing works

Dauer-independent insulin/IGF-1-signalling implicates collagen remodelling in longevity

Ewald, C. Y., Landis, J. N., Abate, J. P., Murphy, C. T., & Blackwell, T. K. (2014) · Nature · doi:10.1038/nature14021 · Cited by 337 · see citing works

Structure of the Sec13/31 COPII coat cage

Stagg, S. M., Gürkan, C., Fowler, D. M., LaPointe, P., Foss, T. R., Potter, C. S., Carragher, B. O., & Balch, W. E. (2006) · Nature · doi:10.1038/nature04339 · Cited by 334 · see citing works

Ubiquitin-dependent regulation of COPII coat size and function

Jin, L., Pahuja, K. B., Wickliffe, K. E., Gorur, A., Baumgärtel, C., Schekman, R., & Rape, M. (2012) · Nature · doi:10.1038/nature10822 · Cited by 330 · see citing works

Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking

Boyadjiev, S. A., Fromme, J. C., Ben, J., Chong, S. S., Nauta, C., Hur, D. J., Zhang, G., Hamamoto, S., Schekman, R. W., Ravazzola, M., et al. (2006) · Nature Genetics · doi:10.1038/ng1876 · Cited by 314 · see citing works

Assembling Neural Crest Regulatory Circuits into a Gene Regulatory Network

Betancur, P. A., Bronner-Fraser, M. E., & Sauka‐Spengler, T. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.042308.113245 · Cited by 305 · see citing works

Extracellular matrix networks in bone remodeling

Alford, A. I., Kozloff, K. M., & Hankenson, K. D. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.05.008 · Cited by 302 · see citing works

The Mechanism of Linkage-Specific Ubiquitin Chain Elongation by a Single-Subunit E2

Wickliffe, K. E., Lorenz, S., Wemmer, D. E., Kuriyan, J., & Rapé, M. (2011) · Cell · doi:10.1016/j.cell.2011.01.035 · Cited by 280 · see citing works

The emerging family of CULLIN3-RING ubiquitin ligases (CRL3s): cellular functions and disease implications

Genschik, P., Sumara, I., & Lechner, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.173 · Cited by 278 · see citing works

N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex

Scott, D. C., Monda, J. K., Bennett, E. J., Harper, J. W., & Schulman, B. A. (2011) · Science · doi:10.1126/science.1209307 · Cited by 270 · see citing works

Mutations in KLHL40 Are a Frequent Cause of Severe Autosomal-Recessive Nemaline Myopathy

Ravenscroft, G., Miyatake, S., Lehtokari, V., Todd, E. J., Vornanen, P., Yau, K. S., Hayashi, Y. K., Miyake, N., Tsurusaki, Y., Doi, H., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.05.004 · Cited by 226 · see citing works

Arrestin Development: Emerging Roles for β-arrestins in Developmental Signaling Pathways

Kovacs, J. J., Hara, M. R., Davenport, C. L., Kim, J., & Lefkowitz, R. J. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.09.011 · Cited by 195 · see citing works

The Genetic Basis of a Craniofacial Disease Provides Insight into COPII Coat Assembly

Fromme, J. C., Ravazzola, M., Hamamoto, S., Balwi, M. A. A., Eyaid, W., Boyadjiev, S. A., Cosson, P., Schekman, R. W., & Orci, L. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.10.005 · Cited by 190 · see citing works

Secretory COPII coat component Sec23a is essential for craniofacial chondrocyte maturation

Lang, M. R., Lapierre, L. A., Frotscher, M., Goldenring, J. R., & Knapik, E. W. (2006) · Nature Genetics · doi:10.1038/ng1880 · Cited by 190 · see citing works

Cell-fate determination by ubiquitin-dependent regulation of translation

Werner, A., Iwasaki, S., McGourty, C. A., Medina-Ruiz, S., Teerikorpi, N., Fedrigo, I., Ingolia, N. T., & Rape, M. (2015) · Nature · doi:10.1038/nature14978 · Cited by 184 · see citing works

E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer

Eletr, Z. M., Huang, D. T. C., Duda, D. M., Schulman, B. A., & Kuhlman, B. A. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb984 · Cited by 167 · see citing works

Sedlin Controls the ER Export of Procollagen by Regulating the Sar1 Cycle

Venditti, R., Scanu, T., Santoro, M. C., Tullio, G. D., Spaar, A., Gaibisso, R., Beznoussenko, G. V., Aa, M., Aa, M., Zelante, L., et al. (2012) · Science · doi:10.1126/science.1224947 · Cited by 165 · see citing works

New insights into craniofacial malformations

Twigg, S. R. F., & Wilkie, A. O. M. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv228 · Cited by 164 · see citing works

The Pathway of Collagen Secretion

Malhotra, V., & Erlmann, P. (2015) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013002 · Cited by 154 · see citing works

Adaptor Protein Self-Assembly Drives the Control of a Cullin-RING Ubiquitin Ligase

Errington, W. J., Khan, M. Q., Bueler, S. A., Rubinstein, J. L., Chakrabartty, A., & Privé, G. G. (2012) · Structure · doi:10.1016/j.str.2012.04.009 · Cited by 139 · see citing works

Calcium Activates Nedd4 E3 Ubiquitin Ligases by Releasing the C2 Domain-mediated Auto-inhibition

Wang, J., Peng, Q., Lin, Q., Childress, C., Carey, D. J., & Yang, W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.086405 · Cited by 135 · see citing works

Lunapark stabilizes nascent three-way junctions in the endoplasmic reticulum

Chen, S., Desai, T. J., McNew, J. A., Gerard, P. D., Novick, P., & Ferro‐Novick, S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1423026112 · Cited by 126 · see citing works

Rapid Ca 2+ -dependent decrease of protein ubiquitination at synapses

Chen, H., Polo, S., Fiore, P. P. D., & Camilli, P. V. D. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2136625100 · Cited by 121 · see citing works

Genetic background has a major effect on the penetrance and severity of craniofacial defects in mice heterozygous for the gene encoding the nucleolar protein treacle

Dixon, J., & Dixon, M. J. (2004) · Developmental Dynamics · doi:10.1002/dvdy.20004 · Cited by 106 · see citing works

Calcineurin and NFAT4 Induce Chondrogenesis

Tomita, M., Reinhold, M. I., Molkentin, J. D., & Naski, M. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200504200 · Cited by 103 · see citing works

A collagen VI–dependent pathogenic mechanism for Hirschsprung’s disease

Soret, R., Mennetrey, M., Bergeron, K., Dariel, A., Neunlist, M., Righini‐Grunder, F., Faure, C. C., Silversides, D. W., Pilon, N., & for the Ente-Hirsch study group (2015) · Journal of Clinical Investigation · doi:10.1172/jci83178 · Cited by 101 · see citing works

Structural studies on the regulation of Ca2+/calmodulin dependent protein kinase II

Stratton, M. M., Chao, L. H., Schulman, H., & Kuriyan, J. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.04.002 · Cited by 89 · see citing works

The Ca 2+ -binding Protein ALG-2 Is Recruited to Endoplasmic Reticulum Exit Sites by Sec31A and Stabilizes the Localization of Sec31A

Yamasaki, A., Tani, K., Yamamoto, A., Kitamura, N., & Komada, M. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-05-0444 · Cited by 89 · see citing works

Ca v 3.2 T-type calcium channel is required for the NFAT-dependent Sox9 expression in tracheal cartilage

Lin, S., Tzeng, B., Lee, K., Smith, R. J., Campbell, K. P., & Chen, C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1323112111 · Cited by 69 · see citing works

CK2 Phosphorylates Sec31 and Regulates ER-To-Golgi Trafficking

Koreishi, M., Yu, S. S. B., Oda, M., Honjo, Y., & Satoh, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054382 · Cited by 60 · see citing works

ALG-2 Attenuates COPII Budding In Vitro and Stabilizes the Sec23/Sec31A Complex

la Cour, J. M., Schindler, A. J., Berchtold, M. W., & Schekman, R. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075309 · Cited by 46 · see citing works

ALG-2 oscillates in subcellular localization, unitemporally with calcium oscillations

la Cour, J. M., Mollerup, J., & Berchtold, M. W. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.143 · Cited by 39 · see citing works

Structural Analysis of the Complex between Penta-EF-Hand ALG-2 Protein and Sec31A Peptide Reveals a Novel Target Recognition Mechanism of ALG-2

Takahashi, T., Kojima, K., Zhang, W., Sasaki, K. E., Ito, M., SUZUKI, H., Kawasaki, M., Soichi Wakatsuki, A., Takahara, T., Shibata, H., et al. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms16023677 · Cited by 33 · see citing works

Genomic factors that shape craniofacial outcome and neural crest vulnerability in FASD

Smith, S. M., Garic, A., Berres, M. E., & Flentke, G. R. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00224 · Cited by 27 · see citing works

Stability of HIB-Cul3 E3 ligase adaptor HIB Is Regulated by Self-degradation and Availability of Its Substrates

Zhou, Z., Xu, C., Chen, P., Liu, C., Pang, S., Yao, X., & Zhang, Q. H. (2015) · Scientific Reports · doi:10.1038/srep12709 · Cited by 24 · see citing works

Ca2+ signalling in the endoplasmic reticulum/secretory granule microdomain

Petersen, O. H. (2015) · Cell Calcium · doi:10.1016/j.ceca.2015.01.006 · Cited by 20 · see citing works

Involvement of the Penta-EF-Hand Protein Pef1p in the Ca2+-Dependent Regulation of COPII Subunit Assembly in Saccharomyces cerevisiae

Yoshibori, M., Yorimitsu, T., & Sato, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040765 · Cited by 12 · see citing works

Targeted protein degradation: expanding the toolbox

Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960 · see citing works

Ubiquitylation at the crossroads of development and disease

Rapé, M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.83 · Cited by 608 · see citing works

Principles of Ubiquitin-Dependent Signaling

Oh, E., Akopian, D., & Rape, M. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062802 · Cited by 339 · see citing works

Cullin-RING Ubiquitin Ligase Regulatory Circuits: A Quarter Century Beyond the F-Box Hypothesis

Harper, J. W., & Schulman, B. A. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-090120-013613 · Cited by 252 · see citing works

Noncanonical autophagy at ER exit sites regulates procollagen turnover

Omari, S., Makareeva, E., Roberts-Pilgrim, A. M., Mirigian, L. S., Jarník, M., Ott, C. M., Lippincott‐Schwartz, J., & Leikin, S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814552115 · Cited by 164 · see citing works

An E3 ligase guide to the galaxy of small-molecule-induced protein degradation

Jevtić, P., Haakonsen, D. L., & Rapé, M. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.002 · Cited by 144 · see citing works

COPII‐mediated trafficking at the ER/ERGIC interface

Peotter, J. L., Kasberg, W., Pustova, I., & Audhya, A. (2019) · Traffic · doi:10.1111/tra.12654 · Cited by 143 · see citing works

ER-to-Golgi trafficking of procollagen in the absence of large carriers

McCaughey, J., Stevenson, N. L., Cross, S., & Stephens, D. J. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201806035 · Cited by 116 · see citing works

Regulating protein breakdown through proteasome phosphorylation

VerPlank, J. J. S., & Goldberg, A. L. (2017) · Biochemical Journal · doi:10.1042/bcj20160809 · Cited by 110 · see citing works

Dosage analysis of the 7q11.23 Williams region identifies <i>BAZ1B</i> as a major human gene patterning the modern human face and underlying self-domestication

Zanella, M., Vitriolo, A., Andirko, A., Martins, P. T., Sturm, S., O’Rourke, T., Laugsch, M., Malerba, N., Skaros, A., Trattaro, S., et al. (2019) · Science Advances · doi:10.1126/sciadv.aaw7908 · Cited by 101 · see citing works

COPII-coated membranes function as transport carriers of intracellular procollagen I

Gorur, A., Yuan, L., Kenny, S. J., Baba, S., Xu, K., & Schekman, R. W. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201702135 · Cited by 99 · see citing works

LncRNA ODIR1 inhibits osteogenic differentiation of hUC-MSCs through the FBXO25/H2BK120ub/H3K4me3/OSX axis

He, S., Yang, S. L., Zhang, Y., Li, X., Gao, D., Zhong, Y., Cao, L., Ma, H., Liu, Y., Li, G., et al. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2148-2 · Cited by 95 · see citing works

Gene expression and cell identity controlled by anaphase-promoting complex

Oh, E., Mark, K. G., Mocciaro, A., Watson, E. R., Prabu, J. R., Denny, D., Kampmann, M., Gamarra, N. I., Zhou, C. Y., & Rapé, M. (2020) · Nature · doi:10.1038/s41586-020-2034-1 · Cited by 95 · see citing works

Kelch-like proteins: Physiological functions and relationships with diseases

Shi, X., Xiang, S., Cao, J., Zhu, H., Yang, B., He, Q., & Ying, M. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104404 · Cited by 88 · see citing works

Dimerization quality control ensures neuronal development and survival

Mena, E. L., Kjolby, R. A. S., Saxton, R. A., Werner, A. A., Lew, B. G., Boyle, J. M., Harland, R. M., & Rapé, M. (2018) · Science · doi:10.1126/science.aap8236 · Cited by 83 · see citing works

ER-to-Golgi Transport: A Sizeable Problem

McCaughey, J., & Stephens, D. J. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.08.007 · Cited by 77 · see citing works

Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian Cell Differentiation

Dubiel, W., Dubiel, D., Wolf, D. A., & Naumann, M. (2017) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2017.11.010 · Cited by 73 · see citing works

Behavioral, circuitry, and molecular aberrations by region-specific deficiency of the high-risk autism gene Cul3

Rapanelli, M., Tan, T., Wang, W., Wang, X., Wang, Z.-J., Zhong, P., Frick, L., Qin, L., Ma, K., Qu, J., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-019-0498-x · Cited by 74 · see citing works

Regulation of the Sar1 GTPase Cycle Is Necessary for Large Cargo Secretion from the Endoplasmic Reticulum

Saito, K., Maeda, M., & Katada, T. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00075 · Cited by 66 · see citing works

In vitro reconstitution of calcium-dependent recruitment of the human ESCRT machinery in lysosomal membrane repair

Shukla, S., Larsen, K. P., Ou, C., Rose, K. M., & Hurley, J. H. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205590119 · Cited by 63 · see citing works

UPR transducer BBF2H7 allows export of type II collagen in a cargo- and developmental stage–specific manner

Ishikawa, T., Toyama, T., Nakamura, Y., Tamada, K., Shimizu, H., Ninagawa, S., Okada, T., Kamei, Y., Ishikawa‐Fujiwara, T., Todo, T., et al. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201609100 · Cited by 62 · see citing works

COPII-dependent ER export in animal cells: adaptation and control for diverse cargo

McCaughey, J., & Stephens, D. J. (2018) · Histochemistry and Cell Biology · doi:10.1007/s00418-018-1689-2 · Cited by 61 · see citing works

Structural basis for dimerization quality control

Mena, E. L., Jevtić, P., Greber, B. J., Gee, C. L., Lew, B. G., Akopian, D., Nogales, E., Kuriyan, J., & Rapé, M. (2020) · Nature · doi:10.1038/s41586-020-2636-7 · Cited by 60 · see citing works

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

Ubiquitin-Dependent Regulation of Stem Cell Biology

Werner, A. A., Manford, A. G., & Rapé, M. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.04.002 · Cited by 50 · see citing works

Cul3 and insomniac are required for rapid ubiquitination of postsynaptic targets and retrograde homeostatic signaling

Kikuma, K., Li, X., Perry, S., Li, Q., Goel, P., Chen, C., Kim, D., Stavropoulos, N., & Dickman, D. K. (2019) · Nature Communications · doi:10.1038/s41467-019-10992-6 · Cited by 53 · see citing works

Dynamic Glycosylation Governs the Vertebrate COPII Protein Trafficking Pathway

Cox, N. J., Ünlü, G., Bisnett, B. J., Meister, T. R., Condon, B. M., Luo, P. M., Smith, T. J., Hanna, M., Chhetri, A., Soderblom, E. J., et al. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00870 · Cited by 50 · see citing works

Integration of cellular ubiquitin and membrane traffic systems: focus on deubiquitylases

Clague, M. J., & Urbé, S. (2017) · FEBS Journal · doi:10.1111/febs.14007 · Cited by 50 · see citing works

PLEKHA4/kramer Attenuates Dishevelled Ubiquitination to Modulate Wnt and Planar Cell Polarity Signaling

Shah, A. S., Batrouni, A. G., Kim, D.-S., Punyala, A., Cao, W., Han, C., Goldberg, M. L., Smolka, M. B., & Baskin, J. M. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.04.060 · Cited by 48 · see citing works

Ubiquitin-dependent remodeling of the actin cytoskeleton drives cell fusion

Rodríguez-Pérez, F., Manford, A. G., Pogson, A. N., Ingersoll, A. J., Martínez-González, B., & Rapé, M. (2021) · Developmental Cell · doi:10.1016/j.devcel.2021.01.016 · Cited by 46 · see citing works

TRPC proteins contribute to development of diabetic retinopathy and regulate glyoxalase 1 activity and methylglyoxal accumulation

Sachdeva, R., Schlotterer, A., Schumacher, D., Matka, C., Mathar, I., Dietrich, N., Medert, R., Kriebs, U., Lin, J., Nawroth, P. P., et al. (2018) · Molecular Metabolism · doi:10.1016/j.molmet.2018.01.003 · Cited by 44 · see citing works

The small GTPase Sar1, control centre of COPII trafficking

der Verren, S. E. V., & Zanetti, G. (2023) · FEBS Letters · doi:10.1002/1873-3468.14595 · Cited by 43 · see citing works

Quality control of protein complex composition

Padovani, C., Jevtić, P., & Rapé, M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.02.029 · Cited by 43 · see citing works

Modulation of DNA methylation and protein expression in the prefrontal cortex by repeated administration of D-lysergic acid diethylamide (LSD): Impact on neurotropic, neurotrophic, and neuroplasticity signaling

Inserra, A., Campanale, A., Cheishvili, D., Dymov, S., Wong, A. H. Y., Marçal, N., Syme, R. A., Taylor, L., Gregorio, D. D., Kennedy, T. E., et al. (2022) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2022.110594 · Cited by 41 · see citing works

COPII gets in shape: Lessons derived from morphological aspects of early secretion

Aridor, M. (2018) · Traffic · doi:10.1111/tra.12603 · Cited by 40 · see citing works

Synaptic homeostats: latent plasticity revealed at the Drosophila neuromuscular junction

Goel, P., & Dickman, D. K. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03732-3 · Cited by 43 · see citing works

Mechanisms of COPII coat assembly and cargo recognition in the secretory pathway

Downes, K. W., & Zanetti, G. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00839-y · Cited by 39 · see citing works

Mechanisms of procollagen and HSP47 sorting during ER-to-Golgi trafficking

Omari, S., Makareeva, E., Gorrell, L. M., Jarník, M., Lippincott‐Schwartz, J., & Leikin, S. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.06.002 · Cited by 38 · see citing works

Structural Basis for Recruitment of DAPK1 to the KLHL20 E3 Ligase

Chen, Z., Picaud, S., Filippakopoulos, P., D'Angiolella, V., & Bullock, A. N. (2019) · Structure · doi:10.1016/j.str.2019.06.005 · Cited by 37 · see citing works

Cul3‐Klhl18 ubiquitin ligase modulates rod transducin translocation during light‐dark adaptation

Chaya, T., Tsutsumi, R., Varner, L. R., Maeda, Y., Yoshida, S., & Furukawa, T. (2019) · The EMBO Journal · doi:10.15252/embj.2018101409 · Cited by 37 · see citing works

Sorting and Export of Proteins at the Endoplasmic ReticulumPreprint

Raote, I., Saxena, S., & Malhotra, V. (2022) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041258 · Cited by 37 · see citing works

Membrane Transport at an Organelle Interface in the Early Secretory Pathway: Take Your Coat Off and Stay a While

Hanna, M. G., Peotter, J. L., Frankel, E. B., & Audhya, A. (2018) · BioEssays · doi:10.1002/bies.201800004 · Cited by 35 · see citing works

Cullin 3, a cellular scripter of the non-proteolytic ubiquitin code

Jerabkova, K., & Sumara, I. (2019) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2018.12.007 · Cited by 33 · see citing works

Modular UBE2H-CTLH E2-E3 complexes regulate erythroid maturation

Sherpa, D., Mueller, J., Karayel, Ö., Xu, P., Yao, Y., Chrustowicz, J., Gottemukkala, K. V., Baumann, C., Groß, A., Czarnecki, O., et al. (2022) · eLife · doi:10.7554/elife.77937 · Cited by 31 · see citing works

Multisite dependency of an E3 ligase controls monoubiquitylation-dependent cell fate decisions

Werner, A. A., Baur, R., Teerikorpi, N., Kaya, D. U., & Rapé, M. (2018) · eLife · doi:10.7554/elife.35407 · Cited by 33 · see citing works

Calcium–Collagen Coupling is Vital for Biomineralization Schedule

Zhang, J., Ji, Y., Jiang, S., Shi, M., Cai, W., Miron, R. J., & Zhang, Y. (2021) · Advanced Science · doi:10.1002/advs.202100363 · Cited by 33 · see citing works

COPII with ALG2 and ESCRTs control lysosome-dependent microautophagy of ER exit sites

Liao, Y.-C., Pang, S., Li, W., Shtengel, G. E., Choi, H., Schaefer, K., Xu, C. S., & Lippincott‐Schwartz, J. (2024) · Developmental Cell · doi:10.1016/j.devcel.2024.03.027 · Cited by 32 · see citing works

Export Control: Post-transcriptional Regulation of the COPII Trafficking Pathway

Bisnett, B. J., Condon, B. M., Lamb, C. H., Georgiou, G. R., & Boyce, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.618652 · Cited by 30 · see citing works

Reciprocal regulation between lunapark and atlastin facilitates ER three-way junction formation

Zhou, X., He, Y., Huang, X., Guo, Y., Li, D., & Hu, J. (2018) · Protein & Cell · doi:10.1007/s13238-018-0595-7 · Cited by 30 · see citing works

A tango for coats and membranes: New insights into ER-to-Golgi traffic

Aridor, M. (2022) · Cell Reports · doi:10.1016/j.celrep.2021.110258 · Cited by 29 · see citing works

Shigella entry unveils a calcium/calpain-dependent mechanism for inhibiting sumoylation

Lapaquette, P., Fritah, S., Lhocine, N., Andrieux, A., Nigro, G., Mounier, J., Sansonetti, P. J., & Dejean, A. (2017) · eLife · doi:10.7554/elife.27444 · Cited by 28 · see citing works

Ca2+ regulation of constitutive vesicle trafficking

Sargeant, J., & Hay, J. (2022) · Faculty Reviews · doi:10.12703/r/11-6 · Cited by 25 · see citing works

Co-adaptor driven assembly of a CUL3 E3 ligase complex

Akopian, D., McGourty, C. A., & Rapé, M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.01.004 · Cited by 26 · see citing works

The calcium-binding protein ALG-2 regulates protein secretion and trafficking via interactions with MISSL and MAP1B proteins

Takahara, T., Inoue, K., Arai, Y., Kuwata, K., Shibata, H., & Maki, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.800201 · Cited by 23 · see citing works

ALG-2 and peflin regulate COPII targeting and secretion in response to calcium signaling

Sargeant, J., Seiler, D. K., Costain, T., Madreiter‐Sokolowski, C. T., Gordon, D. E., Peden, A. A., Malli, R., Graier, W. F., & Hay, J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101393 · Cited by 22 · see citing works

Identification of a PGXPP degron motif in dishevelled and structural basis for its binding to the E3 ligase KLHL12

Chen, Z., Wasney, G. A., Picaud, S., Filippakopoulos, P., Vedadi, M., D’Angiolella, V., & Bullock, A. N. (2020) · Open Biology · doi:10.1098/rsob.200041 · Cited by 22 · see citing works

Adipocyte-specific deletion of HuR induces spontaneous cardiac hypertrophy and fibrosis

Guarnieri, A., Anthony, S., Gozdiff, A., Green, L. C., Fleifil, S., Slone, S., Nieman, M. L., Alam, P., Benoit, J. B., Owens, A. P., et al. (2021) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00957.2020 · Cited by 22 · see citing works

Mechanism and cellular function of direct membrane binding by the ESCRT and ERES-associated Ca 2+ -sensor ALG-2

Shukla, S., Chen, W., Rao, S., Yang, S., Ou, C., Larsen, K. P., Hummer, G., Hanson, P. I., & Hurley, J. H. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2318046121 · Cited by 21 · see citing works

ESCRT-III function in membrane fission and repair

Burigotto, M., & Carlton, J. G. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00909-1 · Cited by 20 · see citing works

Deciphering GRINA/Lifeguard1: Nuclear Location, Ca2+ Homeostasis and Vesicle Transport

Jiménez-González, V., Ogalla, E., García‐Quintanilla, M., & García-Quintanilla, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20164005 · Cited by 20 · see citing works

De novo mutations within metabolism networks of amino acid/protein/energy in Chinese autistic children with intellectual disability

Chen, W., Liu, B., Zhou, L., Xiong, X., Fu, J., Huang, Z.-F., Tan, T., Tang, M., Wang, J., & Tang, Y. (2022) · Human Genomics · doi:10.1186/s40246-022-00427-7 · Cited by 18 · see citing works

LZTR1 deficiency exerts high metastatic potential by enhancing sensitivity to EMT induction and controlling KLHL12-mediated collagen secretion

Abe, T., Kanno, S.-I., Niihori, T., Terao, M., Takada, S., & Aoki, Y. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-06072-9 · Cited by 19 · see citing works

Intrinsically disordered region-mediated condensation of IFN-inducible SCOTIN/SHISA-5 inhibits ER-to-Golgi vesicle transport

Kim, N., Kim, T.-H., Kim, C., Lee, J., Kang, M., Shin, S., Jung, M., Kim, J., Mun, J. Y., Rhee, H., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.08.030 · Cited by 19 · see citing works

A High-Throughput Assay for Collagen Secretion Suggests an Unanticipated Role for Hsp90 in Collagen Production

Wong, M. Y., Doan, N. D., DiChiara, A. S., Papa, L. J., Cheah, J. H., Soule, C. K., Watson, N., Hulleman, J. D., & Shoulders, M. D. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00378 · Cited by 19 · see citing works

Coat flexibility in the secretory pathway: a role in transport of bulky cargoes

Hutchings, J., & Zanetti, G. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.04.002 · Cited by 19 · see citing works

Evidence for nutrient-dependent regulation of the COPII coat by O-GlcNAcylation

Bisnett, B. J., Condon, B. M., Linhart, N. A., Lamb, C. H., Huynh, D. T., Bai, J., Smith, T. J., Hu, J., Georgiou, G. R., & Boyce, M. (2021) · Glycobiology · doi:10.1093/glycob/cwab055 · Cited by 18 · see citing works

The Novel ALG-2 Target Protein CDIP1 Promotes Cell Death by Interacting with ESCRT-I and VAPA/B

Inukai, R., Mori, K., Kuwata, K., Suzuki, C., Maki, M., Takahara, T., & Shibata, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031175 · Cited by 16 · see citing works

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 14 · see citing works

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 · see citing works

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 · 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

ALG-2 participates in recovery of cells after plasma membrane damage by electroporation and digitonin treatment

la Cour, J. M., Winding, P., Ambjørner, S. E. B., Bagge, J., Jensen, S. M., Panina, S., & Berchtold, M. W. (2018) · PLoS ONE · doi:10.1371/journal.pone.0204520 · Cited by 14 · see citing works

Cullin-3: Renal and Vascular Mechanisms Regulating Blood Pressure

Wu, J. F., McCormick, J. A., & Sigmund, C. D. (2020) · Current Hypertension Reports · doi:10.1007/s11906-020-01076-8 · Cited by 14 · see citing works

ALG2 regulates type I interferon responses by inhibiting STING trafficking

Ji, W., Zhang, L., Xu, X., & Liu, X. (2021) · Journal of Cell Science · doi:10.1242/jcs.259060 · Cited by 13 · see citing works

Tibolone Pre-Treatment Ameliorates the Dysregulation of Protein Translation and Transport Generated by Palmitic Acid-Induced Lipotoxicity in Human Astrocytes: A Label-Free MS-Based Proteomics and Network Analysis

Vesga-Jiménez, D. J., Martín-Jiménez, C., Grismaldo, A., Aristizábal-Pachón, A. F., Pinzón, A. M., Barreto, G. E., Ramírez, D., & González, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126454 · Cited by 13 · see citing works

PINK1 controls RTN3L-mediated ER autophagy by regulating peripheral tubule junctions

Chidambaram, R., Kumar, K., Parashar, S., Gowsalya, R., Chen, S., & Ferro‐Novick, S. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202407193 · Cited by 13 · see citing works

Biallelic Novel USP53 Splicing Variant Disrupting the Gene Function that Causes Cholestasis Phenotype and Review of the Literature

Gezdirici, A., Şengül, Ö. K., Doğan, M., Özgüven, B. Y., & Akbulut, E. (2022) · Molecular Syndromology · doi:10.1159/000523937 · Cited by 13 · see citing works

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 · see citing works

Peripheral blood MicroRNAs as biomarkers of schizophrenia: expectations from a meta-analysis that combines deep learning methods

Han, S., Li, Y., & Gao, J. L. (2023) · The World Journal of Biological Psychiatry · doi:10.1080/15622975.2023.2258975 · Cited by 11 · see citing works

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 · see citing works

Osteoporosis and low bone mass among schizophrenia and bipolar disorder: A cross-sectional study with newly diagnosed, drug-naïve subjects

Li, S., Chen, X., Qiu, Y., Teng, Z., Xu, X., Tang, H., Xiang, H., Wang, B., Chen, J., Yuan, H., et al. (2023) · Journal of Affective Disorders · doi:10.1016/j.jad.2023.12.066 · Cited by 11 · see citing works

Spatacsin regulates directionality of lysosome trafficking by promoting the degradation of its partner AP5Z1

Pierga, A., Matusiak, R., Cauhapé, M., Branchu, J., Danglot, L., Boutry, M., & Darios, F. D. (2023) · PLoS Biology · doi:10.1371/journal.pbio.3002337 · Cited by 10 · see citing works

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 10 · see citing works

Ubr1-induced selective endophagy/autophagy protects against the endosomal and Ca2+-induced proteostasis disease stress

Wang, B. B., Xu, H., Isenmann, S., Huang, C., Elorza-Vidal, X., Rychkov, G. Y., Estévez, R., Schittenhelm, R. B., Lukacs, G. L., & Apaja, P. M. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04191-8 · Cited by 10 · see citing works

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 · see citing works

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 · see citing works

A microtubule-associated protein MAP1B binds to and regulates localization of a calcium-binding protein ALG-2

Takahara, T., Arai, Y., Kono, Y., Shibata, H., & Maki, M. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.02.048 · Cited by 9 · see citing works

Structures and functions of penta-EF-hand calcium-binding proteins and their interacting partners: enigmatic relationships between ALG-2 and calpain-7

Maki, M. (2019) · Bioscience Biotechnology and Biochemistry · doi:10.1080/09168451.2019.1700099 · Cited by 9 · see citing works

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 · see citing works

Calreticulin enhances the secretory trafficking of a misfolded α-1-antitrypsin

Mohan, H. M., Yang, B., Jerome, N. A., & Raghavan, M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014372 · Cited by 8 · see citing works

Interplay in neural functions of cell adhesion molecule close homolog of L1 (CHL1) and Programmed Cell Death 6 (PDCD6)

Loers, G., Theis, T., Hao, B., KLEENE, R. B., Arsha, S., Samuel, N., Arsha, N., Young, W., & Schachner, M. (2021) · FASEB BioAdvances · doi:10.1096/fba.2021-00027 · Cited by 8 · see citing works

Gene expression profiling of orbital muscles in treatment-resistant ophthalmoplegic myasthenia gravis

Europa, T. A., Nel, M., & Heckmann, J. M. (2020) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-020-01629-9 · Cited by 6 · see citing works

Analysis of the Mouse Hepatic Peroxisome Proteome—Identification of Novel Protein Constituents Using a Semi-Quantitative SWATH-MS Approach

Singin, Ö., Astapenka, A., Costina, V., Kühl, S., Bonekamp, N. A., Drews, O., & Islinger, M. (2024) · Cells · doi:10.3390/cells13020176 · Cited by 6 · see citing works

The Cul3 ubiquitin ligase engages Insomniac as an adaptor to impact sleep and synaptic homeostasis

Li, Q., Lim, K. Y., Altawell, R., Verderose, F., Li, X., Dong, W., Martinez, J. C., Dickman, D. K., & Stavropoulos, N. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011574 · Cited by 6 · see citing works

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 · 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

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 · see citing works

Dosage analysis of the 7q11.23 Williams region identifies BAZ1B as a major human gene patterning the modern human face and underlying self-domestication

Zanella, M., Vitriolo, A., Andirkó, A., Martins, P. T., Sturm, S., O’Rourke, T., Laugsch, M., Malerba, N., Skaros, A., Trattaro, S., et al. (2020) · Yearbook of pediatric endocrinology · doi:10.1530/ey.17.14.7 · Cited by 5 · see citing works

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 · 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

Regulated activation of the CUL3 ubiquitin ligase by a calcium-dependent co-adaptor complex

McGourty, C. A. (2016) · eScholarship (California Digital Library)

Co-adaptor driven assembly of a CUL3 E3 ligase complex

Akopian, D., McGourty, C. A., & Rapé, M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.01.004 · Cited by 26 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works