Structure–Function Insights into Direct Lipid Transfer between Membranes by Mmm1–Mdm12 of ERMES

A SIMPLE METHOD FOR THE ISOLATION AND PURIFICATION OF TOTAL LIPIDES FROM ANIMAL TISSUES

Folch, J., Lees, M., & Stanley, G. H. S. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64849-5 · Cited by 65,189 · see citing works

Comparison of simple potential functions for simulating liquid water

Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,335 · see citing works

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works

Molecular dynamics with coupling to an external bath

Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984) · The Journal of Chemical Physics · doi:10.1063/1.448118 · Cited by 30,626 · see citing works

Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems

Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,588 · see citing works

Features and development of Coot

Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works

<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works

<i>Phaser</i> crystallographic software

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works

Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n-Alkanes

Ryckaert, J., Ciccotti, G., & Berendsen, H. (1977) · Journal of Computational Physics · doi:10.1016/0021-9991(77)90098-5 · Cited by 19,525 · see citing works

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works

Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features

Kabsch, W., & Sander, C. (1983) · Biopolymers · doi:10.1002/bip.360221211 · Cited by 15,320 · see citing works

Comparative Protein Modelling by Satisfaction of Spatial Restraints

Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977 · see citing works

The Amber biomolecular simulation programs

Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535 · see citing works

REFMAC 5 for the refinement of macromolecular crystal structures

Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M., Long, F., & Vagin, A. A. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911001314 · Cited by 8,385 · see citing works

Comparison of multiple Amber force fields and development of improved protein backbone parameters

Horn̆ák, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A. E., & Simmerling, C. L. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21123 · Cited by 6,903 · see citing works

Structure validation by Cα geometry: ϕ,ψ and Cβ deviation

Lovell, S. C., Davis, I. W., Arendall, W. B., de Bakker, P. I. W., Word, J. M., Prisant, M. G., Richardson, J. S., & Richardson, D. C. (2003) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10286 · Cited by 4,595 · see citing works

An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen

Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275 · see citing works

A series of PDB related databases for everyday needs

Joosten, R., Beek, T. T. T., Krieger, E., Hekkelman, M., Hooft, R., Schneider, R., Sander, C., & Vriend, G. (2010) · Nucleic Acids Res. · doi:10.1093/nar/gkq1105 · Cited by 1,050 · see citing works

Ligand-specific regulation of the extracellular surface of a G-protein-coupled receptor

Bokoch, M. P., Zou, Y., Rasmussen, S. G. F., Liu, C. W., Nygaard, R., Rosenbaum, D. M., Fung, J. J., Choi, H., Thian, F. S., Kobilka, T. S., et al. (2010) · Nature · doi:10.1038/nature08650 · Cited by 471 · see citing works

Genetic Basis of Mitochondrial Function and Morphology in Saccharomyces cerevisiae

Dimmer, K. S., Fritz, S., Fuchs, F., Messerschmitt, M., Weinbach, N., Neupert, W., & Westermann, B. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-12-0588 · Cited by 443 · see citing works

Roll: a new algorithm for the detection of protein pockets and cavities with a rolling probe sphere

Yu, J., Zhou, Y. G., Tanaka, I., & Yao, M. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp599 · Cited by 398 · see citing works

A Dynamic Interface between Vacuoles and Mitochondria in Yeast

Elbaz‐Alon, Y., Rosenfeld-Gur, E., Shinder, V., Futerman, A. H., Geiger, T., & Schuldiner, M. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.007 · Cited by 377 · see citing works

The Conserved GTPase Gem1 Regulates Endoplasmic Reticulum–Mitochondria Connections

Kornmann, B., Osman, C., & Walter, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111314108 · Cited by 335 · see citing works

Cellular Metabolism Regulates Contact Sites between Vacuoles and Mitochondria

Hönscher, C., Mari, M. C., Auffarth, K., Bohnert, M., Griffith, J. M., Geerts, W. J. C., van der Laan, M., Cabrera, M., Reggiori, F., & Ungermann, C. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.06.006 · Cited by 333 · see citing works

Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

Schauder, C. M., Wu, X., Saheki, Y., Narayanaswamy, P., Torta, F. T., Wenk, M. R., Camilli, P. V. D., & Reinisch, K. M. (2014) · Nature · doi:10.1038/nature13269 · Cited by 321 · see citing works

Prohibitins and the functional compartmentalization of mitochondrial membranes

Osman, C., Merkwirth, C., & Langer, T. (2009) · Journal of Cell Science · doi:10.1242/jcs.037655 · Cited by 309 · see citing works

A Conserved Endoplasmic Reticulum Membrane Protein Complex (EMC) Facilitates Phospholipid Transfer from the ER to Mitochondria

Lahiri, S., Chao, J. T., Tavassoli, S., Wong, A. K. O., Choudhary, V., Young, B. P., Loewen, C. J. R., & Prinz, W. A. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001969 · Cited by 306 · see citing works

Ltc1 is an ER-localized sterol transporter and a component of ER–mitochondria and ER–vacuole contacts

Murley, A., Sarsam, R. D., Toulmay, A., Yamada, J., Prinz, W. A., & Nunnari, J. M. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201502033 · Cited by 287 · see citing works

Regulation of Mitochondrial Morphology and Inheritance by Mdm10p, a Protein of the Mitochondrial Outer Membrane

Sogo, L. F., & Yaffe, M. P. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.6.1361 · Cited by 284 · see citing works

MMM1 Encodes a Mitochondrial Outer Membrane Protein Essential for Establishing and Maintaining the Structure of Yeast Mitochondria

Burgess, S. M., Delannoy, M., & Jensen, R. E. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.6.1375 · Cited by 249 · see citing works

Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway

Frederick, R. L., McCaffery, J. M., Cunningham, K. W., Okamoto, K., & Shaw, J. M. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200405100 · Cited by 247 · see citing works

Intramitochondrial Transport of Phosphatidic Acid in Yeast by a Lipid Transfer Protein

Connerth, M., Tatsuta, T., Haag, M., Klecker, T., Westermann, B., & Langer, T. (2012) · Science · doi:10.1126/science.1225625 · Cited by 232 · see citing works

ER–mitochondrial junctions can be bypassed by dominant mutations in the endosomal protein Vps13

Lang, A. B., Peter, A. T. J., Walter, P., & Kornmann, B. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201502105 · Cited by 223 · see citing works

Homology of SMP Domains to the TULIP Superfamily of Lipid-Binding Proteins Provides a Structural Basis for Lipid Exchange between ER and Mitochondria

Kopec, K. O., Alva, V., & Lupas, A. N. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq326 · Cited by 212 · see citing works

Lam6 Regulates the Extent of Contacts between Organelles

Elbaz‐Alon, Y., Eisenberg‐Bord, M., Shinder, V., Stiller, S. B., Shimoni, E., Wiedemann, N., Geiger, T., & Schuldiner, M. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.022 · Cited by 209 · see citing works

LIPID11: A Modular Framework for Lipid Simulations Using Amber

Skjevik, Å. A., Madej, B. D., Walker, R. C., & Teigen, K. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp3059992 · Cited by 202 · see citing works

3Drefine: Consistent protein structure refinement by optimizing hydrogen bonding network and atomic‐level energy minimization

Bhattacharya, D., & Cheng, J. J. (2012) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24167 · Cited by 198 · see citing works

Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly

AhYoung, A. P., Jiang, J., Zhang, J., Dang, X. K., Loo, J. A., Zhou, Z. H., & Egea, P. F. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422363112 · Cited by 197 · see citing works

Mdm12p, a Component Required for Mitochondrial Inheritance That Is Conserved between Budding and Fission Yeast

Berger, K. H., Sogo, L. F., & Yaffe, M. P. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.3.545 · Cited by 197 · see citing works

Gem1 and ERMES Do Not Directly Affect Phosphatidylserine Transport from ER to Mitochondria or Mitochondrial Inheritance

Nguyen, T., Lewandowska, A., Choi, J., Markgraf, D. F., Junker, M., Bilgin, M., Ejsing, C. S., Voelker, D. R., Rapoport, T. A., & Shaw, J. M. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01352.x · Cited by 166 · see citing works

Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a β-propeller protein family

Krick, R., Busse, R. A., Scacioc, A., Stephan, M., Janshoff, A., Thumm, M., & Kühnel, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205128109 · Cited by 166 · see citing works

Mmm2p, a Mitochondrial Outer Membrane Protein Required for Yeast Mitochondrial Shape and Maintenance of mtDNA Nucleoids

Youngman, M. J., Hobbs, A. E. A., Burgess, S. M., Srinivasan, M., & Jensen, R. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200308012 · Cited by 148 · see citing works

Composition and Topology of the Endoplasmic Reticulum–Mitochondria Encounter Structure

Stroud, D. A., Oeljeklaus, S., Wiese, S., Bohnert, M., Lewandrowski, U., Sickmann, A., Guiard, B., van der Laan, M., Warscheid, B., & Wiedemann, N. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.09.012 · Cited by 144 · see citing works

Intramitochondrial phospholipid trafficking

Tatsuta, T., & Langer, T. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.08.006 · Cited by 129 · see citing works

Mcp1 and Mcp2, two novel proteins involved in mitochondrial lipid homeostasis

Tan, T., Özbalci, C., Brügger, B., Rapaport, D., & Dimmer, K. (2013) · Journal of Cell Science · doi:10.1242/jcs.121244 · Cited by 116 · see citing works

ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae

Voss, C., Lahiri, S., Young, B. P., Loewen, C. J. R., & Prinz, W. A. (2012) · Journal of Cell Science · doi:10.1242/jcs.105635 · Cited by 108 · see citing works

Role for Two Conserved Intermembrane Space Proteins, Ups1p and Up2p, in Intra-mitochondrial Phospholipid Trafficking

Tamura, Y., Onguka, O., Hobbs, A. E. A., Jensen, R. E., Iijima, M., Claypool, S. M., & Sesaki, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.338665 · Cited by 105 · see citing works

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 · see citing works

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 · see citing works

Structural and mechanistic insights into phospholipid transfer by Ups1–Mdm35 in mitochondria

Watanabe, Y., Tamura, Y., Kawano, S., & Endo, T. (2015) · Nature Communications · doi:10.1038/ncomms8922 · Cited by 90 · see citing works

Phosphatidylserine 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 · see citing works

Phospholipid Transport via Mitochondria

Tamura, Y., Sesaki, H., & Endo, T. (2014) · Traffic · doi:10.1111/tra.12188 · Cited by 74 · see citing works

Yeast Lipid Analysis and Quantification by Mass Spectrometry

Guan, X. L., Riezman, I., Wenk, M. R., & Riezman, H. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)70015-x · Cited by 72 · see citing works

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 · see citing works

Mitochondrial lipid transport at a glance

Scharwey, M., Tatsuta, T., & Langer, T. (2013) · Journal of Cell Science · doi:10.1242/jcs.134130 · Cited by 68 · see citing works

Bioinformatics of the TULIP domain superfamily

Kopec, K. O., Alva, V., & Lupas, A. N. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391033 · Cited by 54 · see citing works

Improved Methods for the Fatty Acid Analysis of Blood Lipid Classes

ICHIHARA, K.-I., Yoneda, K., Takahashi, A., Hoshino, N., & Matsuda, M. (2011) · Lipids · doi:10.1007/s11745-011-3531-7 · Cited by 23 · see citing works

The functional universe of membrane contact sites

Prinz, W. A., Toulmay, A., & Balla, T. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0180-9 · Cited by 736 · see citing works

Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes

Wong, L. H., Gatta, A. T., & Levine, T. P. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0071-5 · Cited by 470 · see citing works

Atg2 mediates direct lipid transfer between membranes for autophagosome formation

Osawa, T., Kotani, T., Kawaoka, T., Hirata, E., Suzuki, K., Nakatogawa, H., Ohsumi, Y., & Noda, N. N. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0203-4 · Cited by 454 · see citing works

Deficient Endoplasmic Reticulum-Mitochondrial Phosphatidylserine Transfer Causes Liver Disease

Hernández‐Álvarez, M. I., Sebastián, D., Vives, S., Ivanova, S., Bartoccioni, P., Kakimoto, P. A., Plana, N., Veiga, S. R., Hernandez, V. A., Vasconcelos, N., et al. (2019) · Cell · doi:10.1016/j.cell.2019.04.010 · Cited by 400 · see citing works

The autophagic membrane tether ATG2A transfers lipids between membranes

Maeda, S., Otomo, C., & Otomo, T. (2019) · eLife · doi:10.7554/elife.45777 · Cited by 336 · see citing works

Mechanisms of mitochondrial respiratory adaptation

Bennett, C. F., Latorre‐Muro, P., & Puigserver, P. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00506-6 · Cited by 313 · see citing works

Making the connection: How membrane contact sites have changed our view of organelle biology

Voeltz, G. K., Sawyer, E. M., Hajnóczky, G., & Prinz, W. A. (2024) · Cell · doi:10.1016/j.cell.2023.11.040 · Cited by 230 · see citing works

Movement of accessible plasma membrane cholesterol by the GRAMD1 lipid transfer protein complex

Naito, T., Ercan, B., Krshnan, L., Triebl, A., Koh, D. H. Z., Wei, F.-Y., Tomizawa, K., Torta, F. T., Wenk, M. R., & Saheki, Y. (2019) · eLife · doi:10.7554/elife.51401 · Cited by 171 · see citing works

Mitochondrial outer membrane protein FUNDC2 promotes ferroptosis and contributes to doxorubicin-induced cardiomyopathy

Ta, N., Qu, C., Wu, H., Zhang, D., Sun, T., Li, Y., Wang, J., Wang, X., Tang, T.-S., Chen, Q., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2117396119 · Cited by 151 · see citing works

Transport of Proteins into Mitochondria

Hansen, K. G., & Herrmann, J. M. (2019) · The Protein Journal · doi:10.1007/s10930-019-09819-6 · Cited by 116 · see citing works

Vps39 Interacts with Tom40 to Establish One of Two Functionally Distinct Vacuole-Mitochondria Contact Sites

Montoro, A. G., Auffarth, K., Hönscher, C., Bohnert, M., Becker, T., Warscheid, B., Reggiori, F., van der Laan, M., Fröhlich, F., & Ungermann, C. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.05.011 · Cited by 143 · see citing works

Mitochondria-Associated ER Membranes – The Origin Site of Autophagy

Yang, M., Li, C., Yang, S., Xiao, Y., Xiong, X., Chen, W., Zhao, H., Zhang, Q., Han, Y., & Sun, L. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00595 · Cited by 137 · see citing works

In situ architecture of the ER–mitochondria encounter structure

Wozny, M. R., Di Luca, A., Morado, D. R., Picco, A., Khaddaj, R., Campomanes, P., Ivanović, L., Hoffmann, P. C., Miller, E. A., Vanni, S., et al. (2023) · Nature · doi:10.1038/s41586-023-06050-3 · Cited by 134 · see citing works

CDP-Diacylglycerol Synthases (CDS): Gateway to Phosphatidylinositol and Cardiolipin Synthesis

Blunsom, N. J., & Cockcroft, S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00063 · Cited by 123 · see citing works

Tricalbins Contribute to Cellular Lipid Flux and Form Curved ER-PM Contacts that Are Bridged by Rod-Shaped Structures

Hoffmann, P. C., Bharat, T. A. M., Wozny, M. R., Jérôme Boulanger, A., Miller, E. A., & Kukulski, W. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.09.019 · Cited by 116 · see citing works

The Vps13 Family of Lipid Transporters and Its Role at Membrane Contact Sites

Dziurdzik, S. K., & Conibear, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22062905 · Cited by 121 · see citing works

Organelle membrane-specific chemical labeling and dynamic imaging in living cells

Tamura, T., Fujisawa, A., Tsuchiya, M., Shen, Y., Nagao, K., Kawano, S., Tamura, Y., Endo, T., Umeda, M., & Hamachi, I. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-00651-z · Cited by 106 · see citing works

ORP5/8 and MIB/MICOS link ER-mitochondria and intra-mitochondrial contacts for non-vesicular transport of phosphatidylserine

Monteiro-Cardoso, V. F., Rochin, L., Arora, A., Houcine, A., Jääskeläinen, E., Kivelä, A. M., Sauvanet, C., Bars, R. L., Marien, E., Dehairs, J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111364 · Cited by 107 · see citing works

The Expanding and Unexpected Functions of Mitochondria Contact Sites

Lackner, L. L. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.009 · Cited by 107 · see citing works

Phospholipid ebb and flow makes mitochondria go

Acoba, M. G., Senoo, N., & Claypool, S. M. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202003131 · Cited by 102 · see citing works

A programmable DNA-origami platform for studying lipid transfer between bilayers

Bian, X., Zhang, Z., Xiong, Q., Camilli, P. V. D., & Lin, C. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0325-3 · Cited by 102 · see citing works

Lipid exchange at ER-mitochondria contact sites: a puzzle falling into place with quite a few pieces missing

Petrungaro, C., & Kornmann, B. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.11.005 · Cited by 86 · see citing works

Lipid homeostasis in mitochondria

Tamura, Y., Kawano, S., & Endo, T. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0121 · Cited by 81 · see citing works

The endoplasmic reticulum: Homeostasis and crosstalk in retinal health and disease

Zhang, S. X., Wang, J. J., Starr, C. R., Lee, E.-J., Park, K. S., Zhylkibayev, A. A., Medina, A., Lin, J. H., & Gorbatyuk, M. S. (2023) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2023.101231 · Cited by 85 · see citing works

Lipid transfer proteins rectify inter-organelle flux and accurately deliver lipids at membrane contact sites

Hanada, K. (2018) · Journal of Lipid Research · doi:10.1194/jlr.r085324 · Cited by 81 · see citing works

Structural basis for mitoguardin-2 mediated lipid transport at ER-mitochondrial membrane contact sites

Kim, H., Lee, S., Jun, Y., & Lee, C. (2022) · Nature Communications · doi:10.1038/s41467-022-31462-6 · Cited by 80 · see citing works

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 74 · see citing works

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 · see citing works

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 · see citing works

Lipid transporter TMEM24/C2CD2L is a Ca 2+ -regulated component of ER–plasma membrane contacts in mammalian neurons

Sun, E. W., Guillén-Samander, A., Bian, X., Wu, Y., Cai, Y., Messa, M., & Camilli, P. V. D. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1820156116 · Cited by 69 · see citing works

Cnm1 mediates nucleus–mitochondria contact site formation in response to phospholipid levels

Eisenberg‐Bord, M., Zung, N., Collado, J., Drwesh, L., Fenech, E. J., Fadel, A., Dezorella, N., Bykov, Y. S., Rapaport, D., Fernández‐Busnadiego, R., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202104100 · Cited by 59 · see citing works

Organelle contact zones as sites for lipid transfer

Tamura, Y., Kawano, S., & Endo, T. (2018) · The Journal of Biochemistry · doi:10.1093/jb/mvy088 · Cited by 60 · see citing works

Relevance of the endoplasmic reticulum-mitochondria axis in cancer diagnosis and therapy

An, G., Park, J., Song, J., Hong, T., Song, G., & Lim, W. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01137-3 · Cited by 57 · see citing works

Current and Emerging Approaches for Studying Inter-Organelle Membrane Contact Sites

Huang, X. S., Jiang, C., Yu, L., & Yang, A. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00195 · Cited by 59 · see citing works

Mitochondrial Outer Membrane Channels: Emerging Diversity in Transport Processes

Becker, T., & Wagner, R. (2018) · BioEssays · doi:10.1002/bies.201800013 · Cited by 56 · see citing works

METALIC reveals interorganelle lipid flux in live cells by enzymatic mass tagging

Peter, A. T. J., Petrungaro, C., Peter, M., & Kornmann, B. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00917-9 · Cited by 56 · see citing works

Remote homology searches identify bacterial homologues of eukaryotic lipid transfer proteins, including Chorein-N domains in TamB and AsmA and Mdm31p

Levine, T. P. (2019) · BMC Molecular and Cell Biology · doi:10.1186/s12860-019-0226-z · Cited by 54 · see citing works

Lipid Metabolism at Membrane Contacts: Dynamics and Functions Beyond Lipid Homeostasis

Xu, J., & Huang, X. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.615856 · Cited by 54 · see citing works

ER–mitochondria contacts promote mitochondrial-derived compartment biogenesis

English, A. M., Schuler, M.-H., Xiao, T., Kornmann, B., Shaw, J. M., & Hughes, A. L. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202002144 · Cited by 48 · see citing works

ER-Mitochondria Calcium Transfer, Organelle Contacts and Neurodegenerative Diseases

Vallese, F., Barazzuol, L., Maso, L., Brini, M., & Calí, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-12457-1_29 · Cited by 48 · see citing works

Mitochondrial–nuclear heme trafficking in budding yeast is regulated by GTPases that control mitochondrial dynamics and ER contact sites

Martinez-Guzman, O., Willoughby, M. M., Saini, A. G., Dietz, J. V., Bohovych, I., Medlock, A. E., Khalimonchuk, O., & Reddi, A. R. (2020) · Journal of Cell Science · doi:10.1242/jcs.237917 · Cited by 47 · see citing works

The Endoplasmic Reticulum-Mitochondria Encounter Structure Complex Coordinates Coenzyme Q Biosynthesis

Eisenberg‐Bord, M., Tsui, H. S., Antunes, D., Fernández-del-Río, L., Bradley, M. C., Dunn, C. D., Nguyen, T. P. T., Rapaport, D., Clarke, C. F., & Schuldiner, M. (2019) · Contact · doi:10.1177/2515256418825409 · Cited by 45 · see citing works

Decreasing pdzd8-mediated mito–ER contacts improves organismal fitness and mitigates Aβ 42 toxicity

Hewitt, V. L., Miller‐Fleming, L., Twyning, M. J., Andreazza, S., Mattedi, F., Prudent, J., Polleux, F., Vagnoni, A., & Whitworth, A. J. (2022) · Life Science Alliance · doi:10.26508/lsa.202201531 · Cited by 44 · see citing works

MICOS subcomplexes assemble independently on the mitochondrial inner membrane in proximity to ER contact sites

Tirrell, P. S., Nguyen, K. N., Luby‐Phelps, K., & Friedman, J. R. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.202003024 · Cited by 42 · see citing works

Mitochondrial phospholipid metabolism in health and disease

Joshi, A., Richard, T. H., & Gohil, V. M. (2023) · Journal of Cell Science · doi:10.1242/jcs.260857 · Cited by 40 · see citing works

Emr1 regulates the number of foci of the endoplasmic reticulum-mitochondria encounter structure complex

Rasul, F., Zheng, F., Dong, F., He, J., Liu, L., Liu, W., Cheema, J. Y., Wei, W., & Fu, C. (2021) · Nature Communications · doi:10.1038/s41467-020-20866-x · Cited by 35 · see citing works

The ER-SURF pathway uses ER-mitochondria contact sites for protein targeting to mitochondria

Koch, C., Lenhard, S., Räschle, M., Prescianotto‐Baschong, C., Spang, A., & Herrmann, J. M. (2024) · EMBO Reports · doi:10.1038/s44319-024-00113-w · Cited by 37 · see citing works

Transport Pathways That Contribute to the Cellular Distribution of Phosphatidylserine

Lenoir, G., D’Ambrosio, J. M., Dieudonné, T., & Čopič, A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.737907 · Cited by 37 · see citing works

The multifunctional nature of mitochondrial contact site proteins

Harper, C. S., White, A. J., & Lackner, L. L. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.02.010 · Cited by 35 · see citing works

Improved Split-GFP Systems for Visualizing Organelle Contact Sites in Yeast and Human Cells

Tashiro, S., Kakimoto, Y., Shinmyo, M., Fujimoto, S., & Tamura, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.571388 · Cited by 33 · see citing works

Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels

Egea, P. F. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.784367 · Cited by 33 · see citing works

PDZD-8 and TEX-2 regulate endosomal PI(4,5)P2 homeostasis via lipid transport to promote embryogenesis in C. elegans

Jeyasimman, D., Ercan, B., Dharmawan, D., Naito, T., Sun, J., & Saheki, Y. (2021) · Nature Communications · doi:10.1038/s41467-021-26177-z · Cited by 30 · see citing works

Molecular species selectivity of lipid transport creates a mitochondrial sink for di‐unsaturated phospholipids

Renne, M. F., Bao, X., Hokken, M., Bierhuizen, D., Hermansson, M., Sprenger, R. R., Ewing, T. A., Ma, X., Cox, R. C., Brouwers, J. F. H. M., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106837 · Cited by 30 · see citing works

Specialized ER membrane domains for lipid metabolism and transport

Nishimura, T., & Stefan, C. J. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.07.001 · Cited by 30 · see citing works

The ERMES (Endoplasmic Reticulum and Mitochondria Encounter Structures) mediated functions in fungi

Kundu, D., & Pasrija, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.02.010 · Cited by 30 · see citing works

Calcium-dependent and -independent lipid transfer mediated by tricalbins in yeast

Qian, T., Li, C., He, R., Wan, C., Liu, Y., & Yu, H. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100729 · Cited by 30 · see citing works

ER-SURF: Riding the Endoplasmic Reticulum Surface to Mitochondria

Koch, C., Schuldiner, M., & Herrmann, J. M. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179655 · Cited by 30 · see citing works

Putative role of STING-mitochondria associated membrane crosstalk in immunity

Xue, C., Dong, N., & Shan, A. (2022) · Trends in Immunology · doi:10.1016/j.it.2022.04.011 · Cited by 31 · see citing works

SMP domain proteins in membrane lipid dynamics

Jeyasimman, D., & Saheki, Y. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2019.04.007 · Cited by 29 · see citing works

Insights into membrane association of the SMP domain of extended synaptotagmin

Wang, Y., Li, Z., Wang, X., Zhao, Z., Jiao, L., Liu, R., Wang, K., Ma, R., Yang, Y., Chen, G., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37202-8 · Cited by 29 · see citing works

The endoplasmic reticulum-mitochondria encounter structure: coordinating lipid metabolism across membranes

Kornmann, B. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0102 · Cited by 27 · see citing works

Biogenesis of mitochondrial β‐barrel membrane proteins

Ganesan, I., Busto, J. V., Pfanner, N., & Wiedemann, N. (2024) · FEBS Open Bio · doi:10.1002/2211-5463.13905 · Cited by 28 · see citing works

Arabidopsis synaptotagmin 1 mediates lipid transport in a lipid composition‐dependent manner

Qian, T., Li, C., Liu, F., Xu, K., Wan, C., Liu, Y., & Yu, H. (2022) · Traffic · doi:10.1111/tra.12844 · Cited by 28 · see citing works

Molecular Mechanisms of Pathogenic Fungal Virulence Regulation by Cell Membrane Phospholipids

Li, Y., Wang, H., Wang, H., Wang, T., Wu, D., & Wei, W. (2025) · Journal of Fungi · doi:10.3390/jof11040256 · Cited by 27 · see citing works

Mitochondria–ER–PM contacts regulate mitochondrial division and PI(4)P distribution

Casler, J. C., Harper, C. S., White, A. J., Anderson, H. L., & Lackner, L. L. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202308144 · Cited by 24 · see citing works

ER: the Silk Road of interorganellar communication

Wang, J., & Dehesh, K. (2018) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2018.07.012 · Cited by 24 · see citing works

Specificity of lipid transfer proteins: An in vitro story

Hamaï, A., & Drin, G. (2024) · Biochimie · doi:10.1016/j.biochi.2024.09.007 · Cited by 22 · see citing works

Environmental and Nutritional “Stressors” and Oligodendrocyte Dysfunction: Role of Mitochondrial and Endoplasmatic Reticulum Impairment

Maiuolo, J., Gliozzi, M., Musolino, V., Carresi, C., Nucera, S., Scicchitano, M., Scarano, F., Bosco, F., Oppedisano, F., Macrì, R., et al. (2020) · Biomedicines · doi:10.3390/biomedicines8120553 · Cited by 21 · see citing works

Impaired phosphatidylethanolamine metabolism activates a reversible stress response that detects and resolves mutant mitochondrial precursors

Sam, P. N., Calzada, E., Acoba, M. G., Zhao, T., Watanabe, Y., Nejatfard, A., Trinidad, J. C., Shutt, T. E., Neal, S. E., & Claypool, S. M. (2021) · iScience · doi:10.1016/j.isci.2021.102196 · Cited by 23 · see citing works

The phosphatidylcholine transfer protein StarD7 is important for myogenic differentiation in mouse myoblast C2C12 cells and human primary skeletal myoblasts

Horibata, Y., Mitsuhashi, S., Shimizu, H., Maejima, S., Sakamoto, H., Aoyama, C., Ando, H., & Sugimoto, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-59444-y · Cited by 21 · see citing works

Multifaceted roles of porin in mitochondrial protein and lipid transport

Endo, T., & Sakaue, H. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190153 · Cited by 21 · see citing works

Kinetics of Atg2-mediated lipid transfer from the ER can account for phagophore expansionPreprint

von Bülow, S., & Hummer, G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.12.090977 · Cited by 21 · see citing works

New Insights on the Uptake and Trafficking of Coenzyme Q

Guile, M. D., Jain, A., Anderson, K. A., & Clarke, C. F. (2023) · Antioxidants · doi:10.3390/antiox12071391 · Cited by 20 · see citing works

Membrane contact sites and cytoskeleton‐membrane interactions in autophagy

Duckney, P. J., Wang, P., & Hussey, P. J. (2022) · FEBS Letters · doi:10.1002/1873-3468.14414 · Cited by 19 · see citing works

Mitochondrial Control of Fungal Cell Walls: Models and Relevance in Fungal Pathogens

Koch, B., & Traven, A. (2019) · Current Topics in Microbiology and Immunology · doi:10.1007/82_2019_183 · Cited by 19 · see citing works

Mitochondrial junctions with cellular organelles: Ca2+ signalling perspective

Tepikin, A. V. (2018) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-018-2179-z · Cited by 17 · see citing works

Organelle zones in mitochondria

Shimizu, S. (2018) · The Journal of Biochemistry · doi:10.1093/jb/mvy068 · Cited by 18 · see citing works

Dissociation of ERMES clusters plays a key role in attenuating the endoplasmic reticulum stress

Kakimoto, Y., Kojima, R., Shiino, H., Shinmyo, M., Kurokawa, K., Nakano, A., Endo, T., & Tamura, Y. (2022) · iScience · doi:10.1016/j.isci.2022.105362 · Cited by 17 · see citing works

Membrane tethering by the autophagy ATG2A-WIPI4 complex

Graef, M. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1814759115 · Cited by 17 · see citing works

MITOL regulates phosphatidic acid-binding activity of RMDN3/PTPIP51

Ito, N., Takahashi, T., Shiiba, I., Nagashima, S., Inatome, R., & Yanagi, S. (2021) · The Journal of Biochemistry · doi:10.1093/jb/mvab153 · Cited by 16 · see citing works

Navigating the landscape of mitochondrial-ER communication in health and disease

Ronayne, C. T., & Latorre‐Muro, P. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1356500 · Cited by 15 · see citing works

Imaging and proteomics toolkits for studying organelle contact sites

Gamuyao, R., & Chang, C. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1466915 · Cited by 15 · see citing works

Vps39 is required for ethanolamine-stimulated elevation in mitochondrial phosphatidylethanolamine

Iadarola, D. M., Ball, W. B., Trivedi, P. P., Fu, G., Nan, B., & Gohil, V. M. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2020.158655 · Cited by 16 · see citing works

Regulation of mitochondrial cristae organization by Myo19, Miro1 and Miro2, and metaxin 3

Shembekar, S., Nikolaus, P., Honnert, U., Höring, M., Attia, A., Topp, K., Lohmann, B., Liebisch, G., & Bähler, M. (2025) · Journal of Cell Science · doi:10.1242/jcs.263637 · Cited by 14 · see citing works

Mitochondrial phospholipid transport: Role of contact sites and lipid transport proteins

Mavuduru, V. A., Vadupu, L., Ghosh, K. K., Chakrabortty, S., Gulyás, B. Z., Padmanabhan, P., & Ball, W. B. (2024) · Progress in Lipid Research · doi:10.1016/j.plipres.2024.101268 · Cited by 15 · see citing works

Contribution of ERMES subunits to mature peroxisome abundance

Esposito, M., Denmat, S. H., & Delahodde, A. (2019) · PLoS ONE · doi:10.1371/journal.pone.0214287 · Cited by 14 · see citing works

Amino Acids Promote Mitochondrial-Derived Compartment Formation in Mammalian CellsPreprint

Schuler, M.-H., English, A. M., VanderMeer, L., Shaw, J. M., & Hughes, A. L. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.23.424218 · Cited by 13 · see citing works

Mitochondria from the Outside in: The Relationship Between Inter-Organelle Crosstalk and Mitochondrial Internal Organization

Friedman, J. R. (2022) · Contact · doi:10.1177/25152564221133267 · Cited by 12 · see citing works

Mitochondrial protein import machinery conveys stress signals to the cytosol and beyond

Lionaki, E., Gkikas, I., & Tavernarakis, N. (2023) · BioEssays · doi:10.1002/bies.202200160 · Cited by 12 · see citing works

In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility

Okamoto, M., Nakano, K., Takahashi-Nakaguchi, A., Sasamoto, K., Yamaguchi, M., Teixeira, M. C., & Chibana, H. (2023) · Journal of Fungi · doi:10.3390/jof9020240 · Cited by 11 · see citing works

Toward understanding the cellular control of vertebrate mineralization: The potential role of mitochondria

Shapiro, I. M., Risbud, M. V., & Landis, W. J. (2024) · Bone · doi:10.1016/j.bone.2024.117112 · Cited by 12 · see citing works

Complementation Assay Using Fusion of Split-GFP and TurboID (CsFiND) Enables Simultaneous Visualization and Proximity Labeling of Organelle Contact Sites in Yeast

Fujimoto, S., Tashiro, S., & Tamura, Y. (2023) · Contact · doi:10.1177/25152564231153621 · Cited by 11 · see citing works

Structural basis for interorganelle phospholipid transport mediated by VAT-1

Watanabe, Y., Tamura, Y., Kakuta, C., Watanabe, S., & Endo, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011019 · Cited by 11 · see citing works

Mitochondria–plasma membrane contact sites regulate the ER–mitochondria encounter structure

Casler, J. C., Harper, C. S., & Lackner, L. L. (2025) · Journal of Cell Science · doi:10.1242/jcs.263685 · Cited by 10 · see citing works

Suppression of respiratory growth defect of mitochondrial phosphatidylserine decarboxylase deficient mutant by overproduction of Sfh1, a Sec14 homolog, in yeast

Mizuike, A., Kobayashi, S., Rikukawa, T., Ohta, A., Horiuchi, H., & Fukuda, R. (2019) · PLoS ONE · doi:10.1371/journal.pone.0215009 · Cited by 10 · see citing works

Role of the small protein Mco6 in the mitochondrial sorting and assembly machinery

Busto, J. V., Ganesan, I., Mathar, H., Steiert, C., Schneider, E. F., Straub, S. P., Ellenrieder, L., Song, J., Stiller, S. B., Lübbert, P., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.113805 · Cited by 9 · see citing works

Uncovering the principles coordinating systems-level organelle biogenesis with cellular growth

Wang, S., Kailash, D., & Mukherji, S. (2025) · Cell Systems · doi:10.1016/j.cels.2025.101267 · Cited by 9 · see citing works

Supramolecular architecture of the ER-mitochondria encounter structure in its native environmentPreprint

Wozny, M. R., Luca, A. D., Morado, D. R., Picco, A., Hoffmann, P. C., Miller, E. A., Vanni, S., & Kukulski, W. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.12.488000 · Cited by 9 · see citing works

Chemical inhibition of phosphatidylcholine biogenesis reveals its role in mitochondrial division

Shiino, H., Tashiro, S., Hashimoto, M., Sakata, Y., Hosoya, T., Endo, T., Kojima, H., & Tamura, Y. (2024) · iScience · doi:10.1016/j.isci.2024.109189 · Cited by 8 · see citing works

The Endoplasmic Reticulum-Mitochondria Encounter Structure and its Regulatory Proteins

Cheema, J. Y., He, J., Wei, W., & Fu, C. (2021) · Contact · doi:10.1177/25152564211064491 · Cited by 9 · see citing works

Assembly of ERMES Subunit Mdm12 and its Interaction with Synthetic Lipid Bilayers

Coscia, A. (2017) · OpenCommons at University of Connecticut (University of Connecticut)

Crystal structures of Mmm1 and Mdm12–Mmm1 reveal mechanistic insight into phospholipid trafficking at ER-mitochondria contact sites

Jeong, H., Park, J., Jun, Y., & Lee, C. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715592114 · Cited by 108 · see citing works

Determining the Lipid-Binding Specificity of SMP Domains: An ERMES Subunit as a Case Study

AhYoung, A. P., & Egea, P. F. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9136-5_16 · Cited by 6 · see citing works

Mitochondrially tethered Mmm1 can function as a sole lipid transporter at ER–mitochondria contacts

Covill‐Cooke, C., Hirashima, T., Kawano, S., Ganellin, J., Moody, A., van Schie, S. N. S., Peter, A. T. J., Saito, C., Endo, T., & Kornmann, B. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202411196 · Cited by 4 · see citing works

A conserved ER‐membrane complex facilitates phospholipid exchange between the ER and mitochondria (758.5)

Lahiri, S., Chao, J. T., Tavassoli, S., Wong, A., Young, B. P., Loewen, C. J. R., & Prinz, W. A. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.758.5