The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Open accessAbstract
Making Connections: Endoplasmic reticulum (ER)–mitochondria connections have been implicated in many physiological processes, including calcium homeostasis, signaling, membrane biogenesis, and apoptosis. Kornmann et al. (p. 477 , published online 25 June; see the Perspective by Wiedemann et al. ) looked for a proteinaceous link between the ER and mitochondria and, using combinations of synthetic biology and classical yeast genetics, found a protein complex that tethers the two organelles. A large-scale genetic interaction map suggests that these ER-mitochondria connections are important for interorganellar phospholipid exchange.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The ERMES complex is composed of four core subunits: an ER-resident protein Mmm1, a cytosolic protein Mdm12, and mitochondrial outer membrane proteins Mdm10 and Mdm34 [21] (Figure 1A).”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [21]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“MDM34 encodes a protein of the mitochondrial outer membrane that is a part of the ERMES complex that tethers mitochondria to the ER and is also involved in their contact with peroxisomes (Kornmann et al. 2009; Cohen et al. 2014).”
From Mitochondrial retrograde control of transcription evolves with respiratory stress, metabolic adaptation, and virulence in budding yeasts (2026) · cites this paper as Kornmann et al. 2009
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Deletion of any four proteins of the ERMES core complex results in the impaired formation of the ERMES complex and instability of ER-mitochondrial contact [21].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [21]
The cited source says what the claim attributes to it.
In the citing paper
“In Saccharomyces cerevisiae, the outer mitochondrial membrane is connected to the endoplasmic reticulum (ER) through the contact site formed by the ER-mitochondria encounter structure (ERMES) complex [21].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [21]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
Self-citationMitofusin 2 tethers endoplasmic reticulum to mitochondria
de Brito, O. M., & Scorrano, L. (2008) · Nature · doi:10.1038/nature07534 · Cited by 2,442
Close Contacts with the Endoplasmic Reticulum as Determinants of Mitochondrial Ca 2+ Responses
Rizzuto, R., Pinton, P., Carrington, W., Fay, F. S., Fogarty, K. E., Lifshitz, L. M., Tuft, R. A., & Pozzan, T. (1998) · Science · doi:10.1126/science.280.5370.1763 · Cited by 2,257
Hayashi, T., & Su, T.-P. (2007) · Cell · doi:10.1016/j.cell.2007.08.036 · Cited by 1,826
Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels
Szabadkai, G., Bianchi, K., Várnai, P., De Stefani, D., Wieckowski, M. R., Cavagna, D., Nagy, A. I., Balla, T., & Rizzuto, R. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200608073 · Cited by 1,413
Csordás, G., Renken, C. W., Várnai, P., Walter, L., Weaver, D., BUTTLE, K. F., Balla, T., Mannella, C. A., & Hajnóczky, G. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200604016 · Cited by 1,377
Rizzuto, R., Brini, M., Murgia, M., & Pozzan, T. (1993) · Science · doi:10.1126/science.8235595 · Cited by 1,207
Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis
Pinton, P., Giorgi, C., Siviero, R., Zecchini, E., & Rizzuto, R. (2008) · Oncogene · doi:10.1038/onc.2008.308 · Cited by 1,178
Rapid changes of mitochondrial Ca2+ revealed by specifically targeted recombinant aequorin
Rizzuto, R., Simpson, A. W. M., Brini, M., & Pozzan, T. (1992) · Nature · doi:10.1038/358325a0 · Cited by 931
The Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871
Flagged first, then by citations
Cited by
Sorted by citations
Items 301–400 of 1,001
Malleable Mitochondrion of Trypanosoma brucei
Verner, Z., Basu, S., Benz, C., Dixit, S., Dobáková, E., Faktorová, D., Hashimi, H., Horáková, E., Huang, Z., Paris, Z., et al. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2014.11.001 · Cited by 91
Wei, D., Jacobs, S., Modla, S., Zhang, S., Young, C. L., Cirino, R., Caplan, J. L., & Czymmek, K. J. (2012) · BioTechniques · doi:10.2144/000113850 · Cited by 104
Wollweber, F., von der Malsburg, K., & van der Laan, M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.004 · Cited by 98
Veeresh, P., Kaur, H., Sarmah, D., Mounica, L., Verma, G., Kotian, V., Kesharwani, R., Kalia, K., Borah, A., Wang, X., et al. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14212 · Cited by 98
Adverse Bioenergetic Consequences of Na + -Ca 2+ Exchanger–Mediated Ca 2+ Influx in Cardiac Myocytes
Kohlhaas, M., & Maack, C. (2010) · Circulation · doi:10.1161/circulationaha.110.968057 · Cited by 102
Mdm10 as a dynamic constituent of the TOB/SAM complex directs coordinated assembly of Tom40
Yamano, K., Tanaka‐Yamano, S., & Endo, T. (2010) · EMBO Reports · doi:10.1038/embor.2009.283 · Cited by 98
Reign in the membrane: How common lipids govern mitochondrial function
Funai, K., Summers, S. A., & Rutter, J. P. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.01.006 · Cited by 100
Designing biological systems: Systems Engineering meets Synthetic Biology
Rollié, S., Mangold, M., & Sundmacher, K. (2011) · Chemical Engineering Science · doi:10.1016/j.ces.2011.10.068 · Cited by 100
Thornton, N., Stroud, D. A., Milenkovic, D., Guiard, B., Pfanner, N., & Becker, T. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.12.026 · Cited by 98
Chan, E. Y. L., & McQuibban, G. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.399428 · Cited by 97
Topological Regulation of Lipid Balance in Cells
Drin, G. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035307 · Cited by 101
Friedman, J. R., Kannan, M., Toulmay, A., Jan, C. H., Weissman, J. S., Prinz, W. A., & Nunnari, J. M. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.11.023 · Cited by 94
Self-citationMitophagy: A Mechanism for Plant Growth and Survival
Broda, M., Millar, A. H., & Aken, O. V. (2018) · Trends in Plant Science · doi:10.1016/j.tplants.2018.02.010 · Cited by 95
Jadiya, P., Garbincius, J. F., & Elrod, J. W. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01224-4 · Cited by 94
Miceli, M. V., Jiang, J. C., Tiwari, A., Rodríguez-Quiñones, J. F., & Jazwinski, S. M. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2011.00102 · Cited by 96
Mitochondrial metabolic regulation by GRP78
Prasad, M., Pawlak, K. J., Burak, W. E., Perry, E. E., Marshall, B., Whittal, R. M., & Bose, H. S. (2017) · Science Advances · doi:10.1126/sciadv.1602038 · Cited by 99
Highlighting the endoplasmic reticulum-mitochondria connection: Focus on Mitofusin 2
Filadi, R., Greotti, E., & Pizzo, P. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.01.003 · Cited by 104
Mechanistic perspective of mitochondrial fusion: Tubulation vs. fragmentation
Escobar‐Henriques, M., & den Brave, F. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.07.016 · Cited by 100
SMP-domain proteins at membrane contact sites: Structure and function
Reinisch, K. M., & Camilli, P. V. D. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2015.12.003 · Cited by 94
Zhao, C., Liu, H., Xiao, T., Wang, Z., Nie, X., Li, X., Qian, P., Qin, L., Han, X., Zhang, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18936-1 · Cited by 98
Intertwined and Finely Balanced: Endoplasmic Reticulum Morphology, Dynamics, Function, and Diseases
Perkins, H. T., & Allan, V. (2021) · Cells · doi:10.3390/cells10092341 · Cited by 93
Intracellular trafficking of ceramide by ceramide transfer protein
Hanada, K. (2010) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.86.426 · Cited by 94
Protein import into plant mitochondria: signals, machinery, processing, and regulation
Murcha, M. W., Kmiec, B., Kubiszewski-Jakubiak, S., Teixeira, P. F., Glaser, E. G., & Whelan, J. (2014) · Journal of Experimental Botany · doi:10.1093/jxb/eru399 · Cited by 93
Structure and function of the N‐terminal domain of the human mitochondrial calcium uniporter
Lee, Y., Min, C. K., Kim, T., Song, H. K., Lim, Y., Kim, D., Shin, K., Kang, M., Kang, J. Y., Youn, H., et al. (2015) · EMBO Reports · doi:10.15252/embr.201540436 · Cited by 94
Tom7 Regulates Mdm10-mediated Assembly of the Mitochondrial Import Channel Protein Tom40
Yamano, K., Tanaka‐Yamano, S., & Endo, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163238 · Cited by 92
Ugo1 and Mdm30 act sequentially during Fzo1-mediated mitochondrial outer membrane fusion
den Brave, F., Fres, J. M., Schauss, A. C., Pinson, B., Praefcke, G. J. K., Langer, T., & Escobar‐Henriques, M. (2011) · Journal of Cell Science · doi:10.1242/jcs.073080 · Cited by 98
Saheki, Y., & Camilli, P. V. D. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.03.013 · Cited by 95
Membrane dynamics and organelle biogenesis—lipid pipelines and vesicular carriers
Stefan, C. J., Trimble, W. S., Grinstein, S., Drin, G., Reinisch, K. M., Camilli, P. V. D., Cohen, S., Valm, A. M., Lippincott‐Schwartz, J., Levine, T. P., et al. (2017) · BMC Biology · doi:10.1186/s12915-017-0432-0 · Cited by 95
A Phospholipid Transfer Function of ER-Mitochondria Encounter Structure Revealed in Vitro
Kojima, R., Endo, T., & Tamura, Y. (2016) · Scientific Reports · doi:10.1038/srep30777 · Cited by 91
Simmen, T., & Herrera-Cruz, M. S. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.04.014 · Cited by 90
Mitochondrial behaviour throughout the lytic cycle of Toxoplasma gondii
Ovciarikova, J., Lemgruber, L., Stilger, K. L., Sullivan, W. J., & Sheiner, L. (2017) · Scientific Reports · doi:10.1038/srep42746 · Cited by 85
Schlattner, U., Tokarska-Schlattner, M., Rousseau, D. L., Boissan, M., Mannella, C. A., Epand, R. M., & Lacombe, M. (2014) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2013.12.008 · Cited by 93
Martinvalet, D. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0237-7 · Cited by 94
Crosstalk between mitochondria–ER contact sites and the apoptotic machinery as a novel health meter
Larrañaga-SanMiguel, A., Bengoa‐Vergniory, N., & Flores‐Romero, H. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.08.007 · Cited by 94
Becker, T., Wenz, L.-S., Thornton, N., Stroud, D., Meisinger, C., Wiedemann, N., & Pfanner, N. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.11.002 · Cited by 89
Mitochondrial inheritance in yeast
Westermann, B. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.005 · Cited by 87
Protein trafficking at the crossroads to mitochondria
Wasilewski, M., Chojnacka, K., & Chacińska, A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.10.019 · Cited by 95
Cho, I., Adelmant, G., Lim, Y., Marto, J. A., Cho, G., & Golden, J. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.795286 · Cited by 90
Endoplasmic Reticulum–Mitochondria Contact Sites and Neurodegeneration
Xu, L., Wang, X., & Tong, C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00428 · Cited by 87
Doa1 targets ubiquitinated substrates for mitochondria-associated degradation
Wu, X., Li, L., & Jiang, H. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201510098 · Cited by 99
McNew, J. A., Sondermann, H., Tina Munn Yi, L. E. E., Stern, M., & Brandizzí, F. (2013) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101512-122328 · Cited by 85
Alva, V., & Lupas, A. N. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.01.016 · Cited by 90
Baker, C. D., Ball, W. B., Pryce, E. N., & Gohil, V. M. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-12-0865 · Cited by 86
Petrungaro, C., & Kornmann, B. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.11.005 · Cited by 90
Self-citationRegulation of autophagy by mitochondrial phospholipids in health and diseases
Hsu, P., & Shi, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.003 · Cited by 86
Molecular mechanisms of organelle inheritance: lessons from peroxisomes in yeast
Fagarasanu, A. D., Mast, F. D., Knoblach, B., & Rachubinski, R. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2960 · Cited by 85
Ellenrieder, L., Opaliński, Ł., Becker, L., Krüger, V., Mirus, O., Straub, S. P., Ebell, K., Flinner, N., Stiller, S. B., Guiard, B., et al. (2016) · Nature Communications · doi:10.1038/ncomms13021 · Cited by 84
Subramanian, K., Jochem, A., Vasseur, M. L., Lewis, S. C., Paulson, B. R., Reddy, T. R., Russell, J. D., Coon, J. J., Pagliarini, D. J., & Nunnari, J. M. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201808044 · Cited by 82
Self-citationLipid homeostasis in mitochondria
Tamura, Y., Kawano, S., & Endo, T. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0121 · Cited by 81
Mitochondrial lipids in neurodegeneration
Aufschnaiter, A., Kohler, V., Diessl, J., Peselj, C., Carmona‐Gutiérrez, D., Keller, W., & Büttner, S. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2463-1 · Cited by 91
Overlap of cargo binding sites on myosin V coordinates the inheritance of diverse cargoes
Eves, P. T., Jin, Y., Brunner, M., & Weisman, L. S. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201201024 · Cited by 84
Shirane, M., Wada, M., Morita, K., Hayashi, N., Kunimatsu, R., Matsumoto, Y., Matsuzaki, F., Nakatsumi, H., Ohta, K., Tamura, Y., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18413-9 · Cited by 84
Quantitative Genetic Interaction Mapping Using the E-MAP Approach
Collins, S. R., Roguev, A., & Krogan, N. J. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)70009-4 · Cited by 88
Self-citationThe ERMES complex and ER–mitochondria connections
Michel, A. H., & Kornmann, B. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110758 · Cited by 86
Self-citationPhosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria
Miyata, N., Watanabe, Y., Tamura, Y., Endo, T., & Kuge, O. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201601082 · Cited by 83
Pascual‐Ahuir, A., Manzanares‐Estreder, S., & Proft, M. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/9860841 · Cited by 87
Mitochondrial Quality Control Mechanisms and the PHB (Prohibitin) Complex
Hernando‐Rodríguez, B., & Artal‐Sanz, M. (2018) · Cells · doi:10.3390/cells7120238 · Cited by 90
Mitofusins: Disease Gatekeepers and Hubs in Mitochondrial Quality Control by E3 Ligases
Escobar‐Henriques, M., & Joaquim, M. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00517 · Cited by 85
PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes
Guillén-Samander, A., Bian, X., & Camilli, P. V. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913509116 · Cited by 82
Mitochondria-Associated Membranes (MAMs): Overview and Its Role in Parkinson’s Disease
Rodríguez‐Arribas, M., Yakhine-Diop, S. M. S., Pedro, J. M. B., Gómez‐Suaga, P., Gómez‐Sánchez, R., Martínez-Chacón, G., Fuentes, J. M., González‐Polo, R. A., & Niso‐Santano, M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0140-8 · Cited by 82
Ping, H. A., Kraft, L. M., Chen, W., Nilles, A. E., & Lackner, L. L. (2016) · Journal of Cell Biology · doi:10.1083/jcb.201511021 · Cited by 82
Renault, T. T., & Chipuk, J. E. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.10.009 · Cited by 86
Peroxisome Formation and Maintenance Are Dependent on the Endoplasmic Reticulum
Tabak, H. F., Braakman, I., & van der Zand, A. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-081111-125123 · Cited by 82
Phosphatidylserine synthesis at membrane contact sites promotes its transport out of the ER
Kannan, M., Lahiri, S., Liu, L., Choudhary, V., & Prinz, W. A. (2017) · Journal of Lipid Research · doi:10.1194/jlr.m072959 · Cited by 81
MIRO GTPases in Mitochondrial Transport, Homeostasis and Pathology
Tang, B. L. (2015) · Cells · doi:10.3390/cells5010001 · Cited by 81
Ligand-dependent localization and function of ORP–VAP complexes at membrane contact sites
Weber‐Boyvat, M., Kentala, H., Peränen, J., & Olkkonen, V. M. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1786-x · Cited by 81
Maintaining social contacts: The physiological relevance of organelle interactions
Silva, B. S. C., DiGiovanni, L. F., Kumar, R., Carmichael, R. E., Kim, P. K., & Schrader, M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118800 · Cited by 84
Neurodegenerative diseases: Lessons from genome‐wide screens in small model organisms
van Ham, T. J., Breitling, R., Swertz, M. A., & Nollen, E. A. A. (2009) · EMBO Molecular Medicine · doi:10.1002/emmm.200900051 · Cited by 82
Tying trafficking to fusion and fission at the mighty mitochondria
Farmer, T., Naslavsky, N., & Caplan, S. (2018) · Traffic · doi:10.1111/tra.12573 · Cited by 87
Dorn, G. W., & Scorrano, L. (2010) · Circulation Research · doi:10.1161/circresaha.110.225714 · Cited by 82
Podocyte Injury in Diabetic Kidney Disease: A Focus on Mitochondrial Dysfunction
Liu, S., Yuan, Y., Yi, X., Xing, C., & Zhang, B. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.832887 · Cited by 82
Mitochondrial ryanodine receptors and other mitochondrial Ca2+ permeable channels
Ryu, S.-Y., Beutner, G., Dirksen, R. T., Kinnally, K. W., & Sheu, S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.032 · Cited by 80
The role of Sec3p in secretory vesicle targeting and exocyst complex assembly
Luo, G., Zhang, J., & Guo, W. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-04-0907 · Cited by 75
Cholesterol ester droplets and steroidogenesis
Kraemer, F. B., Khor, V. K., Shen, W., & Azhar, S. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.10.012 · Cited by 82
Role of Phosphatidylethanolamine in the Biogenesis of Mitochondrial Outer Membrane Proteins
Becker, T., Horvath, S. E., Böttinger, L., Gebert, N., Daum, G., & Pfanner, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442392 · Cited by 85
The ubiquitous and ancient ER membrane protein complex (EMC): tether or not?
Wideman, J. G. (2015) · F1000Research · doi:10.12688/f1000research.6944.1 · Cited by 78
Assembly of β-barrel proteins in the mitochondrial outer membrane
Höhr, A. I. C., Straub, S. P., Warscheid, B., Becker, T., & Wiedemann, N. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.10.006 · Cited by 78
Miro: A molecular switch at the center of mitochondrial regulation
Eberhardt, E. L., Ludlam, A. V., Tan, Z., & Cianfrocco, M. A. (2020) · Protein Science · doi:10.1002/pro.3839 · Cited by 82
Oxysterol-binding proteins: Functions in cell regulation beyond lipid metabolism
Weber‐Boyvat, M., Zhong, W., Yan, D., & Olkkonen, V. M. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.02.016 · Cited by 81
The ubiquitous and ancient ER membrane protein complex (EMC): tether or not?
Wideman, J. G. (2015) · F1000Research · doi:10.12688/f1000research.6944.2 · Cited by 74
The mitochondrial protein import machinery has multiple connections to the respiratory chain
Kulawiak, B., Höpker, J., Gebert, M., Guiard, B., Wiedemann, N., & Gebert, N. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.12.004 · Cited by 82
Tether Me, Tether Me Not—Dynamic Organelle Contact Sites in Metabolic Rewiring
Bohnert, M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.06.026 · Cited by 77
Mitochondrial compartmentalization: emerging themes in structure and function
Iovine, J. C., Claypool, S. M., & Alder, N. N. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.06.003 · Cited by 82
A microRNA’s journey to the center of the mitochondria
Macgregor-Das, A. M., & Das, S. (2018) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00714.2017 · Cited by 76
Phosphatidate-mediated regulation of lipid synthesis at the nuclear/endoplasmic reticulum membrane
Kwiatek, J. M., Han, G., & Carman, G. M. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.03.006 · Cited by 76
Marriott, K.-S. C., Prasad, M., Thapliyal, V., & Bose, H. S. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.198168 · Cited by 75
Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex
Jeong, H., Park, J., & Lee, C. (2016) · EMBO Reports · doi:10.15252/embr.201642706 · Cited by 71
Lipid Dynamics at Contact Sites Between the Endoplasmic Reticulum and Other Organelles
Balla, T., Kim, Y. J., Álvarez-Prats, A., & Pemberton, J. G. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100818-125251 · Cited by 79
One ring to bring them all and in the darkness bind them: The trafficking of heme without deliverers
Chambers, I. G., Willoughby, M. M., Hamza, I., & Reddi, A. R. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118881 · Cited by 77
Vps13-like proteins provide phosphatidylethanolamine for GPI anchor synthesis in the ER
Toulmay, A., Whittle, F. B., Yang, J. M., Bai, X., Diarra, J., Banerjee, S., Levine, T. P., Golden, A., & Prinz, W. A. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202111095 · Cited by 75
Jin, C., Liu, J., Chen, Y., Zeng, L., Guan, R., Ouyang, C., Ji, L., & Chao, H. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201501882 · Cited by 76
Mechanisms of Autophagy in Metabolic Stress Response
Gross, A. S., & Graef, M. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.09.005 · Cited by 77
Phospholipid Transport via Mitochondria
Tamura, Y., Sesaki, H., & Endo, T. (2014) · Traffic · doi:10.1111/tra.12188 · Cited by 75
Lau, D. H. W., Hartopp, N., Welsh, N. J., Mueller, S., Glennon, E. B. C., Mórotz, G. M., Annibali, A., Gómez‐Suaga, P., Stoica, R., Paillusson, S., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0022-7 · Cited by 77
Li, C., Duckney, P. J., Zhang, T., Fu, Y., Li, X., Kroon, J., Jaeger, G. D., Cheng, Y., Hussey, P. J., & Wang, P. (2022) · Nature Communications · doi:10.1038/s41467-022-33402-w · Cited by 78
Förtsch, J., Hummel, E., Krist, M., & Westermann, B. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201012088 · Cited by 73
Degradation of Host Sphingomyelin Is Essential for Leishmania Virulence
Zhang, O., Wilson, M. C., Xu, W., Hsu, F., TURK, J. W., Kuhlmann, F., Wang, Y., Soong, L., Key, P. N., Beverley, S. M., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000692 · Cited by 74
Like iron in the blood of the people: the requirement for heme trafficking in iron metabolism
Korolnek, T., & Hamza, I. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00126 · Cited by 73
Membrane contact sites, ancient and central hubs of cellular lipid logistics
Jain, A., & Holthuis, J. C. M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.017 · Cited by 77
Lim, D., Tapella, L., Dematteis, G., Genazzani, A. A., Corazzari, M., & Verkhratsky, A. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101914 · Cited by 75
Metadata
- Authors
- Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P.
- Affiliations
- Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94158, USA.
- University of California, San Francisco (US)
- Howard Hughes Medical Institute (US)
- Weizmann Institute of Science (IL)
- University of California, Davis (US)
- Corresponding author
- Currie, Erin
- Collins, Sean R.
- Venue
- Science
- Published
- 2009-07-24
- Volume
- 325
- Issue
- 5939
- Pages
- 477-481
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2933203
- OpenAlex
- W1997527771
- Cited by
- 1,275
- References
- 32
- Citations by year
- 2026: 29 · 2025: 49 · 2024: 79 · 2023: 54 · 2022: 63 · 2021: 91 · 2020: 86 · 2019: 89 · 2018: 80 · 2017: 85 · 2016: 90 · 2015: 74 · 2014: 91 · 2013: 88 · 2012: 73
- FWCI
- 30.30
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation
- Howard Hughes Medical Institute
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM062942, R01GM032384)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- ER-mitochondria tethering, inter-organelle communication, phospholipid synthesis, calcium signaling, genetic interaction mapping
- MeSH terms
- Animals, Endoplasmic Reticulum, Membrane Proteins, Mitochondria, Phospholipids, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Calcium Signaling, Mitochondrial Proteins, Saccharomyces cerevisiae Proteins, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
