Misfolded proteins partition between two distinct quality control compartments

Protein Misfolding, Functional Amyloid, and Human Disease

Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497

Methods in Yeast Genetics

Jacob, H. (1988) · Bioelectrochemistry and Bioenergetics · doi:10.1016/0302-4598(88)80052-7 · Cited by 4,911

Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein

Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N. G., Palmer, A. E., & Tsien, R. Y. (2004) · Nature Biotechnology · doi:10.1038/nbt1037 · Cited by 4,619

p62/SQSTM1 Binds Directly to Atg8/LC3 to Facilitate Degradation of Ubiquitinated Protein Aggregates by Autophagy

Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578

Functional Characterization of the S. cerevisiae Genome by Gene Deletion and Parallel Analysis

Winzeler, E. A., Shoemaker, D. D., Astromoff, A., Liang, H., Anderson, K., Andre, B., Bangham, R., Benito, R., Boeke, J. D., Bussey, H., et al. (1999) · Science · doi:10.1126/science.285.5429.901 · Cited by 3,953

Adapting Proteostasis for Disease Intervention

Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,209

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979

The effect of yeast Saccharomyces cerevisiae red pigment on the expression of cloned human α-synuclein

Nevzglyadova, O. V., Artemov, A. V., Mikhailova, E. V., Lyublinskaya, O. G., Ozerova, Y. E., Ivanova, P. A., Kostyleva, E. I., & Soidla, T. R. (2016) · Cell and Tissue Biology · doi:10.1134/s1990519x16040106 · Cited by 1

The generation of detergent-insoluble clipped fragments from an ERAD substrate in mammalian cells

Daskivich, G. J., & Brodsky, J. L. (2023) · Scientific Reports · doi:10.1038/s41598-023-48769-z · Cited by 1

Protein aggregation in neurodegenerative disease: the nucleolar connection

Latonen, L. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.3.324 · Cited by 1

ER-associated Degradation and Its Involvement in Human Disease: Insights from Yeast

Campagnolo, N., & Ghislain, M. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_14 · Cited by 1

ATP-Dependent Proteases: The Cell's Degradation Machines

Bhattacharyya, S., Wilmington, S. R., & Matouschek, A. T. (2011) · Cambridge University Press eBooks · doi:10.1017/cbo9781139003704.014 · Cited by 1

The VHL short variant involves in protein quality control

Liu, Y., Yang, H., Zuo, F., & Chen, L. (2016) · Gene · doi:10.1016/j.gene.2016.05.027 · Cited by 1

A Budding Topic

Smith, J. T., & Schneider, B. L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811353-0.00029-4 · Cited by 1

Response and Cytoprotective Mechanisms Against Proteotoxic Stress in Yeast and Fungi

Kimata, Y., Nguyen, T. M. P., & Kohno, K. (2018) · Springer eBooks · doi:10.1007/978-3-030-00683-9_5 · Cited by 1

Proteome-scale studies of protein stability

Calloni, G., & Vabulas, R. M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819132-3.00004-x · Cited by 1

Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit

Yakubu, U. M., Catumbela, C. S. G., Morales, R., & Morano, K. A. (2020) · Open Biology · doi:10.1098/rsob.200282 · Cited by 1

Overview of Autophagy

Hayat, M. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-805421-5.00001-x · Cited by 1

Components and mechanisms of cytoplasmic protein quality control and elimination of regulatory enzymes

Eisele, F. (2011) · OPUS Publication Server of the University of Stuttgart (University of Stuttgart) · doi:10.18419/opus-1338 · Cited by 1

The interplay between Lewy body-like alpha-synuclein aggregates and protein degradation pathways in a cell-based model of Parkinson's disease

Tanik, S. A. (2013) · Scholarly Commons (University of Pennsylvania) · Cited by 1

High‐Resolution 4 D Imaging in Live Cells

Shamir, M., & Kaganovich, D. (2013) · Wiley eBooks · doi:10.1002/9780470027318.a9326 · Cited by 1

Characterisation of SerpinB2 as a stress response modulator

Lee, J. A. (2015) · Research Online (University of Wollongong) · Cited by 1

Autophagy Gene Overexpression in Saccharomyces cerevisiae for Accelerated Sparkling Wine Production

Preiss, R. (2017) · The Atrium (University of Guelph) · Cited by 1

Functional characterization of the Arabidopsis HSP70-HSP90 organizing protein (HOP) family in response to stress

Fernández‐Bautista, N. (2017) · doi:10.20868/upm.thesis.48105 · Cited by 1

Mechanisms of Aggresome Biogenesis Ubiquitination, Transport, & MaintenancePreprint

Keefe, A. (2018) · Preprints.org · doi:10.20944/preprints201812.0332.v1 · Cited by 1

Reconstitution of retrotranslocation by the Hrd1 ubiquitin ligase with purified components

Vasic, V. (2020) · doi:10.53846/goediss-7915 · Cited by 1

Super-resolution microscopy informs on the molecular architecture of alpha-synuclein inclusions in model systems and in the human brainPreprint

Weish, P., Lázaro, D. F., Palmares, L. M. M., Santos, P. I., Stadelmann, C., Höglinger, G. U., Rizzoli, S. O., & Outeiro, T. F. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.25.441304 · Cited by 1

Clearance of protein aggregates during cell divisionPreprint

Du, S., Wang, Y., Chen, B., Xie, S., Chan, K. Y., Hay, D. C., & Chew, T. G. (2024) · eLife · doi:10.7554/elife.96675.1 · Cited by 1

A dynamic redox switch turns TRC40 into a chaperone protecting human cells against ATP-depleting, oxidative stressPreprint

Dempsey, B., Dubrall, R., Chan, O., Lapacz, K. J., Riemer, J., Jakob, U., & Ulrich, K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.10.602939 · Cited by 1

Fitness defects due to cytosolic protein misfolding in S. cerevisiae can be alleviated by decreasing mitochondrial protein import capacityPreprint

Zaidi, Z., Dash, D. P., Sharma, A., Kundu, S., Bhatt, S., Rao, S., Padia, K., Rai, M., & Chakraborty, K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.26.609637 · Cited by 1

Clearance of protein aggregates during cell divisionPreprint

Du, S., Wang, Y., Chen, B., Xie, S., Chan, K. Y., Hay, D. C., & Chew, T. G. (2025) · eLife · doi:10.7554/elife.96675.2 · Cited by 1

Molecular Chaperones as Facilitators of Protein Degradation

Höhfeld, J., Dick, N., & Arndt, V. (2010) · Springer eBooks · doi:10.1007/978-1-4419-7061-9_3

Protein Aggregation in Unicellular Eukaryotes

Caldara, M., Winderickx, J., & Franssens, V. (2014) · Wiley eBooks · doi:10.1002/9781118845363.ch5

Redox Regulation of Protein Misfolding, Synaptic Damage, and Neuronal Loss in Neurodegenerative Diseases

Nakamura, T., & Lipton, S. A. (2011) · Wiley eBooks · doi:10.1002/9781118063903.ch2

The proteasome activator Blm10 facilitates nuclear import of mature proteasome core particles in yeast

Weberruss, M. H. (2014) · OPUS Publication Server of the University of Stuttgart (University of Stuttgart) · doi:10.18419/opus-1417

Localization and Mutational Analysis of the Nuclear and Aggregation-Prone Ime4 Protein in Saccharomyces cerevisiae

Mott, P. D. (2012) · ScholarWorks @ The University of New Orleans (The University of New Orleans)

Role of members of the phosducin gene family in protein translation and folding

Sono‐Koree, N. K. (2010) · ScholarsArchive (Brigham Young University)

Search for selection pressures associated with aggregation propensity following whole genome duplication in S.cerevisiae.

Wittig, M. (2011) · Texas ScholarWorks (Texas Digital Library)

Mutant Superoxide Dismutase-1-caused pathogenesis in Amyotrophic Lateral Sclerosis

Bergemalm, D. (2010) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Damage Segregation and Cellular Rejuvenation in Saccharomyces cerevisiae

Hill, S. M. (2015)

The dynamic role of Hsp40 chaperones in protein aggregation and proteotoxicity

Douglas, P. M. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/1rfy-jm42

Neziskové léky: Aktivita komplexu disulfiramu (antabusu) s mědí proti buněčné linii odvozené od osteosarkomu

Daněk, P. (2013)

Physiological and Environmental Regulation of Amyloid and Prion Formation

Chernova, T. A. (2012) · Journal of Physiobiochemical Metabolism · doi:10.4172/2324-8793.1000e103

Regulation of Hsp70 function by nucleotide-exchange factors

Gowda, N. K. C. (2016) · KTH Publication Database DiVA (KTH Royal Institute of Technology)

Parkin Misfolding, Dysfunction, and Degradation in Parkinson's Disease

McCarton, A. S. (2016) · Scholarship@Western (Western University)

Aggregation-promoting factors in neurodegenerative diseases

Sin, O. (2016)

Autophagy-linked FYVE protein mediates the turnover of mutant huntingtin and modifies pathogenesis in mouse models of Huntington’s disease

Fox, L. M. (2016) · doi:10.7916/d83b60cm

Exosomes in the Preservation of Cellular Homeostasis

Baixauli, F., & Mittelbrunn, M. (2016) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-319-33486-8_2

The Role of the Hsp40 Chaperone Sis1 in Yeast Prion Propagation

Reidy, M. J. (2017) · InTech eBooks · doi:10.5772/66449

Review of cardiac protein quality control and major degradation pathways

Osalusi, B. S. (2017) · International Journal of Medicine and Medical Sciences · doi:10.5897/ijmms2014.1056

Estudo dos efeitos da superexpressão da alfa-sinucleína sobre o tráfego mitocondrial e autofagia em leveduras, células SH-SY5Y e neurônios dopaminérgicos derivados de hiPSC de pacientes com doença de Parkinson

Melo, T. Q. (2017) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2017.tde-01032017-131637

Factors that Contribute to de novo Protein Misfolding and Prion Formation in Saccharomyces cerevisiae

Keefer, K. M. (2017) · Open Scholarship Institutional Repository (Washington University in St. Louis) · doi:10.7936/k7416vgq

Assembly and Disassembly of Protein Aggregates

Seneci, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800186-8.00006-7

Molecular mechanisms underlying selective clearance of protein aggregates and mitochondria by autophagy

Tan, S. (2017) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/72655

Substrate recognition and processing by the 26S proteasome

Bashore, C. (2015) · eScholarship (California Digital Library)

The Role of Ubiquitin on Yeast Proteasome Dynamics in Quiescence

Wu, E. S. C. (2013) · TSpace (University of Toronto)

Translational control in nutrient response and aging

Harris, M. S. (2016)

Investigation into the molecular complexity of Alzheimer's disease : an amyloid-β centered approach

Cioffi, F. (2019) · doi:10.3990/1.9789036548410

Oosit in vitro maturasyonunda fosfatidilinositol 4,5- bifosfat (PIP2) kullanımının etkisi

Tepeköy, F. (2020) · Sakarya Medical Journal · doi:10.31832/smj.728050

Dynamics of Ubiquitin-Conjugate Population in Response to Inhibition of Ubiquitin-Proteasome Pathway

Minissale, J. (2018) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)

On chaperone co-operation in temporal and spatial protein quality control

Andersson, R. (2021) · Gothenburg University Publications Electronic Archive (Gothenburg University)

AgDD System: A Chemical Controllable Protein Aggregates in Cells

Miyazaki, Y. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1441-9_16

Metabolic strategies for enabling microbial-based green chemistry solutions

Latimer, L. N. (2017) · eScholarship (California Digital Library)

Programming supramolecular peptide materials for immunological applications

Lau, C. Y. J. (2021) · doi:10.33540/604

Proteostasis beyond chaperones - Auxiliary systems in the management of damaged proteins

Josefson, R. (2021) · Gothenburg University Publications Electronic Archive (Gothenburg University)

Insights into the function and dysfunction of α-synuclein in cells

Raiss, C. C. (2015) · University of Twente Research Information · doi:10.3990/1.9789461089458

Delivery and Removal: Probing cargo sorting and degradation using inducible tools

Janssen, A. F. J. (2019) · Utrecht University Repository (Utrecht University) · doi:10.33540/925

Exploring the human Hsp70-Hop-Hsp90 system for Tau recognition

Moll, A. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9131

A felgyorsult fehérje körforgás szerepe a transzlációs hibákkal szembeni alkalmazkodási folyamatokban

Kalapis, D. (2017) · doi:10.14232/phd.3941

Faculty Opinions recommendation of p62 links the autophagy pathway and the ubiqutin-proteasome system upon ubiquitinated protein degradation.

Lipton, S. A. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.727653084.793538935

Sequence Grammar Underlying Unfolding and Phase Separation of Globular ProteinsPreprint

Ruff, K. M., Choi, Y. H., Cox, D., Ormsby, A. R., Myung, Y., Ascher, D. B., Radford, S. E., Pappu, R. V., & Hatters, D. M. (2021) · SSRN Electronic Journal · doi:10.2139/ssrn.3929009

Faculty Opinions recommendation of Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans.

David, D. C. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.717968823.793468464

Faculty Opinions recommendation of A novel single-cell screening platform reveals proteome plasticity during yeast stress responses.

Bähler, J., & Rallis, C. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.717990445.793473399

Faculty Opinions recommendation of Substrate Insolubility Dictates Hsp104-Dependent Endoplasmic-Reticulum-Associated Degradation.

Römisch, K. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733072366.793545528

Mechanisms of Aggresome Biogenesis: Ubiquitination, Transport, & MaintenancePreprint

Keefe, A. (2019) · Preprints.org · doi:10.20944/preprints201812.0332.v2

Molecular and clinical determinants of pathogenic protein aggregation

de Mattos, E. P. (2022) · University of Groningen research database (University of Groningen / Centre for Information Technology) · doi:10.33612/diss.220760500

Liquid–liquid phase separation and biomolecular condensates in cell quiescence

Uversky, V. N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-823967-4.00001-4

Cyclic AMP (cAMP)-dependent proteolysis of GATA6 by proteasome: Zinc-finger domain of GATA6 has signals for nuclear export and proteolysis, both of which are responsive to cAMP

Yamamoto, T., Tsuge, T., Araki, M., & Maeda, M. (2023) · Drug Discoveries & Therapeutics · doi:10.5582/ddt.2022.01107

Cell identification and phenotyping using classical machine learning and deep learning

Balassa, T. (2022) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2021.207

Introduction: Molecular Chaperones and Protein Quality Control

Balchin, D., Rangel, M. A., & Samant, R. S. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781839165986-00001

Adaptation to ER Stress by Slt2, Counterpart of Human MAP Kinase ERK1/2, via Enhancing Splicing and Translation of HAC1 mRNA in Saccharomyces cerevisiaePreprint

Uppala, J. K., Chakraborty, A., George, J., Mayer, K. A., Ghosh, C., Dey, R., Chaluvally–Raghavan, P., & Dey, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.19.567283

Reviewer #2 (Public Review): Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipids

(2023) · eLife · doi:10.7554/elife.92180.1.sa0

Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipidsPreprint

Cao, X., Wu, X., Zhao, L., Zheng, J., Jin, X., Hao, X., Winderickx, J., Liu, S., Chen, L., & Liu, B. (2023) · eLife · doi:10.7554/elife.92180

Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipidsPreprint

Cao, X., Wu, X., Zhao, L., Zheng, J., Jin, X., Hao, X., Winderickx, J., Liu, S., Chen, L., & Liu, B. (2023) · eLife · doi:10.7554/elife.92180.1

Get3 in Arabidopsis

Bodensohn, U. (2021) · doi:10.21248/gups.65190

Cellular Senescence

Lynch, M. (2024) · Oxford University Press eBooks · doi:10.1093/oso/9780192847287.003.0011

The proteasome interactome and its role in the mechanisms of brain plasticity

Бунеева, О. А., Kopylov, A. T., & Medvedev, A. E. (2023) · Biochemistry (Moscow) · doi:10.31857/s032097252303003x

eLife Assessment: Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipids

Mapa, K. (2024) · eLife · doi:10.7554/elife.92180.2.sa3

Reviewer #2 (Public Review): Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipids

Cao, X., Wu, X., Zhao, L., et al. (2024) · eLife · doi:10.7554/elife.92180.2.sa1

Reviewer #1 (Public Review): Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipids

Cao, X., Wu, X., Zhao, L., et al. (2024) · eLife · doi:10.7554/elife.92180.2.sa2

Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipidsPreprint

Cao, X., Wu, X., Zhao, L., Zheng, J., Jin, X., Hao, X., Winderickx, J., Liu, S., Chen, L., & Liu, B. (2024) · eLife · doi:10.7554/elife.92180.2

Author response: Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipids

Cao, X., Wu, X., Zhao, L., Zheng, J., Jin, X., Hao, X., Winderickx, J., Liu, S., Chen, L., & Liu, B. (2024) · eLife · doi:10.7554/elife.92180.2.sa0

The phase separation landscape of genome-wide genetic perturbationsPreprint

Heidenreich, M., Mathur, S., Shu, T., Xie, Y., Sriker, D., Dubreuil, B., Holt, L. J., & Levy, E. D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.25.620319

Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipidsPreprint

Cao, X., Wu, X., Zhao, L., Zheng, J., Jin, X., Hao, X., Winderickx, J., Liu, S., Chen, L., & Liu, B. (2025) · eLife · doi:10.7554/elife.92180.3

Author response: Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipids

Cao, X., Wu, X., Zhao, L., Zheng, J., Jin, X., Hao, X., Winderickx, J., Liu, S., Chen, L., & Liu, B. (2025) · eLife · doi:10.7554/elife.92180.3.sa0

Clearance of protein aggregates during cell divisionPreprint

Du, S., Wang, Y., Chen, B., Xie, S., Chan, K. Y., Hay, D. C., & Chew, T. G. (2025) · eLife · doi:10.7554/elife.96675.3

Cell membrane asymmetries and cellular aging

Salzman, V., & Aguilar, P. S. (2025) · Biochemical Journal · doi:10.1042/bcj20253265

Application of brain organoids in Huntington's disease

Gnanarajan, R., Ravichandran, N., Karuppusamy, P. A., Uvarajan, D., & Narayanasamy, A. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29898-1.00001-0

Modeling liquid-liquid phase separation and its impact on proteasomal substrate degradation

Wu, D., Ouyang, Q., & Wang, H. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.11.029

Molecular chaperones mediated proteostasis depletion: A cause of neurodegeneration?

Kinger, S., Choudhary, A., Kumar, P., Jagtap, Y. A., Sharma, V., Dhiman, R., Prasad, A., Verma, R., Chinnathambi, S., & Mishra, A. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.033

In silico studies on potential binding sites of amyloid inhibitor compounds on amyloid beta peptide

Rudra, S. (2012)

Estudi del metabolisme del glicogen en la funció neuronal i la seva implicació en la malaltia de Lafora i l’envelliment

Ortega, J. V. (2012) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

On aging and the role of Ubp3 in heterochromatic gene silencing and protein quality control

Öling, D. (2014) · Gothenburg University Publications Electronic Archive (Gothenburg University)

A Cdc48p cofactor affects ubiquitinated protein levels, endoplasmic reticulum associated degradation and proteasome subtypes

Tran, J. R. (2012) · D-Scholarship@Pitt (University of Pittsburgh)

Spatial organization of ER-derived protein aggregates in the nucleus requires the Hsp70-family member BiP

Du, S., Wang, Y., & Chew, T. G. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.153406

Differential inclusion formation of an aggregation-prone protein reveals differences in the proteostasis capacity of neuronal cell lines

McMahon, S., Cox, D., Cheng, F., Lee, A., Yerbury, J. J., & Ecroyd, H. W. (2026) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2026.120124

L'alpha-tubuline B et ses régulateurs chez le champignon Botrytis cinerea : régulation, rôles et interactants

Talmey, Y. F. (2014) · theses.fr (ABES) · doi:10.70675/19614ee5zadd0z4838z930cz4ac6a7f7afc4

Molecular Origami: Protein folding and misfolding in health and disease

Frydman, J. (2009) · The FASEB Journal · doi:10.1096/fasebj.23.1_supplement.195.3

Compartment‐specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition

Miller, S. B. M., Ho, C., Winkler, J., Khokhrina, M., Neuner, A., Mohamed, M. Y. H., Guilbride, D. L., Richter, K., Lisby, M., Schiebel, E., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201489524 · Cited by 278

4D Imaging of Protein Aggregation in Live Cells

Spokoini, R., Shamir, M., Keness, A., & Kaganovich, D. (2013) · Journal of Visualized Experiments · doi:10.3791/50083-v

Distinct proteostasis circuits cooperate in nuclear and cytoplasmic protein quality control

Samant, R. S., Livingston, C. M., Sontag, E. M., & Frydman, J. (2018) · Nature · doi:10.1038/s41586-018-0678-x · Cited by 172

Mechanisms and Functions of Spatial Protein Quality Control

Sontag, E. M., Samant, R. S., & Frydman, J. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014616 · Cited by 276