Control of mitochondrial morphology by a human mitofusin

Basic local alignment search tool

Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669

Predicting coiled coils from protein sequences.

Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953

The GTPase superfamily: conserved structure and molecular mechanism

Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392

PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization

Nakai, K., & Horton, P. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01336-x · Cited by 2,181

Mitochondrial transcription factor A is necessary for mtDNA maintance and embryogenesis in mice

Larsson, N.-G., Wang, J., Wilhelmsson, H., Oldfors, A., Rustin, P., Lewandoski, M., Barsh, G. S., & Clayton, D. A. (1998) · Nature Genetics · doi:10.1038/ng0398-231 · Cited by 1,594

The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast

Bleazard, W., McCaffery, J. M., King, E. J., Bale, S., Mozdy, A. D., Tieu, Q., Nunnari, J. M., & Shaw, J. M. (1999) · Nature Cell Biology · doi:10.1038/13014 · Cited by 795

Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms.

Piperno, G., & Fuller, M. T. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.6.2085 · Cited by 758

A Human Dynamin-related Protein Controls the Distribution of Mitochondria

Смирнова, Е. А., Shurland, D., Ryazantsev, S. N., & van der Bliek, A. M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.351 · Cited by 734

MultiCoil: A program for predicting two‐and three‐stranded coiled coils

Wolf, E., Kim, P. S., & Berger, B. (1997) · Protein Science · doi:10.1002/pro.5560060606 · Cited by 720

C. elegans Dynamin-Related Protein DRP-1 Controls Severing of the Mitochondrial Outer Membrane

Labrousse, A. M., Zappaterra, M. D., Rube, D. A., & van der Bliek, A. M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80391-3 · Cited by 670

Tuberculosis infection and lung adenocarcinoma: Mendelian randomization and pathway analysis of genome-wide association study data from never-smoking Asian women

Wong, J. Y. Y., Zhang, H., Hsiung, C. A., Shiraishi, K., Yu, K., Matsuo, K., Wong, M. P., Hong, Y., Wang, J., Seow, W. J., et al. (2019) · Genomics · doi:10.1016/j.ygeno.2019.07.008 · Cited by 24

Mitochondria: A mirror into cellular dysfunction in heart disease

White, M. Y., Edwards, A. V. G., Cordwell, S. J., & Eyk, J. E. V. (2008) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200780135 · Cited by 24

Calcium-induced alteration of mitochondrial morphology and mitochondrial-endoplasmic reticulum contacts in rat brown adipocytes

Golić, I., Veličković, K., Markelic, M. B., Stančić, A., Janković, A., Vučetić, M., Otašević, V., Buzadžić, B., Korać, B., & Korać, A. (2014) · European Journal of Histochemistry · doi:10.4081/ejh.2014.2377 · Cited by 24

Site-specific mitochondrial dysfunction in neurodegeneration

Vodičková, A., Koren, S. A., & Wojtovich, A. P. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.02.004 · Cited by 22

C1QBP regulates mitochondrial plasticity to impact tumor progression and antitumor immune response

Wang, Q., Chai, D., Sobhani, N., Sun, N., Neeli, P. K., Zheng, J., & Tian, H. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.1012112 · Cited by 29

The regulatory role of adipocyte mitochondrial homeostasis in metabolism-related diseases

Song, H., Zhang, X., Wang, J., Wu, Y., Xiong, T., Shen, J., Lin, R., Xiao, T., & Lin, W. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1261204 · Cited by 22

Mitofusin 1 degradation is induced by a disruptor of mitochondrial calcium homeostasis, CGP37157: A role in apoptosis in prostate cancer cells

Choudhary, V., Kaddour‐Djebbar, I., Alaisami, R., Kumar, M. V., & Bollag, W. B. (2014) · International Journal of Oncology · doi:10.3892/ijo.2014.2343 · Cited by 23

Role of the permeability transition pore complex in lethal inter-organelle crosstalk

Dein, O. S. E. (2009) · Frontiers in bioscience · doi:10.2741/3465 · Cited by 28

Mitochondrial Dysfunction in Cardiorenal Syndrome

Doi, K., & Noiri, E. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6654 · Cited by 24

High-resolution profiles of gene expression and DNA methylation highlight mitochondrial modifications during early embryonic development

Ren, L., Zhang, C., Tao, L., Jing, H. A. O., Tan, K., Miao, K., Yu, Y., Sui, L., Wu, Z., Tian, J., et al. (2017) · Journal of Reproduction and Development · doi:10.1262/jrd.2016-168 · Cited by 23

Pla2g6 Deficiency in Zebrafish Leads to Dopaminergic Cell Death, Axonal Degeneration, Increased β-Synuclein Expression, and Defects in Brain Functions and Pathways

Sánchez, E., Azcona, L. J., & Paisán‐Ruiz, C. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0846-2 · Cited by 23

Mitofusin-2 Triggers Cervical Carcinoma Cell Hela Apoptosis via Mitochondrial Pathway in Mouse Model

Wang, W., Liu, X., Guo, X., & Quan, H. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000488410 · Cited by 23

Mitochondrial fusion and Bid-mediated mitochondrial apoptosis are perturbed by alcohol with distinct dependence on its metabolism

Naghdi, S., Slovinsky, W. S., Madesh, M., Rubin, E., & Hajnóczky, G. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1070-3 · Cited by 23

Bacterial dynamin‐like protein DynA mediates lipid and content mixing

Guo, L., & Bramkamp, M. (2019) · The FASEB Journal · doi:10.1096/fj.201900844rr · Cited by 23

Renal ischemia alters expression of mitochondria-related genes and impairs mitochondrial structure and function in swine scattered tubular-like cells

Farahani, R. A., Zhu, X.-Y., Tang, H., Jordan, K. L., Lerman, L. O., & Eirin, A. (2020) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00120.2020 · Cited by 23

Scission, spores, and apoptosis: a proposal for the evolutionary origin of mitochondria in cell death induction

Frank, S., Robert, E. G., & Youle, R. J. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00620-x · Cited by 23

Peripheral neuropathy in mitochondrial disease

Horváth, R., Medina, J. M., Reilly, M. M., Shy, M. E., & Zuchner, S. L. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-12-821751-1.00014-2 · Cited by 22

Mitochondrial GTP metabolism controls reproductive aging in C. elegans

Lee, Y.-T., Savini, M., Chen, T., Yang, J., Zhao, Q., Ding, L., Gao, S. M., Şentürk, M., Sowa, J. N., Wang, J. D., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.08.019 · Cited by 24

Mitochondrial hyperfusion induces metabolic remodeling in lung endothelial cells by modifying the activities of electron transport chain complexes I and III

Yegambaram, M., Sun, X., Lü, Q., Jin, Y., Ornatowski, W., Soto, J. E., Aggarwal, S., Wang, T., Tieu, K., Gu, H., et al. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.11.008 · Cited by 23

High expression of Mfn1 promotes early development of bovine SCNT embryos: Improvement of mitochondrial membrane potential and oxidative metabolism

Hua, S., Zhang, H., Song, Y., Li, R., Liu, J., Wang, Y., Quan, F., & Zhang, Y. (2012) · Mitochondrion · doi:10.1016/j.mito.2011.12.002 · Cited by 22

MFN2‐related genetic and clinical features in a cohort of Chinese CMT2 patients

Xie, Y., Li, X., Liu, L., Hu, Z., Huang, S., Zhan, Y., Zi, X., Xia, K., Tang, B., & Zhang, R. (2016) · Journal of the Peripheral Nervous System · doi:10.1111/jns.12159 · Cited by 22

Dietary Macronutrient Management to Treat Mitochondrial Dysfunction in Parkinson’s Disease

Bajracharya, R., Youngson, N. A., & Ballard, J. W. O. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081850 · Cited by 24

Inhibition of cAMP/PKA Pathway Protects Optic Nerve Head Astrocytes against Oxidative Stress by Akt/Bax Phosphorylation-Mediated Mfn1/2 Oligomerization

Ju, W., Shim, M. S., Keun-young Kim, A., Park, T. L., Ahn, S., Edwards, G., & Weinreb, R. N. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/8060962 · Cited by 22

Knocking-out the Siah2 E3 ubiquitin ligase prevents mitochondrial NCX3 degradation, regulates mitochondrial fission and fusion, and restores mitochondrial function in hypoxic neurons

Sisalli, M. J., Ianniello, G., Savoia, C., Cuomo, O., Annunziato, L., & Scorziello, A. (2020) · Cell Communication and Signaling · doi:10.1186/s12964-020-0529-x · Cited by 23

Epstein–Barr virus immediate-early proteins BZLF1 and BRLF1 alter mitochondrial morphology during lytic replication

LaJeunesse, D., Brooks, K., & Adamson, A. L. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.05.120 · Cited by 22

Mechanisms of Modulation of Mitochondrial Architecture

Muñoz, J. P., Basei, F. L., Rojas, M. L., Galvis, D., & Antonio Zorzano, A. (2023) · Biomolecules · doi:10.3390/biom13081225 · Cited by 21

The nonstructural protein 1 of respiratory syncytial virus hijacks host mitophagy as a novel mitophagy receptor to evade the type I IFN response in HEp-2 cells

Cheng, J., Wang, Y., Yin, L., Liang, W., Zhang, J., Ma, C., Zhang, Y., Liu, B., Wang, J., Zhao, W., et al. (2023) · mBio · doi:10.1128/mbio.01480-23 · Cited by 23

Higd-1a regulates the proliferation of pancreatic cancer cells through a pERK/p27KIP1/pRB pathway

An, H., Ryu, M., Jeong, H. J., Kang, M., Jeon, H.-M., Lee, J., Kim, Y. S., & Lee, H. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.07.007 · Cited by 21

Endoplasmic Reticulum Stress of Gut Enterocyte and Intestinal Diseases

Gao, H., He, C., Hua, R., Guo, Y., Wang, B., Liang, C., Gao, L., Shang, H., & Xu, J. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.817392 · Cited by 21

Modeling neuromuscular diseases in zebrafish

Singh, J., & Patten, S. A. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1054573 · Cited by 21

Control of mitochondrial integrity in Parkinson’s disease

Vives-Bauzá, C., Tocilescu, M. A., deVries, R. L. A., Wolken, D. M. A., Jackson-Lewis, V. R., & Przedborski, S. (2010) · Progress in brain research · doi:10.1016/s0079-6123(10)83006-7 · Cited by 20

A Disturbance in the Force: Cellular Stress Sensing by the Mitochondrial Network

Gilkerson, R. (2018) · Antioxidants · doi:10.3390/antiox7100126 · Cited by 22

A Novel Potential Role for Gametogenetin-Binding Protein 1 (GGNBP1) in Mitochondrial Morphogenesis During Spermatogenesis in Mice1

Aihara, T., Nakamura, N., Honda, S., & Hirose, S. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.108.074013 · Cited by 21

Axonal Length Determines Distinct Homeostatic Phenotypes in Human iPSC Derived Motor Neurons on a Bioengineered Platform

Hagemann, C., Moreno-Gonzalez, C., Guetta, L., Tyzack, G. E., Chiappini, C., Legati, A., Patani, R., & Serio, A. (2022) · Advanced Healthcare Materials · doi:10.1002/adhm.202101817 · Cited by 20

Oxidative Stress and Mitochondria Are Involved in Anaphylaxis and Mast Cell Degranulation: A Systematic Review

Piotin, A., Oulehri, W., Charles, A., Tacquard, C. A., Collange, O., Mertès, P., & Gény, B. (2024) · Antioxidants · doi:10.3390/antiox13080920 · Cited by 21

Mitochondrial remodeling following fission inhibition by 15d-PGJ2 involves molecular changes in mitochondrial fusion protein OPA1

Kar, R., Mishra, N., Singha, P. K., Venkatachalam, M. A., & Saikumar, P. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.07.108 · Cited by 22

Two Spanish families with Charcot–Marie–Tooth type 2A: Clinical, electrophysiological and molecular findings

Banchs, I., Casasnovas, C., Montero, J., Martínez‐Matos, J. A., & Volpini, V. (2008) · Neuromuscular Disorders · doi:10.1016/j.nmd.2008.09.006 · Cited by 20

Regulation of adrenocortical steroid hormone production by RhoA–diaphanous 1 signaling and the cytoskeleton

Sewer, M. B., & Li, D. (2012) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2012.11.014 · Cited by 19

Clinical and molecular aspects of diseases of mitochondrial DNA instability.

Mao, C.-C., & Holt, I. J. (2009) · PubMed · Cited by 20

The Shape of Mitochondrial Dysfunction in Down Syndrome

Zamponi, E., & Helguera, P. R. (2019) · Developmental Neurobiology · doi:10.1002/dneu.22673 · Cited by 20

A novel therapy, using Ghrelin with pegylated G-CSF, inhibits brain hemorrhage from ionizing radiation or combined radiation injury

Jg, K., Jt, S., Anderson, M. N., Umali, M. V., Ho, C., Zhai, M., Lin, B., & Jiang, S. (2019) · Pharmacy & Pharmacology International Journal · doi:10.15406/ppij.2019.07.00243 · Cited by 20

What is the biological significance of the two mitofusin proteins present in the outer mitochondrial membrane of mammalian cells?

Zorzano, A., & Pich, S. (2006) · IUBMB Life · doi:10.1080/15216540600644838 · Cited by 20

The dynamin-related mouse mitochondrial GTPase OPA1 alters the structure of the mitochondrial inner membrane when exogenously introduced into COS-7 cells

Misaka, T., Murate, M., Fujimoto, K., & Kubo, Y. (2006) · Neuroscience Research · doi:10.1016/j.neures.2006.02.010 · Cited by 20

Germ‐line specific variants of components of the mitochondrial outer membrane import machinery in Drosophila

Hwa, J. J., Zhu, A. J., Hiller, M. A., Kon, C., Fuller, M. T., & Santel, A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.07.025 · Cited by 20

Over-Expressing Mitofusin-2 in Healthy Mature Mammalian Skeletal Muscle Does Not Alter Mitochondrial Bioenergetics

Lally, J. S. V., Herbst, E. A. F., Matravadia, S., Maher, A. C., Perry, C. G. R., Ventura-Clapier, R., & Holloway, G. P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055660 · Cited by 19

Japanese Encephalitis Virus Infection Causes an Imbalance in the Activation of Mitochondrial Fusion/Fission Genes and Triggers the Activation of NOX2-mediated Oxidative Stress and Neuronal Cell Death

Singh, G., & Kumar, A. (2023) · Neurochemical Research · doi:10.1007/s11064-023-03898-9 · Cited by 19

Epigenetic Regulation of Cardiomyocyte Maturation by Arginine Methyltransferase CARM1

Garbutt, T. A., Wang, Z., Wang, H., Ma, H., Ruan, H., Dong, Y., Xie, Y., Tan, L., Phookan, R., Stouffer, J. A., et al. (2024) · Circulation · doi:10.1161/circulationaha.121.055738 · Cited by 19

So close, yet so far away: the relationship between MAM and cardiac disease

Lu, J., Chen, X., Ma, Y., Gui, M., Yao, L., Li, J., Wang, M., Zhou, X., & Fu, D. (2024) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2024.1353533 · Cited by 19

Effect of mitofusin 2 overexpression on the proliferation and apoptosis of high-glucose-induced rat glomerular mesangial cells

Tang, W., Cui, T., Ben, W., Wu, W., & Fu, P. (2012) · Journal of Nephrology · doi:10.5301/jn.5000089 · Cited by 19

Relationship between mitofusin 2 and cancer

Allegra, A., Innao, V., Allegra, A. G., & Musolino, C. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.11.009 · Cited by 21

The second genome: Effects of the mitochondrial genome on cancer progression

Scheid, A. D., Beadnell, T. C., & Welch, D. R. (2019) · Advances in cancer research · doi:10.1016/bs.acr.2019.01.001 · Cited by 21

Miro1 functions as an inhibitory regulator of MFN at elevated mitochondrial Ca2+ levels

Fatiga, F. F., Wang, L., Hsu, T., Capuno, J. I., & Fu, C. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30138 · Cited by 20

The regulation of mitochondrial physiology by organelle‐associated GTP‐binding proteins

Thomson, M. (2002) · Cell Biochemistry and Function · doi:10.1002/cbf.974 · Cited by 19

Mitochondrial dynamics at the intersection of macrophage polarization and metabolism

Li, P., Fan, Z., Huang, Y., Luo, L., & Wu, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1520814 · Cited by 23

Dysfunctional mitochondria elicit bioenergetic decline in the aged heart

Mone, P., Agyapong, E. D., Morciano, G., Jankauskas, S. S., Luca, A. D., Varzideh, F., Pinton, P., & Santulli, G. (2024) · The Journal of Cardiovascular Aging · doi:10.20517/jca.2023.50 · Cited by 19

The Effect of a Novel c.820C>T (Arg274Trp) Mutation in the Mitofusin 2 Gene on Fibroblast Metabolism and Clinical Manifestation in a Patient

Beresewicz, M., Boratyńska-Jasińska, A., Charzewski, Ł., Kawalec, M., Kabzińska, D., Kochański, A., Krzyśko, K. A., & Zabłocka, B. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169999 · Cited by 18

Parvalbumin alters mitochondrial dynamics and affects cell morphology

Janickova, L., Henzi, T., Safiulina, D., Kaasik, A., & Schwaller, B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2921-x · Cited by 18

A catalytic domain variant of mitofusin requiring a wildtype paralog for function uncouples mitochondrial outer-membrane tethering and fusion

Engelhart, E. A., & Hoppins, S. C. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006347 · Cited by 19

Clock-Controlled Mitochondrial Dynamics Correlates with Cyclic Pregnenolone Synthesis

Witzig, M., Grimm, A., Schmitt, K., Lejri, I., Frank, S., Brown, S. A., & Eckert, A. (2020) · Cells · doi:10.3390/cells9102323 · Cited by 20

A Molecular Perspective on Mitochondrial Membrane Fusion: From the Key Players to Oligomerization and Tethering of Mitofusin

Vecchis, D. D., Brandner, A. F., Baaden, M., Cohen, M. M., & Taly, A. (2019) · The Journal of Membrane Biology · doi:10.1007/s00232-019-00089-y · Cited by 20

Ferroptosis: Iron-mediated cell death linked to disease pathogenesis

Zhang, X., Hu, Y., Wang, B., & Yang, S. (2024) · Journal of Biomedical Research · doi:10.7555/jbr.37.20230224 · Cited by 18

Dynamic interaction of REEP5–MFN1/2 enables mitochondrial hitchhiking on tubular ER

Chen, S., Sun, Y., Qin, Y., Yang, L., Hao, Z., Xu, Z., Björklund, M., Liu, W., & Hong, Z. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202304031 · Cited by 17

The Role of Mitochondrial Enzymes, Succinate-Coupled Signaling Pathways and Mitochondrial Ultrastructure in the Formation of Urgent Adaptation to Acute Hypoxia in the Myocardium

Germanova, E. L., Khmil, N. V., Pavlik, L. L., Mikheeva, I. B., Mironova, G. D., & Lukyanova, L. D. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214248 · Cited by 17

Pediatric Neuromuscular Diseases

Rathore, G., & Kang, P. B. (2023) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2023.08.034 · Cited by 19

Determining the target protein localization in 3D using the combination of FIB-SEM and APEX2

Shi, Y., Wang, L., Zhang, J., Zhai, Y., & Sun, F. (2017) · Biophysics Reports · doi:10.1007/s41048-017-0043-x · Cited by 17

Hemagglutinin-neuraminidase and fusion proteins of virulent Newcastle disease virus cooperatively disturb fusion–fission homeostasis to enhance mitochondrial function by activating the unfolded protein response of endoplasmic reticulum and mitochondrial stress

Ren, S., Rehman, Z. U., Shi, M., Yang, B., Liu, P., Yin, Y., Qu, Y., Meng, C., Yang, Z., Gao, X., et al. (2019) · Veterinary Research · doi:10.1186/s13567-019-0654-y · Cited by 18

Ubiquitination of interleukin-1α is associated with increased pro-inflammatory polarization of murine macrophages deficient in the E3 ligase ITCH

Lin, X., Zhang, H., Boyce, B. F., & Xing, L. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014298 · Cited by 17

MFN2 interacts with nuage-associated proteins and is essential for male germ cell development by controlling mRNA fate during spermatogenesis

Wang, X., Wen, Y., Zhang, J., Swanson, G., Guo, S., Cao, C., Krawetz, S. A., Zhang, Z., & Yuan, S. (2021) · Development · doi:10.1242/dev.196295 · Cited by 17

Embryonic Surface Ectoderm-specific Mitofusin 2 Conditional Knockout Induces Congenital Cataracts in Mice

Zhao, J., Wu, X., Wu, D., Yu, Y., Yu, Y., Wang, Y., Fu, Q., Zhang, J., & Yao, K. (2018) · Scientific Reports · doi:10.1038/s41598-018-19849-2 · Cited by 17

Regulation of PGC-1α and PGC-1α-responsive genes with forskolin-induced Schwann cell differentiation

Cowell, R. M., Blake, K. R., Inoue, T., & Russell, J. W. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.04.104 · Cited by 17

Mitochondrial quality control: a pathophysiological mechanism and potential therapeutic target for chronic obstructive pulmonary disease

Xu, M., Feng, P., Yan, J., & Li, L. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1474310 · Cited by 19

The evaluative value of Sema3C and MFN2 co-expression detected by immunohistochemistry for prognosis in hepatocellular carcinoma patients after hepatectomy

liu, J., Zhu, K.-L., Chen, J., tang, J., Liang, Y., Xu, F., Jin, R., Liang, X. H., & Cai, X. (2016) · OncoTargets and Therapy · doi:10.2147/ott.s98322 · Cited by 16

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Gilkerson, R., Kaur, H., Carrillo, O., & Ramos, I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084566 · Cited by 16

Bex3 associates with replicating mitochondria and is involved in possible growth control of F9 teratocarcinoma cells

Kim, A., Lee, C.-S., & Schlessinger, D. (2004) · Gene · doi:10.1016/j.gene.2004.08.031 · Cited by 16

Physics-based oligomeric models of the yeast mitofusin Fzo1 at the molecular scale in the context of membrane docking

Brandner, A. F., Vecchis, D. D., Baaden, M., Cohen, M. M., & Taly, A. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.06.010 · Cited by 18

Defective nucleotide-dependent assembly and membrane fusion in Mfn2 CMT2A variants improved by Bax

Samanas, N. B., Engelhart, E. A., & Hoppins, S. C. (2020) · Life Science Alliance · doi:10.26508/lsa.201900527 · Cited by 16

Mitofusin 2 but not mitofusin 1 mediates Bcl-XL-induced mitochondrial aggregation

Du, M., Si, Y., Su, W., Zhao, M., Yang, F., Liu, Y., Mai, Z., Wang, Y., Wang, X., & Chen, T. (2020) · Journal of Cell Science · doi:10.1242/jcs.245001 · Cited by 16

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Zou, W., Ji, D., Zhang, Z., Yang, L., & Cao, Y. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.717328 · Cited by 18

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Wang, J., Lin, X., Zhao, N., Dong, G., Wu, W., Huang, K., & Fu, J. (2022) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2703107 · Cited by 16

Mitofusin 1 inhibits an apoptosis-associated amino-terminal conformational change in Bax, but not its mitochondrial translocation, in a GTPase-dependent manner

Ryu, S., Choi, K., Park, J., Park, Y., Kim, S., & Choi, C. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.03.038 · Cited by 16

Natural Compounds Play Therapeutic Roles in Various Human Pathologies via Regulating Endoplasmic Reticulum Pathway

Ma, R., Ni, Z., Thakur, K., Zhang, F., Zhang, Y., Zhang, J., & Wei, Z. (2020) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2020.100065 · Cited by 16

In Vivo Pravastatin Treatment Reverses Hypercholesterolemia Induced Mitochondria-Associated Membranes Contact Sites, Foam Cell Formation, and Phagocytosis in Macrophages

Assis, L. H. D. P., Dorighello, G. G., Rentz, T., de Souza, J. C., Vercesi, A. E., & Oliveira, H. C. F. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.839428 · Cited by 15

The ER-Mitochondria Interface as a Dynamic Hub for T Cell Efficacy in Solid Tumors

Hunt, E. G., Andrews, A. M., Larsen, S. R., & Thaxton, J. E. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.867341 · Cited by 16

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