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Interactome Analysis Reveals Ezrin Can Adopt Multiple Conformational States

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α3β1 integrin promotes cell survival via multiple interactions between 14-3-3 isoforms and proapoptotic proteins

Oh, J.-E., Jang, D. H., Kim, H., Kang, H. K., Chung, C., Park, W. H., & Min, B. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.08.002 · Cited by 34 · see citing works

Alternative Wnt Signaling Activates YAP/TAZ

Park, H. W., Kim, Y. C., Yu, B., Moroishi, T., Mo, J., Plouffe, S. W., Meng, Z., Lin, K. C., Yu, F., Alexander, C. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.013 · Cited by 708 · see citing works

The Hippo Pathway in Heart Development, Regeneration, and Diseases

Zhou, Q., Li, L., Zhao, B., & Guan, K. (2015) · Circulation Research · doi:10.1161/circresaha.116.303311 · Cited by 219 · see citing works

The ciliary membrane‐associated proteome reveals actin‐binding proteins as key components of cilia

Kohli, P., Höhne, M., Jüngst, C., Bertsch, S., Ebert, L. K., Schauss, A. C., Benzing, T., Rinschen, M. M., & Schermer, B. (2017) · The EMBO Reports · doi:10.15252/embr.201643846 · Cited by 145 · see citing works

YAP and TAZ Are Not Identical Twins

Reggiani, F., Gobbi, G., Ciarrocchi, A., & Sancisi, V. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.08.012 · Cited by 153 · see citing works

YAP and TAZ in Lung Cancer: Oncogenic Role and Clinical Targeting

Sardo, F. L., Strano, S., & Blandino, G. (2018) · Cancers · doi:10.3390/cancers10050137 · Cited by 120 · see citing works

The mammalian Hippo pathway: regulation and function of YAP1 and TAZ

Kodaka, M., & Hata, Y. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1742-9 · Cited by 108 · see citing works

A Multi-layered Quantitative In Vivo Expression Atlas of the Podocyte Unravels Kidney Disease Candidate Genes

Rinschen, M. M., Gödel, M., Grahammer, F., Zschiedrich, S., Helmstädter, M., Kretz, O., Zarei, M., Braun, D. A., Dittrich, S., Pahmeyer, C., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.059 · Cited by 105 · see citing works

Hippo and TGF-β interplay in the lung field

Saito, A., & Nagase, T. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00238.2015 · Cited by 92 · see citing works

YAP-mediated mechanotransduction determines the podocyte’s response to damage

Rinschen, M. M., Grahammer, F., Hoppe, A.-K., Kohli, P., Hagmann, H., Kretz, O., Bertsch, S., Höhne, M., Göbel, H., Bartram, M. P., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aaf8165 · Cited by 90 · see citing works

The MST/Hippo Pathway and Cell Death: A Non-Canonical Affair

Fallahi, E., O’Driscoll, N. A., & Matallanas, D. (2016) · Genes · doi:10.3390/genes7060028 · Cited by 89 · see citing works

The emerging role of Hippo signaling in neurodegeneration

Sahu, M. R., & Mondal, A. C. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24551 · Cited by 80 · see citing works

Yap is essential for retinal progenitor cell cycle progression and RPE cell fate acquisition in the developing mouse eye

Kim, J. Y., Park, R., Lee, J. H. J., Shin, J., Nickas, J. M., Kim, S., & Cho, S. (2016) · Developmental Biology · doi:10.1016/j.ydbio.2016.09.001 · Cited by 78 · see citing works

Altered lipid metabolism in the aging kidney identified by three layered omic analysis

Braun, F., Rinschen, M. M., Bartels, V., Frommolt, P., Habermann, B. H., Hoeijmakers, J. H. J., Schumacher, B., Dollé, M. E. T., Müller, R., Benzing, T. R., et al. (2016) · Aging · doi:10.18632/aging.100900 · Cited by 70 · see citing works

The Hippo pathway in disease and therapy: cancer and beyond

Gómez-Ferrer, M., Gómez, V., & Hergovich, A. (2014) · Clinical and Translational Medicine · doi:10.1186/2001-1326-3-22 · Cited by 66 · see citing works

Versatile approach for functional analysis of human proteins and efficient stable cell line generation using FLP-mediated recombination system

Szczęsny, R. J., Kowalska, K. J., Kłosowska-Kosicka, K., Chlebowski, A., Owczarek, E. P., Warkocki, Z., Kuliński, T. M., Adamska, D., Affek, K., Jędroszkowiak, A., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0194887 · Cited by 59 · see citing works

Single-nephron proteomes connect morphology and function in proteinuric kidney disease

Höhne, M., Frese, C. K., Grahammer, F., Dafinger, C., Ciarimboli, G., Butt, L., Binz-Lotter, J., Hackl, M. J., Rahmatollahi, M., Kann, M., et al. (2018) · Kidney International · doi:10.1016/j.kint.2017.12.012 · Cited by 58 · see citing works

Hippo‐yap signaling in ocular development and disease

Lee, M., Goraya, N., Kim, S., & Cho, S. (2018) · Developmental Dynamics · doi:10.1002/dvdy.24628 · Cited by 57 · see citing works

The ubiquitin ligase Ubr4 controls stability of podocin/MEC-2 supercomplexes

Rinschen, M. M., Bharill, P., Wu, X., Kohli, P., Reinert, M. J., Kretz, O., Sáez, I., Schermer, B., Höhne, M., Bartram, M. P., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw016 · Cited by 55 · see citing works

G Protein-Coupled Receptor Systems and Their Role in Cellular Senescence

Santos‐Otte, P., Leysen, H., van Gastel, J., Hendrickx, J. O., Martin, B., & Maudsley, S. R. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.08.005 · Cited by 54 · see citing works

The tissue proteome in the multi-omic landscape of kidney disease

Rinschen, M. M., & Sáez-Rodríguez, J. (2020) · Nature Reviews Nephrology · doi:10.1038/s41581-020-00348-5 · Cited by 45 · see citing works

Cysteine S-Glutathionylation Promotes Stability and Activation of the Hippo Downstream Effector Transcriptional Co-activator with PDZ-binding Motif (TAZ)

Gandhirajan, R. K., Jain, M., Walla, B., Johnsen, M., Bartram, M. P., Anh, M. H., Rinschen, M. M., Benzing, T. R., & Schermer, B. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.712539 · Cited by 42 · see citing works

Three-layered proteomic characterization of a novelACTN4mutation unravels its pathogenic potential in FSGS

Bartram, M. P., Habbig, S., Pahmeyer, C., Höhne, M., Weber, L. T., Thiele, H., Altmüller, J., Kottoor, N., Wenzel, A., Krüger, M., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddv638 · Cited by 42 · see citing works

Unraveling Subcellular and Ultrastructural Changes During Vitrification of Human Spermatozoa: Effect of a Mitochondria-Targeted Antioxidant and a Permeable Cryoprotectant

Kumar, P., Wang, M., Isachenko, E., Rahimi, G., Mallmann, P. K., Wang, W., von Brandenstein, M., & Isachenko, V. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.672862 · Cited by 40 · see citing works

Combined role for YAP-TEAD and YAP-RUNX2 signalling in substrate-stiffness regulation of cardiac fibroblast proliferation

Ebrahimighaei, R., Sala‐Newby, G. B., Hudson, C. A., Kimura, T. E., Hathway, T., Hawkins, J., McNeill, M. C., Richardson, R. J., Newby, A. C., & Bond, M. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119329 · Cited by 39 · see citing works

Angiomotin Regulates YAP Localization during Neural Differentiation of Human Pluripotent Stem Cells

Zaltsman, Y., Masuko, S., Bensen, J. J., & Kiessling, L. L. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2019.03.009 · Cited by 37 · see citing works

Quantitative deep mapping of the cultured podocyte proteome uncovers shifts in proteostatic mechanisms during differentiation

Rinschen, M. M., Schroeter, C. B., Koehler, S., Ising, C., Schermer, B., Kann, M., Benzing, T. R., & Brinkkoetter, P. T. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00121.2016 · Cited by 36 · see citing works

Decoding protein networks during virus entry by quantitative proteomics

Gerold, G., Bruening, J., & Pietschmann, T. (2015) · Virus Research · doi:10.1016/j.virusres.2015.09.006 · Cited by 33 · see citing works

Comparative phosphoproteomic analysis of mammalian glomeruli reveals conserved podocin C‐terminal phosphorylation as a determinant of slit diaphragm complex architecture

Rinschen, M. M., Pahmeyer, C., Pisitkun, T., Schnell, N., Wu, X., Maaß, M., Bartram, M. P., Lamkemeyer, T., Schermer, B., Benzing, T. R., et al. (2014) · PROTEOMICS · doi:10.1002/pmic.201400235 · Cited by 26 · see citing works

Targeted deletion of the AAA-ATPase Ruvbl1 in mice disrupts ciliary integrity and causes renal disease and hydrocephalus

Dafinger, C., Rinschen, M. M., Borgal, L., Ehrenberg, C., Basten, S. G., Franke, M., Höhne, M., Rauh, M., Göbel, H., Bloch, W., et al. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0108-z · Cited by 26 · see citing works

A protein-RNA interaction atlas of the ribosome biogenesis factor AATF

Kaiser, R. W. J., Ignarski, M., Nostrand, E. L. V., Frese, C. K., Jain, M., Cukoski, S., Heinen, H., Schaechter, M., Seufert, L., Bunte, K., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-47552-3 · Cited by 25 · see citing works

Proteomic analysis of the kidney filtration barrier—Problems and perspectives

Rinschen, M. M., Benzing, T. R., Limbutara, K., & Pisitkun, T. (2015) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400201 · Cited by 22 · see citing works

Molecular mechanisms underlying TGF-ß/Hippo signaling crosstalks – Role of baso-apical epithelial cell polarity

Mimoun, S. B., & Mauviel, A. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.03.006 · Cited by 21 · see citing works

YAP/TAZ affects the development of pulmonary fibrosis by regulating multiple signaling pathways

Zhu, T., Ma, Z., Wang, H., Jia, X., Wu, Y., Fu, L., Li, Z., Zhang, C., & Yu, G. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03866-9 · Cited by 20 · see citing works

Protein half‐life determines expression of proteostatic networks in podocyte differentiation

Schroeter, C. B., Koehler, S., Kann, M., Schermer, B., Benzing, T. R., Brinkkoetter, P. T., & Rinschen, M. M. (2018) · The FASEB Journal · doi:10.1096/fj.201701307r · Cited by 18 · see citing works

Experimental Models to Study Podocyte Biology: Stock-Taking the Toolbox of Glomerular Research

Hagmann, H., & Brinkkoetter, P. T. (2018) · Frontiers in Pediatrics · doi:10.3389/fped.2018.00193 · Cited by 19 · see citing works

Increased expression of the tight junction protein TJP1/ZO-1 is associated with upregulation of TAZ-TEAD activity and an adult tissue stem cell signature in carfilzomib-resistant multiple myeloma cells and high-risk multiple myeloma patients

Riz, I., & Hawley, R. G. (2017) · Oncoscience · doi:10.18632/oncoscience.356 · Cited by 18 · see citing works

Effect of TEAD4 on multilineage differentiation of muscle-derived stem cells.

Wang, J., Zhang, F., Yang, H., Wu, H., Cui, R., Zhao, Y., Jiao, C., Wang, X., Liu, X., LiQiong, W., et al. (2018) · PubMed Central · Cited by 16 · see citing works

Yap/Taz are required for establishing the cerebellar radial glia scaffold and proper foliation

Hughes, L. J., Park, R., Lee, M. J., Terry, B. K., Lee, D., Kim, H., Cho, S., & Kim, S. (2019) · Developmental Biology · doi:10.1016/j.ydbio.2019.10.002 · Cited by 15 · see citing works

Transformation by Polyomavirus Middle T Antigen Involves a Unique Bimodal Interaction with the Hippo Effector YAP

Rouleau, C., Pores‐Fernando, A. T., Hwang, J. H., Faure, N., Jiang, T., White, E. A., Roberts, T. M., & Schaffhausen, B. S. (2016) · Journal of Virology · doi:10.1128/jvi.00417-16 · Cited by 15 · see citing works

Substrate stiffness promotes vascular smooth muscle cell calcification by reducing the levels of nuclear actin monomers

McNeill, M. C., Chee, F. L. M., Ebrahimighaei, R., Sala‐Newby, G. B., Newby, A. C., Hathway, T., Annaiah, A. S., Joseph, S., Carrabba, M., & Bond, M. (2024) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2023.12.005 · Cited by 14 · see citing works

Jade-1S phosphorylation induced by CK1α contributes to cell cycle progression

Borgal, L., Rinschen, M. M., Dafinger, C., Liebrecht, V. I., Abken, H., Benzing, T. R., & Schermer, B. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1152429 · Cited by 14 · see citing works

Hippo Signaling in Mitosis: An Updated View in Light of the MEN Pathway

Hergovich, A. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6502-1_19 · Cited by 14 · see citing works

In vivo Polycystin-1 interactome using a novel Pkd1 knock-in mouse model

Lin, C.-C., Menezes, L. F., Qiu, J., Pearson, E. A., Zhou, F., Ishimoto, Y., Anderson, D. E., & Germino, G. G. (2023) · PLoS ONE · doi:10.1371/journal.pone.0289778 · Cited by 12 · see citing works

Functional proteomics of cellular mechanosensing mechanisms

Wasik, A. A., & Schiller, H. B. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.06.019 · Cited by 12 · see citing works

PALS1 is a key regulator of the lateral distribution of tight junction proteins in renal epithelial cells

Groh, A.-C., Möller‐Kerutt, A., Gilhaus, K., Höffken, V., Nedvetsky, P. I., Kleimann, S., Behrens, M., Ghosh, S., Hansen, U. J., Krahn, M. P., et al. (2024) · Journal of Cell Science · doi:10.1242/jcs.261303 · Cited by 10 · see citing works

Expression‐level dependent perturbation of cell proteostasis and nuclear morphology by aggregation‐prone polyglutamine proteins

Lü, M., Williamson, N. R., Boschetti, C., Ellis, T., Yoshimi, T., & Tunnacliffe, A. (2015) · Biotechnology and Bioengineering · doi:10.1002/bit.25606 · Cited by 10 · see citing works

Considerations for Identifying Endogenous Protein Complexes from Tissue via Immunoaffinity Purification and Quantitative Mass Spectrometry

Federspiel, J. D., & Cristea, I. M. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9232-4_9 · Cited by 10 · see citing works

Cbfβ: A key regulator in skeletal stem cell differentiation, bone development, and disease

Zheng, C., Zhang, C., He, Y., Lin, S., Zhu, Z., Wang, H., & Chen, G. (2025) · The FASEB Journal · doi:10.1096/fj.202500030r · Cited by 9 · see citing works

TEAD-Independent Cell Growth of Hippo-Inactive Mesothelioma Cells: Unveiling Resistance to TEAD Inhibitor K-975 through MYC Signaling Activation

Akao, K., Sato, T., Mishiro‐Sato, E., Mukai, S., Ghani, F. I., Kondo‐Ida, L., Imaizumi, K., & Sekido, Y. (2024) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-24-0308 · Cited by 8 · see citing works

Glucocorticoids activate Yes-associated protein in human vocal fold fibroblasts

Nakamura, R., Bing, R., Doyle, C. P., Garabedian, M. J., & Branski, R. C. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112681 · Cited by 8 · see citing works

Drosophila melanogaster and its nephrocytes: A versatile model for glomerular research

Odenthal, J., & Brinkkoetter, P. T. (2019) · Methods in cell biology · doi:10.1016/bs.mcb.2019.03.011 · Cited by 8 · see citing works

Restoration of atypical protein kinase C ζ function in autosomal dominant polycystic kidney disease ameliorates disease progression

Akbari, M., West, J. D., Doerr, N., Kipp, K. R., Marhamati, N., Vuong, S., Wang, Y., Rinschen, M. M., Talbot, J. J., Wessely, O., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2121267119 · Cited by 7 · see citing works

Proline‐dependent and basophilic kinases phosphorylate human TRPC6 at serine 14 to control channel activity through increased membrane expression

Hagmann, H., Mangold, N., Rinschen, M. M., König, T., Kunzelmann, K., Schermer, B., Benzing, T. R., & Brinkkoetter, P. T. (2017) · The FASEB Journal · doi:10.1096/fj.201700309r · Cited by 7 · see citing works

Evaluation of Quantification and Normalization Strategies for Phosphoprotein Phosphatase Affinity Proteomics: Application to Breast Cancer Signaling

Brauer, B. L., Wiredu, K., Gerber, S. A., & Kettenbach, A. N. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00465 · Cited by 1 · see citing works

Effect of TEA domain transcription factor 1 ( TEAD1 ) on the differentiation of intramuscular preadipocytes in goats

Liu, K., Zheng, J., Wang, Y., Li, Y., Xiong, Y., Wang, Y., Cheng, J., Huang, X., Zhang, L.-Y., & Lin, Y. (2023) · Animal Biotechnology · doi:10.1080/10495398.2023.2178932 · Cited by 1 · see citing works

TAZ interactome analysis using nanotrap-based affinity purification–mass spectrometry

Kelebeev, J., MacKeracher, A., Miyake, T., & McDermott, J. C. (2025) · Journal of Cell Science · doi:10.1242/jcs.263527 · Cited by 1 · see citing works

Letter to the editor: “Systems biology versus reductionism in cell physiology”

Knepper, M. A., Raghuram, V., Bradford, D., Chou, C., Hoffert, J. D., & Pisitkun, T. (2014) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00175.2014 · Cited by 1 · see citing works

Implicación de Caveolina-1 en procesos de mecanotransducción: modulación de la respuesta a cambios en la rigidez de la matriz extracelular a través del control de la actividad

Moreno-Vicente, R. (2018) · doi:10.4321/repisalud.6731

Extracellular Matrix Stiffness Promotes Vascular Smooth Muscle Cell Calcification By Reducing The Levels Of Nuclear Actin MonomersPreprint

McNeill, M. C., Chee, F. L. M., Ebrahimighaei, R., Sala‐Newby, G. B., Newby, A. C., Hathway, T., Annaiah, A. S., Joseph, S., Carrabba, M., & Bond, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.18.545506

A YAP–TEAD4–CTCF transcriptional regulatory axis associated with the elimination of injured hepatocytes from the liverPreprint

Hatakeyama, D., Okamoto‐Uchida, Y., Kosaka, M., Hirose, H., Kofuji, S., Kanayama, K., Endo, Y., Nakagawa, M., Kanai, A., Suzuki, Y., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9490879/v1

A YAP – TEAD – CTCF Transcriptional Regulatory Axis Associated With the Elimination of Injured Hepatocytes From the Liver

Hatakeyama, D., Okamoto‐Uchida, Y., Kosaka, M., Hirose, H., Kofuji, S., Danzaki, K., Endo, Y., Nakagawa, M., Kanai, A., Suzuki, Y., et al. (2026) · Genes to Cells · doi:10.1111/gtc.70150

TAZ interactome analysis using nanotrap-based affinity purification–mass spectrometry

Kelebeev, J., MacKeracher, A., Miyake, T., & McDermott, J. C. (2025) · Journal of Cell Science · doi:10.1242/jcs.263527 · Cited by 1 · see citing works

SEAMing Proteins from the TAP: Charting Protein InteractionNetworks in Yeast by Tandem Affinity Purification and MassSpectrometry

Shevchenko, A., Schaft, D., Roguev, A., Pijnappel, W. W. M. P., Havliš, J., Stewart, F., & Shevchenko, A. (2002)

Tandem affinity purification technique: an extraordinary valuable tool for purifying protein complexes

Xiaozhong, P. (2006) · Basic & Clinical Medicine

Deciphering Protein Complexes and Protein Interaction Networks by Tandem Affinity Purification and Mass Spectrometry

Shevchenko, A., Schaft, D., Roguev, A., Pijnappel, W. W. M. P., Stewart, A. F., & Shevchenko, A. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200005-mcp200 · Cited by 69 · see citing works

An Integrated Mass Spectrometry-based Proteomic Approach

Guerrero, C., Tagwerker, C., Kaiser, P., & Huang, L. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500303-mcp200 · Cited by 258 · see citing works