Ubiquitin-dependent regulation of COPII coat size and function

Metastasis: from dissemination to organ-specific colonization

Nguyen, D. X., Bos, P. D., & Massagué, J. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2622 · Cited by 2,637 · see citing works

Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome

Kim, W., Bennett, E. J., Huttlin, E. L., Guo, A., Li, J., Possemato, A. P., Sowa, M. E., Rad, R., Rush, A. J., Comb, M. J., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.025 · Cited by 1,614 · see citing works

Control of the Embryonic Stem Cell State

Young, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.01.032 · Cited by 1,189 · see citing works

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 · see citing works

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 947 · see citing works

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 746 · see citing works

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

Zhang, X. H.-F., Wang, Q., Gerald, W. L., Hudis, C. A., Norton, L., Smid, M., Foekens, J. A., & Massagué, J. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.05.017 · Cited by 663 · see citing works

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

Shaw, L. M., Rabinovitz, I., Wang, H. H.-F., Toker, A., & Mercurio, A. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80486-9 · Cited by 613 · see citing works

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

Stephens, L., Sutherland, A. E., Klimanskaya, I. V., Andrieux, A., Meneses, J., Pedersen, R. A., & Damsky, C. H. (1995) · Genes & Development · doi:10.1101/gad.9.15.1883 · Cited by 596 · see citing works

Integrins: masters and slaves of endocytic transport

Caswell, P. T., Vadrevu, S., & Norman, J. C. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2799 · Cited by 527 · see citing works

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

Xu, L., Yue, W., Reboul, J., Vaglio, P., Shin, T.-H., Vidal, M., Elledge, S. J., & Harper, J. W. (2003) · Nature · doi:10.1038/nature01985 · Cited by 497 · see citing works

The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase

Pintard, L., Willis, J. H., Willems, A. R., Johnson, J.-L., Srayko, M., Kurz, T., Luke-Glaser, S., Mains, P. E., Tyers, M., Bowerman, B. A., et al. (2003) · Nature · doi:10.1038/nature01959 · Cited by 431 · see citing works

Cullin-3 targets cyclin E for ubiquitination and controls S phase in mammalian cellsPreprint

Singer, J. D., Gurian-West, M., Clurman, B. E., & Roberts, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.18.2375 · Cited by 404 · see citing works

Global Identification of Modular Cullin-RING Ligase Substrates

Emanuele, M. J., Elia, A. E. H., Xu, Q., Thoma, C. R., Izhar, L., Leng, Y., Guo, A., Chen, Y., Rush, A. J., Hsu, P. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.09.019 · Cited by 403 · 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

Transmembrane collagen receptors

Leitinger, B. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154013 · Cited by 354 · see citing works

BTB/POZ Domain Proteins Are Putative Substrate Adaptors for Cullin 3 Ubiquitin Ligases

Geyer, R. K., Wee, S., Anderson, S., Yates, J. R., & Wolf, D. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00341-1 · Cited by 339 · see citing works

Bcl‐2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types.

Zhu, W., Cowie, A., Wasfy, G. W., Penn, L. Z., Leber, B. F., & Andrews, D. W. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00788.x · Cited by 327 · 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

Structure and Organization of Coat Proteins in the COPII Cage

Fath, S., Mancias, J. D., Bi, X., & Goldberg, J. D. (2007) · Cell · doi:10.1016/j.cell.2007.05.036 · Cited by 304 · see citing works

Identification of a physiological E2 module for the human anaphase-promoting complex

Williamson, A. P., Wickliffe, K. E., Mellone, B. G., Song, L., Karpen, G. H., & Rapé, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907887106 · Cited by 294 · see citing works

Structural Basis for Cargo Regulation of COPII Coat Assembly

Stagg, S. M., LaPointe, P., Razvi, A., Gürkan, C., Potter, C. S., Carragher, B. O., & Balch, W. E. (2008) · Cell · doi:10.1016/j.cell.2008.06.024 · Cited by 274 · see citing works

Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement

Chen, Y., Yang, Z., Meng, M., Zhao, Y., Dong, N., Yan, H., Liu, L., Ding, M., Peng, H. B., & Shao, F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.004 · Cited by 270 · see citing works

A Cul3-Based E3 Ligase Removes Aurora B from Mitotic Chromosomes, Regulating Mitotic Progression and Completion of Cytokinesis in Human Cells

Sumara, I., Quadroni, M., Frei, C., Olma, M. H., Sumara, G., Ricci, R., & Peter, M. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.03.019 · Cited by 230 · see citing works

COPII-mediated vesicle formation at a glance

Jensen, D., & Schekman, R. W. (2010) · Journal of Cell Science · doi:10.1242/jcs.069773 · Cited by 229 · see citing works

Global defects in collagen secretion in a Mia3/TANGO1 knockout mouse

Wilson, D. G., Phamluong, K., Li, L., Sun, M., Cao, T. C., Liu, P. S., Modrusan, Z. D., Sandoval, W. N., Rangell, L. K., Carano, R. A. D., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201007162 · Cited by 197 · 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-Cell and Cell-Extracellular Matrix Interactions Regulate Embryonic Stem Cell Differentiation

Chen, S. S., Fitzgerald, W., Zimmerberg, J. J., Kleinman, H. K., & Margolis, L. B. (2007) · Stem Cells · doi:10.1634/stemcells.2006-0419 · Cited by 190 · see citing works

Efficient coupling of Sec23-Sec24 to Sec13-Sec31 drives COPII-dependent collagen secretion and is essential for normal craniofacial development

Townley, A. K., Feng, Y., Schmidt, K., Carter, D. A., Porter, R., Verkade, P., & Stephens, D. J. (2008) · Journal of Cell Science · doi:10.1242/jcs.031070 · Cited by 174 · see citing works

cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites

Saito, K., Yamashiro, K., Ichikawa, Y., Erlmann, P., Kontani, K., Malhotra, V., & Katada, T. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-02-0143 · Cited by 173 · see citing works

Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER

Hughes, H., Budnik, A., Schmidt, K., Palmer, K. J., Mantell, J., Noakes, C., Johnson, A., Carter, D. A., Verkade, P., Watson, P., et al. (2009) · Journal of Cell Science · doi:10.1242/jcs.044032 · Cited by 160 · see citing works

Sec24D-Dependent Transport of Extracellular Matrix Proteins Is Required for Zebrafish Skeletal Morphogenesis

Sarmah, S., Barrallo‐Gimeno, A., Melville, D. B., Topczewski, J., Solnica‐Krezel, L., & Knapik, E. W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010367 · Cited by 141 · see citing works

Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells

Stephens, D. J., & Pepperkok, R. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.6.1149 · Cited by 125 · see citing works

COPII-coated vesicles: flexible enough for large cargo?

Fromme, J. C., & Schekman, R. W. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.06.004 · Cited by 103 · see citing works

Genetic Analyses of Integrin SignalingPreprint

Wickstrom, S. A., Radovanac, K., & Fassler, R. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005116 · Cited by 95 · see citing works

Expression of Human COL1A1 Gene in Stably Transfected HT1080 Cells: The Production of a Thermostable Homotrimer of Type I Collagen in a Recombinant System

Geddis, A. E., & Prockop, D. J. (1993) · Matrix · doi:10.1016/s0934-8832(11)80045-4 · Cited by 80 · see citing works

Identification of specific autoantigens in Sjögren's syndrome by SEREX

Uchida, K., Akita, Y., Matsuo, K., Fujiwara, S., Nakagawa, A., Kazaoka, Y., Hachiya, H., Naganawa, Y., Oh‐iwa, I., Ohura, K., et al. (2005) · Immunology · doi:10.1111/j.1365-2567.2005.02197.x · Cited by 72 · see citing works

sec24d encoding a component of COPII is essential for vertebra formation, revealed by the analysis of the medaka mutant, vbi

Ohisa, S., Inohaya, K., Takano, Y., & Kudō, A. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2010.03.016 · Cited by 58 · see citing works

Ubiquitin ligases: structure, function, and regulation

Zheng, N., & Shabek, N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014922 · Cited by 1,499 · see citing works

The increasing complexity of the ubiquitin code

Yau, R., & Rape, M. (2016) · Nature Cell Biology · doi:10.1038/ncb3358 · Cited by 1,054 · 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

Organization of the ER–Golgi interface for membrane traffic control

Brandizzí, F., & Barlowe, C. K. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3588 · Cited by 523 · see citing works

Protein quality control in the secretory pathway

Sun, Z., & Brodsky, J. L. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201906047 · Cited by 381 · 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

Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway

Barlowe, C. K., & Miller, E. A. (2013) · Genetics · doi:10.1534/genetics.112.142810 · Cited by 321 · see citing works

Building and remodelling Cullin–RING E3 ubiquitin ligases

Lydeard, J. R., Schulman, B. A., & Harper, J. W. (2013) · The EMBO Reports · doi:10.1038/embor.2013.173 · Cited by 327 · see citing works

Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases

Canning, P., Cooper, C. D. O., Krojer, T., Murray, J. W., Pike, A. C. W., Chaikuad, A., Keates, T., Thangaratnarajah, C., Hojzan, V., Marsden, B. D., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.437996 · Cited by 284 · 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

Protein sorting at the ER–Golgi interface

Gómez‐Navarro, N., & Miller, E. A. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201610031 · Cited by 276 · see citing works

Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation

Scott, D. C., Rhee, D. Y., Duda, D. M., Kelsall, I. R., Olszewski, J. L., Paulo, J. A., de Jong, A., Ovaa, H., Alpi, A. F., Harper, J. W., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.027 · Cited by 229 · see citing works

Phosphatidylinositol 3-kinase and COPII generate LC3 lipidation vesicles from the ER-Golgi intermediate compartment

Ge, L., Zhang, M., & Schekman, R. W. (2014) · eLife · doi:10.7554/elife.04135 · Cited by 208 · see citing works

Control of the negative IREStrans-acting factor KHSRP by ubiquitination

Kung, Y.-A., Hung, C.-T., Chien, K., & Shih, S. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1042 · Cited by 204 · see citing works

A Cellular Mechanism to Detect and Alleviate Reductive Stress.

Manford, A., Rodríguez-Pérez, F., Shih, K. Y., Shi, Z., Berdan, C. A., Choe, M., Titov, D., Nomura, D., & Rapé, M. (2020) · Cell · doi:10.1016/j.cell.2020.08.034 · Cited by 185 · see citing works

Salivary Exosomes: Emerging Roles in Systemic Disease

Han, Y., Jia, L., Zheng, Y., & Li, W. (2018) · International Journal of Biological Sciences · doi:10.7150/ijbs.25018 · Cited by 193 · 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

K33-Linked Polyubiquitination of Coronin 7 by Cul3-KLHL20 Ubiquitin E3 Ligase Regulates Protein Trafficking

Yuan, W.-C., Lee, Y.-R., Lin, S., Chang, L.-Y., Tan, Y. P., Hung, C., Kuo, J., Liu, C., Lin, M.-Y., Xu, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.035 · Cited by 182 · see citing works

A molecular ensemble in the rER for procollagen maturation

Ishikawa, Y., & Bächinger, H. P. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.04.008 · Cited by 176 · see citing works

TANGO1 builds a machine for collagen export by recruiting and spatially organizing COPII, tethers and membranes

Raote, I., Bellido, M., Santos, A. J. M., Foresti, O., Zhang, C., Parajo, M. F. G., Campelo, F., & Malhotra, V. (2018) · eLife · doi:10.7554/elife.32723 · Cited by 164 · 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

Endoplasmic Reticulum–Associated Degradation and Lipid Homeostasis

Stevenson, J., Huang, E. Y., & Olzmann, J. A. (2016) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071715-051030 · Cited by 158 · 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

A Rab10-Dependent Mechanism for Polarized Basement Membrane Secretion during Organ Morphogenesis

Lerner, D. W., McCoy, D., Isabella, A. J., Mahowald, A. P., Gerlach, G. F., Chaudhry, T. A., & Horne‐Badovinac, S. (2013) · Developmental Cell · doi:10.1016/j.devcel.2012.12.005 · Cited by 152 · see citing works

Vesicle-mediated export from the ER: COPII coat function and regulation

D’Arcangelo, J. G., Stahmer, K. R., & Miller, E. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.003 · Cited by 147 · see citing works

COPII — a flexible vesicle formation system

Miller, E. A., & Schekman, R. W. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2013.04.005 · Cited by 150 · see citing works

Structural basis and regulation of the reductive stress response

Manford, A. G., Mena, E. L., Shih, K. Y., Gee, C. L., McMinimy, R., Martínez-González, B., Sherriff, R., Lew, B., Zoltek, M., Rodríguez-Pérez, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.002 · Cited by 152 · see citing works

Contact of cis-Golgi with ER exit sites executes cargo capture and delivery from the ER

Kurokawa, K., Okamoto, M., & Nakano, A. (2014) · Nature Communications · doi:10.1038/ncomms4653 · Cited by 149 · see citing works

Assembly of COPI and COPII Vesicular Coat Proteins on Membranes

Béthune, J., & Wieland, F. (2018) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070317-033259 · Cited by 149 · 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

The structure of the COPII transport-vesicle coat assembled on membranes

Zanetti, G., Prinz, S., Daum, S., Meister, A., Schekman, R. W., Bacia, K., & Briggs, J. A. G. (2013) · eLife · doi:10.7554/elife.00951 · Cited by 131 · see citing works

The Highly Conserved COPII Coat Complex Sorts Cargo from the Endoplasmic Reticulum and Targets It to the GolgiPreprint

Lord, C. L., Ferro‐Novick, S., & Miller, E. A. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013367 · Cited by 131 · see citing works

KLHL40 deficiency destabilizes thin filament proteins and promotes nemaline myopathy

Garg, A., O’Rourke, J., Long, C., Doering, J., Ravenscroft, G., Bezprozvannaya, S., Nelson, B. R., Beetz, N., Li, L., Chen, S., et al. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74994 · Cited by 127 · see citing works

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

McGourty, C. A., Akopian, D., Walsh, C., Gorur, A., Werner, A., Schekman, R., Bautista, D., & Rape, M. (2016) · Cell · doi:10.1016/j.cell.2016.09.026 · Cited by 126 · see citing works

Selective mRNA translation during eIF2 phosphorylation induces expression of IBTKα

Baird, T. D., Palam, L. R., Fusakio, M. E., Willy, J. A., Davis, C. M., McClintick, J. N., Anthony, T. G., & Wek, R. C. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-02-0704 · Cited by 122 · see citing works

Dynamin-Related Protein 1 Inhibition Attenuates Cardiovascular Calcification in the Presence of Oxidative Stress

Rogers, M. A., Maldonado, N., Hutcheson, J. D., Goettsch, C., Goto, S., Yamada, I., Faits, T., Sesaki, H., Aikawa, M., & Aikawa, E. R. (2017) · Circulation Research · doi:10.1161/circresaha.116.310293 · Cited by 122 · see citing works

Collagen Biosynthesis, Processing, and Maturation in Lung Ageing

Onursal, C., Dick, E., Angelidis, I., Schiller, H. B., & Staab-Weijnitz, C. A. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.593874 · Cited by 122 · see citing works

Differential role of TIMP2 and TIMP3 in cardiac hypertrophy, fibrosis, and diastolic dysfunction

Dong, F., Takawale, A. R., Basu, R., Patel, V. B., Lee, J., Kandalam, V., Wang, X., Oudit, G. Y., & Kassiri, Z. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu072 · Cited by 120 · see citing works

SEC24A deficiency lowers plasma cholesterol through reduced PCSK9 secretion

Chen, X., Wang, H., Pahuja, K. B., Zhang, P., Meng, Z., Ma, D., Bai, Y., Liu, H.-H., Adams, E., Baines, A. C., et al. (2013) · eLife · doi:10.7554/elife.00444 · Cited by 118 · see citing works

Rab1-dependent ER–Golgi transport dysfunction is a common pathogenic mechanism in SOD1, TDP-43 and FUS-associated ALS

Soo, K. Y., Halloran, M. A., Sundaramoorthy, V., Parakh, S., Toth, R. P., Southam, K. A., McLean, C., Lock, P., King, A. E., Farg, M. A., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1468-2 · Cited by 117 · see citing works

Intracellular mechanisms of molecular recognition and sorting for transport of large extracellular matrix molecules

Ishikawa, Y., Ito, S., Nagata, K., Sakai, L. Y., & Bächinger, H. P. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1609571113 · Cited by 119 · see citing works

Ubiquitylation-dependent localization of PLK1 in mitosis

Beck, J., Maerki, S., Posch, M., Metzger, T., Persaud, A. K., Scheel, H., Hofmann, K., Rotin, D., Pedrioli, P. G. A., Swedlow, J. R., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2695 · Cited by 119 · see citing works

TFG clusters COPII‐coated transport carriers and promotes early secretory pathway organization

Johnson, A. J., Bhattacharya, N., Hanna, M., Pennington, J. G., Schuh, A. L., Wang, L., Otegui, M. S., Stagg, S. M., & Audhya, A. (2015) · The EMBO Journal · doi:10.15252/embj.201489032 · Cited by 117 · 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

TANGO1 and Mia2/cTAGE5 (TALI) cooperate to export bulky pre-chylomicrons/VLDLs from the endoplasmic reticulum

Santos, A. J. M., Nogueira, C., Bellido, M., & Malhotra, V. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201603072 · Cited by 111 · see citing works

TANGO1 recruits ERGIC membranes to the endoplasmic reticulum for procollagen export

Santos, A. J. M., Raote, I., Scarpa, M., Brouwers, N., & Malhotra, V. (2015) · eLife · doi:10.7554/elife.10982 · Cited by 114 · see citing works

Extracellular Matrix Communication and Turnover in Cardiac Physiology and Pathology

Takawale, A. R., Sakamuri, S. S. V. P., & Kassiri, Z. (2015) · Comprehensive physiology · doi:10.1002/cphy.c140045 · Cited by 114 · see citing works

TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats

Ma, W., & Goldberg, J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605916113 · Cited by 108 · see citing works

Interaction mapping of endoplasmic reticulum ubiquitin ligases identifies modulators of innate immune signalling

Fenech, E. J., Lari, F., Charles, P. D., Fischer, R., Laétitia-Thézénas, M., Bagola, K., Paton, A. W., Paton, J. C., Gyrd‐Hansen, M., Kessler, B. M., et al. (2020) · eLife · doi:10.7554/elife.57306 · Cited by 104 · see citing works

Concentration of Sec12 at ER exit sites via interaction with cTAGE5 is required for collagen export

Saito, K., Yamashiro, K., Shimazu, N., Tanabe, T., Kontani, K., & Katada, T. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201312062 · Cited by 107 · see citing works

Regulation of endocytic clathrin dynamics by cargo ubiquitination

Henry, A. G., Hislop, J. N., Grove, J., Thorn, K., Marsh, M., & von Zastrow, M. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.08.003 · Cited by 100 · 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

Retrograde Traffic from the Golgi to the Endoplasmic ReticulumPreprint

Spang, A. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013391 · Cited by 98 · see citing works

Cab45 is required for Ca2+-dependent secretory cargo sorting at the trans-Golgi network

von Blume, J., Alleaume, A.-M., Kienzle, C., Carreras‐Sureda, A., Valverde, M. A., & Malhotra, V. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201207180 · Cited by 96 · see citing works

Tango1 spatially organizes ER exit sites to control ER export

Liu, M., Feng, Z. J., Ke, H., Liu, Y., Sun, T., Dai, J., Cui, W., & Pastor-Pareja, J. C. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611088 · Cited by 92 · see citing works

TFG facilitates outer coat disassembly on COPII transport carriers to promote tethering and fusion with ER–Golgi intermediate compartments

Hanna, M. G., Block, S., Frankel, E. B., Hou, F., Johnson, A. J., Yuan, L., Knight, G. T., Moresco, J. J., Yates, J. R., Ashton, R. S., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1709120114 · Cited by 91 · see citing works

CUL3-KBTBD6/KBTBD7 Ubiquitin Ligase Cooperates with GABARAP Proteins to Spatially Restrict TIAM1-RAC1 Signaling

Genau, H. M., Huber, J., Baschieri, F., Akutsu, M., Dötsch, V., Farhan, H., Rogov, V. V., & Behrends, C. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.040 · Cited by 91 · see citing works

Anti‐kelch‐like 12 and anti‐hexokinase 1: novel autoantibodies in primary biliary cirrhosis

Norman, G. L., Yang, C., Ostendorff, H. P., Shums, Z., Lim, M. J., Wang, J., Awad, A., Hirschfield, G. M., Milkiewicz, P., Bloch, D. B., et al. (2015) · Liver International · doi:10.1111/liv.12690 · Cited by 87 · see citing works

The Back and Forth of Cargo Exit from the Endoplasmic Reticulum

Geva, Y., & Schuldiner, M. (2014) · Current Biology · doi:10.1016/j.cub.2013.12.008 · Cited by 89 · 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

COMP-assisted collagen secretion - a novel intracellular function required for fibrosis

Schulz, J.-N., Nüchel, J., Niehoff, A., Bloch, W., Schönborn, K., Hayashi, S., Kamper, M., Brinckmann, J., Plomann, M., Paulsson, M., et al. (2016) · Journal of Cell Science · doi:10.1242/jcs.180216 · 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

Collagen transport and related pathways in Osteogenesis Imperfecta

Claeys, L., Storoni, S., Eekhoff, E. M. W., Elting, M. W., Wisse, L. E., Pals, G., Bravenboer, N., Maugeri, A., & Micha, D. (2021) · Human Genetics · doi:10.1007/s00439-021-02302-2 · Cited by 85 · see citing works

SLY1 and Syntaxin 18 specify a distinct pathway for procollagen VII export from the endoplasmic reticulum

Nogueira, C., Erlmann, P., Villeneuve, J., Santos, A. J. M., Martínez‐Alonso, E., Martínez‐Menárguez, J. A., & Malhotra, V. (2014) · eLife · doi:10.7554/elife.02784 · Cited by 85 · see citing works

Fighting the Fiber: Targeting Collagen in Lung Fibrosis

Staab-Weijnitz, C. A. (2021) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2021-0342tr · Cited by 83 · see citing works

VLDL Biogenesis and Secretion: It Takes a Village

Zwol, W. H.-V., van de Sluis, B., Ginsberg, H. N., & Kuivenhoven, J. A. (2024) · Circulation Research · doi:10.1161/circresaha.123.323284 · Cited by 83 · see citing works

Tunnels for Protein Export from the Endoplasmic Reticulum

Raote, I., & Malhotra, V. (2021) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-080120-022017 · Cited by 82 · see citing works

Functional analysis of Cullin 3 E3 ligases in tumorigenesis

Cheng, J., Guo, J., Wang, Z. P., North, B. J., Tao, K., Dai, X., & Wei, W. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.11.001 · Cited by 80 · 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

Crystal Structure of KLHL3 in Complex with Cullin3

Ji, A. X., & Privé, G. G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060445 · Cited by 76 · see citing works

Exiting the ER: what we know and what we don't.

Venditti, R., Wilson, C., & Matteis, M. D. D. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.08.005 · Cited by 72 · see citing works

Understanding Cullin-RING E3 Biology through Proteomics-based Substrate Identification

Harper, J. W., & Tan, M.-K. M. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r112.021154 · Cited by 71 · see citing works

Protein monoubiquitylation: targets and diverse functions

Nakagawa, T., & Nakayama, K. (2015) · Genes to Cells · doi:10.1111/gtc.12250 · Cited by 69 · see citing works

Quantitative Lys-ϵ-Gly-Gly (diGly) Proteomics Coupled with Inducible RNAi Reveals Ubiquitin-mediated Proteolysis of DNA Damage-inducible Transcript 4 (DDIT4) by the E3 Ligase HUWE1

Thompson, J. W., Nagel, J., Sjouke Hoving, B., Gerrits, B., Bauer, A., Thomas, J. R., Kirschner, M. W., Schirle, M., & Luchansky, S. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.573352 · Cited by 66 · 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

TFG Promotes Organization of Transitional ER and Efficient Collagen Secretion

McCaughey, J., Miller, V. J., Stevenson, N. L., Brown, A. K., Budnik, A., Heesom, K. J., Alibhai, D., & Stephens, D. J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.062 · Cited by 65 · see citing works

Silencing of Mammalian Sar1 Isoforms Reveals COPII ‐Independent Protein Sorting and Transport

Cutrona, M. B., Beznoussenko, G. V., Fusella, A., Martella, O., Moral, P., & Aa, M. (2013) · Traffic · doi:10.1111/tra.12060 · Cited by 63 · see citing works

Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network

Hutchings, J., Stancheva, V. G., Brown, N. R., Cheung, A. C. M., Miller, E. A., & Zanetti, G. (2021) · Nature Communications · doi:10.1038/s41467-021-22110-6 · Cited by 64 · see citing works

The role of ubiquitination in health and disease

Liao, Y., Zhang, W., Liu, Y., Zhu, C., & Zou, Z. (2024) · MedComm · doi:10.1002/mco2.736 · Cited by 67 · see citing works

MicroRNA-based discovery of barriers to dedifferentiation of fibroblasts to pluripotent stem cells

Judson, R. L., Greve, T., Parchem, R. J., & Blelloch, R. H. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2665 · Cited by 62 · 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

Control of chylomicron export from the intestine

Mansbach, C. M., & Siddiqi, S. A. (2016) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00228.2015 · Cited by 61 · see citing works

A pseudoatomic model of the COPII cage obtained from cryo-electron microscopy and mass spectrometry

Noble, A. J., Zhang, Q., O’Donnell, J., Hariri, H. H., Bhattacharya, N., Marshall, A. G., & Stagg, S. M. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2467 · Cited by 61 · 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

Characterizing Ubiquitination Sites by Peptide-based Immunoaffinity Enrichment

Bustos, D. J., Bakalarski, C. E., Yang, Y., Peng, J., & Kirkpatrick, D. S. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r112.019117 · Cited by 60 · 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

Distinct isoform-specific complexes of TANGO1 cooperatively facilitate collagen secretion from the endoplasmic reticulum

Maeda, M., Saito, K., & Katada, T. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-03-0196 · Cited by 60 · 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

CideB Protein Is Required for the Biogenesis of Very Low Density Lipoprotein (VLDL) Transport Vesicle

Tiwari, S., Siddiqi, S., & Siddiqi, S. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.434258 · Cited by 57 · see citing works

CRL3s: The BTB-CUL3-RING E3 Ubiquitin Ligases

Wang, P., Song, J., & Ye, D. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-981-15-1025-0_13 · Cited by 53 · see citing works

Compound heterozygous variants in NBAS as a cause of atypical osteogenesis imperfecta

Balasubramanian, M., Hurst, J. A., Brown, S., Bishop, N. J., Arundel, P., DeVile, C. J., Pollitt, R. C., Crooks, L., Longman, D., Cáceres, J. F., et al. (2016) · Bone · doi:10.1016/j.bone.2016.10.023 · Cited by 56 · see citing works

Advances in characterizing ubiquitylation sites by mass spectrometry

Sylvestersen, K. B., Young, C., & Nielsen, M. L. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.12.009 · Cited by 55 · 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

Regulation of stem cell function by protein ubiquitylation

Strikoudis, A., Guillamot, M., & Aifantis, I. (2014) · EMBO Reports · doi:10.1002/embr.201338373 · Cited by 53 · 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

Trafficking mechanisms of extracellular matrix macromolecules: Insights from vertebrate development and human diseases

Ünlü, G., Levic, D. S., Melville, D. B., & Knapik, E. W. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.11.005 · Cited by 51 · 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

Biological Scaling Problems and Solutions in AmphibiansPreprint

Levy, D. L., & Heald, R. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a019166 · Cited by 52 · see citing works

Ubiquitin-dependent regulation of COPII coat size and function. Nature 482

Jin, L., Pahuja, K. B., Wickliffe, K. E., Gorur, A., Schekman, Y., & Rapé, M. (2012)

Collagen secretion explained

Stephens, D. J. (2012) · Nature · doi:10.1038/482474a · Cited by 30 · see citing works

The role of COPII coated vesicles in procollagen-1 trafficking

Gorur, A. (2016) · eScholarship (California Digital Library)

Mechanisms of Large COPII-coated Procollagen I Carrier Formation

Yuan, L. (2017) · eScholarship (California Digital Library)

COPII Vesicles Get Supersized by Ubiquitin

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