Small heat shock protein HSPB8 interacts with a pre-fibrillar TDP43 low complexity domain species to delay fibril formation

Highly accurate protein structure prediction with AlphaFold

Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · see citing works

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · see citing works

Phase Separation by Low Complexity Domains Promotes Stress Granule Assembly and Drives Pathological Fibrillization

Molliex, A., Temirov, J. P., Lee, J., Coughlin, M., Kanagaraj, A., Kim, H. J., Mittag, T., & Taylor, J. P. (2015) · Cell · doi:10.1016/j.cell.2015.09.015 · Cited by 2,658 · see citing works

Principles and Properties of Stress Granules

Protter, D. S. W., & Parker, R. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.05.004 · Cited by 1,738 · see citing works

Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report

Nelson, P. T., Dickson, D. W., Trojanowski, J. Q., Jack, C. R., Boyle, P. A., Arfanakis, K., Rademakers, R., Alafuzoff, I., Attems, J., Brayne, C., et al. (2019) · Brain · doi:10.1093/brain/awz099 · Cited by 1,547 · see citing works

TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia

Mackenzie, I. R., Rademakers, R., & Neumann, M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70195-2 · Cited by 977 · see citing works

Misfolded proteins partition between two distinct quality control compartments

Kaganovich, D., Kopito, R., & Frydman, J. (2008) · Nature · doi:10.1038/nature07195 · Cited by 932 · see citing works

RNA-Induced Conformational Switching and Clustering of G3BP Drive Stress Granule Assembly by Condensation

Guillén‐Boixet, J., Kopach, A., Holehouse, A. S., Wittmann, S., Jahnel, M., Schlüßler, R., Kim, K., Trussina, I. R. E. A., Wang, J., Matějů, D., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.049 · Cited by 869 · see citing works

ALS Mutations Disrupt Phase Separation Mediated by α-Helical Structure in the TDP-43 Low-Complexity C-Terminal Domain

Conicella, A. E., Zerze, G. H., Mittal, J., & Fawzi, N. L. (2016) · Structure · doi:10.1016/j.str.2016.07.007 · Cited by 860 · see citing works

Distinct stages in stress granule assembly and disassembly

Wheeler, J., Matheny, T., Jain, S., Abrisch, R. G., & Parker, R. (2016) · eLife · doi:10.7554/elife.18413 · Cited by 806 · see citing works

Stress granules and neurodegeneration

Wolozin, B. L., & Ivanov, P. V. (2019) · Nature reviews. Neuroscience · doi:10.1038/s41583-019-0222-5 · Cited by 782 · see citing works

Competing Protein-RNA Interaction Networks Control Multiphase Intracellular Organization

Sanders, D. W., Kedersha, N., Lee, D. S. W., Strom, A. R., Drake, V., Riback, J. A., Bracha, D., Eeftens, J. M., Iwanicki, A. G., Wang, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.050 · Cited by 779 · see citing works

Overcoming Expression and Purification Problems of RhoGDI Using a Family of “Parallel” Expression Vectors

Sheffield, P., Garrard, S. M., & Derewenda, Z. S. (1999) · Protein Expression and Purification · doi:10.1006/prep.1998.1003 · Cited by 639 · see citing works

Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy

Evgrafov, O. V., Mersiyanova, I., Irobi, J., Bosch, L. V. D., Dierick, I., Leung, C. L., Shchagina, O., Verpoorten, N., Impe, K. V., Fedotov, V. P., et al. (2004) · Nature Genetics · doi:10.1038/ng1354 · Cited by 581 · see citing works

A high-speed search engine pLink 2 with systematic evaluation for proteome-scale identification of cross-linked peptides

Chen, Z.-L., Meng, J., Cao, Y., Yin, J., Fang, R.-Q., Fan, S., Liu, C., Zeng, W., Ding, Y., Tan, D., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11337-z · Cited by 526 · see citing works

A guide to membraneless organelles and their various roles in gene regulation

Hirose, T., Ninomiya, K., Nakagawa, S., & Yamazaki, T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00558-8 · Cited by 496 · see citing works

An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function

Matějů, D., Franzmann, T. M., Patel, A., Kopach, A., Boczek, E. E., Maharana, S., Lee, H. O., Carra, S., Hyman, A. A., & Alberti, S. (2017) · The EMBO Journal · doi:10.15252/embj.201695957 · Cited by 480 · see citing works

ThT 101: a primer on the use of thioflavin T to investigate amyloid formation

Malmos, K. G., Blancas‐Mejía, L. M., Weber, B., Büchner, J., Ramı́rez-Alvarado, M., Naiki, H., & Otzen, D. E. (2017) · Amyloid · doi:10.1080/13506129.2017.1304905 · Cited by 453 · see citing works

Hot-spot residue in small heat-shock protein 22 causes distal motor neuropathy

Irobi, J., Impe, K. V., Seeman, P., Jordanova, A., Dierick, I., Verpoorten, N., Michalik, A., Vriendt, E. D., Jacobs, A., Gerwen, V. V., et al. (2004) · Nature Genetics · doi:10.1038/ng1328 · Cited by 417 · see citing works

Mechanistic View of hnRNPA2 Low-Complexity Domain Structure, Interactions, and Phase Separation Altered by Mutation and Arginine Methylation

Ryan, V. H., Dignon, G. L., Zerze, G. H., Chabata, C. V., Silva, R., Conicella, A. E., Amaya, J., Burke, K. A., Mittal, J., & Fawzi, N. L. (2018) · Molecular Cell · doi:10.1016/j.molcel.2017.12.022 · Cited by 417 · see citing works

The role of liquid–liquid phase separation in aggregation of the TDP-43 low-complexity domain

Babinchak, W. M., Haider, R., Dumm, B. K., Sarkar, P., Surewicz, K. A., Choi, J.-K., & Surewicz, W. K. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007222 · Cited by 400 · see citing works

TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1

McDonald, K. K., Aulas, A., Destroismaisons, L., Pickles, S. R., Beleac, E., Camu, W., Rouleau, G. A., & Velde, C. V. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr021 · Cited by 394 · see citing works

HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells

Yu, H., Lu, S., Gasior, K. I., Singh, D., Vazquez‐Sanchez, S., Tapia, O., Toprani, D., Beccari, M. S., Yates, J. R., Cruz, S. D., et al. (2021) · Science · doi:10.1126/science.abb4309 · Cited by 355 · see citing works

Translation inhibition and stress granules in the antiviral immune response

McCormick, C., & Khaperskyy, D. A. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.63 · Cited by 354 · see citing works

HspB8 Chaperone Activity toward Poly(Q)-containing Proteins Depends on Its Association with Bag3, a Stimulator of Macroautophagy

Carra, S., Seguin, S. J., Lambert, H., & Landry, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706304200 · Cited by 347 · see citing works

The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)

Crippa, V., Sau, D., Rusmini, P., Boncoraglio, A., Onesto, E., Bolzoni, E., Galbiati, M., Fontana, E., Marino, M., Carra, S., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq257 · Cited by 330 · see citing works

Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress

Escusa-Toret, S., Vonk, W. I. M., & Frydman, J. (2013) · Nature Cell Biology · doi:10.1038/ncb2838 · Cited by 321 · see citing works

A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism

Ganassi, M., Matějů, D., Bigi, I., Mediani, L., Poser, I., Lee, H. O., Seguin, S. J., Morelli, F. F., Vinet, J., Leo, G., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.07.021 · Cited by 312 · see citing works

Structure of pathological TDP-43 filaments from ALS with FTLD

Arseni, D., Hasegawa, M., Murzin, A. G., Kametani, F., Arai, M., Yoshida, M., & Falcon, B. (2021) · Nature · doi:10.1038/s41586-021-04199-3 · Cited by 303 · see citing works

How Hsp70 Molecular Machines Interact with Their Substrates to Mediate Diverse Physiological Functions

Clérico, E. M., Tilitsky, J. M., Meng, W., & Gierasch, L. M. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.02.004 · Cited by 299 · see citing works

xiNET: cross-link network maps with residue resolution

Combe, C. W., Fischer, L., & Rappsilber, J. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.042259 · Cited by 296 · see citing works

Crystal Structures of α-Crystallin Domain Dimers of αB-Crystallin and Hsp20

Bagnéris, C., Bateman, O. A., Naylor, C. E., Cronin, N., Boelens, W. C., Keep, N. H., & Slingsby, C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.069 · Cited by 271 · see citing works

Substrate binding site flexibility of the small heat shock protein molecular chaperones

Jaya, N., Garcia, V. G., & Vierling, E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902177106 · Cited by 241 · see citing works

Functional Significance of TDP-43 Mutations in Disease

Buratti, E. (2015) · Advances in genetics · doi:10.1016/bs.adgen.2015.07.001 · Cited by 225 · see citing works

N-terminal domain of αB-crystallin provides a conformational switch for multimerization and structural heterogeneity

Jehle, S., Vollmar, B. S., Bardiaux, B., Dove, K. K., Rajagopal, P., Gonen, T., Oschkinat, H., & Klevit, R. E. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014656108 · Cited by 210 · see citing works

Yeast Alcohol Dehydrogenase Structure and Catalysis

Raj, S. B., Ramaswamy, S., & Plapp, B. V. (2014) · Biochemistry · doi:10.1021/bi5006442 · Cited by 210 · see citing works

Identification of the key structural motifs involved in HspB8/HspB6–Bag3 interaction

Fuchs, M., Poirier, D. J., Seguin, S. J., Lambert, H., Carra, S., Charette, S. J., & Landry, J. (2010) · Biochemical Journal · doi:10.1042/bj20090907 · Cited by 190 · see citing works

The Pathobiology of TDP-43 C-Terminal Fragments in ALS and FTLD

Berning, B. A., & Walker, A. K. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00335 · Cited by 183 · see citing works

Interaction of the Molecular Chaperone DNAJB6 with Growing Amyloid-beta 42 (Aβ42) Aggregates Leads to Sub-stoichiometric Inhibition of Amyloid Formation

Månsson, C., Arosio, P., Hussein, R. M., Kampinga, H. H., Hashem, R. M., Boelens, W. C., Dobson, C. M., Knowles, T. P. J., Linse, S. S., & Emanuelsson, C. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595124 · Cited by 180 · see citing works

Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation

Liu, Z., Zhang, S., Gu, J., Tong, Y., Li, Y., Gui, X., Long, H., Wang, C., Zhao, C., Lu, J., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0399-3 · Cited by 171 · see citing works

HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells

Carra, S., Sivilotti, M., Chávez-Zobel, A. T., Lambert, H., & Landry, J. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi174 · Cited by 163 · see citing works

Heat-shock chaperone HSPB1 regulates cytoplasmic TDP-43 phase separation and liquid-to-gel transition

Lu, S., Hu, J., Arogundade, O. A., Goginashvili, A., Vazquez‐Sanchez, S., Diedrich, J. K., Gu, J., Blum, J. A., Oung, S., Ye, Q., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00988-8 · Cited by 163 · see citing works

TDP-43 regulation of stress granule dynamics in neurodegenerative disease-relevant cell types

Khalfallah, Y., Kuta, R., Grasmuck, C., Prat, A., Durham, H. D., & Velde, C. V. (2018) · Scientific Reports · doi:10.1038/s41598-018-25767-0 · Cited by 159 · see citing works

TDP-43 forms amyloid filaments with a distinct fold in type A FTLD-TDP

Arseni, D., Chen, R., Murzin, A. G., Peak‐Chew, S., Garringer, H. J., Newell, K. L., Kametani, F., Robinson, A., Vidal, R., Ghetti, B. F., et al. (2023) · Nature · doi:10.1038/s41586-023-06405-w · Cited by 159 · see citing works

Mechanisms of Small Heat Shock ProteinsPreprint

Janowska, M. K., Baughman, H. E. R., Woods, C. N., & Klevit, R. E. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a034025 · Cited by 157 · see citing works

Surface charge and hydrophobicity determine ErbB2 binding to the Hsp90 chaperone complex

Xu, W., Yuan, X., Xiang, Z., Mimnaugh, E. G., Marcu, M. G., & Neckers, L. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb885 · Cited by 152 · see citing works

Cryo-EM structure of amyloid fibrils formed by the entire low complexity domain of TDP-43

Li, Q., Babinchak, W. M., & Surewicz, W. K. (2021) · Nature Communications · doi:10.1038/s41467-021-21912-y · Cited by 152 · see citing works

The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client

Mainz, A., Peschek, J., Stavropoulou, M., Back, K. C., Bardiaux, B., Asami, S., Prade, E., Peters, C., Weinkauf, S., Büchner, J., et al. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3108 · Cited by 149 · see citing works

Effects of Site-directed Mutations on the Chaperone-like Activity of αB-Crystallin

Plater, M. L., Goode, D., & Crabbe, M. J. C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.45.28558 · Cited by 144 · see citing works

Human small heat shock proteins: Protein interactomes of homo‐ and hetero‐oligomeric complexes: An update

Arrigo, A. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.05.011 · Cited by 138 · see citing works

Identification of 1,1′-Bi(4-anilino)naphthalene-5,5′-disulfonic Acid Binding Sequences in α-Crystallin

Sharma, K. K., Kumar, G. S., Murphy, A. S., & Kester, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15474 · Cited by 129 · see citing works

Chaperone‐like activity and hydrophobicity of α‐crystallin

Reddy, G. B., Pasupulati, A. K., & Kumar, M. (2006) · IUBMB Life · doi:10.1080/15216540601010096 · Cited by 129 · see citing works

Coomassie Blue Staining

Brunelle, J. L., & Green, R. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-420119-4.00013-6 · Cited by 123 · see citing works

Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation

Cox, D., Selig, E. E., Griffin, M. D. W., Carver, J. A., & Ecroyd, H. W. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.739250 · Cited by 116 · see citing works

Three-Dimensional Structure of α-Crystallin Domain Dimers of Human Small Heat Shock Proteins HSPB1 and HSPB6

Baranova, E. V., Weeks, S. D., Beelen, S., Bukach, O. V., Gusev, N. B., & Strelkov, S. V. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.05.024 · Cited by 115 · see citing works

Functional Elements in Molecular Chaperone α-Crystallin: Identification of Binding Sites in αB-Crystallin

Sharma, K. K., Kaur, H., & Kester, K. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7460 · Cited by 113 · see citing works

Interactive Domains for Chaperone Activity in the Small Heat Shock Protein, Human αB Crystallin

Ghosh, J. G., Estrada, M. R., & Clark, J. I. (2005) · Biochemistry · doi:10.1021/bi0503910 · Cited by 102 · see citing works

The HSPB8‐BAG3 chaperone complex is upregulated in astrocytes in the human brain affected by protein aggregation diseases

Seidel, K., Vinet, J., den Dunnen, W. F. A., Brunt, E. R. P., Meister, M., Boncoraglio, A., Zijlstra, M. P., Boddeke, H. W. G. M., Rüb, U., Kampinga, H. H., et al. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2011.01198.x · Cited by 98 · see citing works

Inhibitors and chemical probes for molecular chaperone networks

Gestwicki, J. E., & Shao, H. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.002813 · Cited by 97 · see citing works

Mutations linked to neurological disease enhance self-association of low-complexity protein sequences

Zhou, X., Sumrow, L., Tashiro, K., Sutherland, L. B., Liu, D., Qin, T., Kato, M., Liszczak, G., & McKnight, S. L. (2022) · Science · doi:10.1126/science.abn5582 · Cited by 96 · see citing works

The chaperone HSPB8 reduces the accumulation of truncated TDP-43 species in cells and protects against TDP-43-mediated toxicity

Crippa, V., Cicardi, M. E., Ramesh, N., Seguin, S. J., Ganassi, M., Bigi, I., Diacci, C., Zelotti, E., Baratashvili, M., Gregory, J. M., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw232 · Cited by 95 · see citing works

HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain

Boczek, E. E., Fürsch, J., Niedermeier, M. L., Jawerth, L. M., Jahnel, M., Ruer, M., Kammer, K.-M., Heid, P., Mediani, L., Wang, J., et al. (2021) · eLife · doi:10.7554/elife.69377 · Cited by 94 · see citing works

Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage

Kumar, S. T., Nazarov, S., Porta, S., Maharjan, N., Cendrowska, U., Kabani, M., Finamore, F., Xu, Y., Lee, V. M. ‐., & Lashuel, H. A. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01341-4 · Cited by 88 · see citing works

Biology and Pathobiology of TDP-43 and Emergent Therapeutic StrategiesPreprint

Guo, L. E., & Shorter, J. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024554 · Cited by 84 · see citing works

Dynamical structure of αB-crystallin

Hochberg, G. K. A., & Benesch, J. L. P. (2014) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.03.003 · Cited by 78 · see citing works

Membraneless organelles: P granules in Caenorhabditis elegans

Marnik, E. A., & Updike, D. L. (2019) · Traffic · doi:10.1111/tra.12644 · Cited by 76 · see citing works

Hsp90-mediated regulation of DYRK3 couples stress granule disassembly and growth via mTORC1 signaling

Mediani, L., Antoniani, F., Galli, V., Vinet, J., Carrà, A. D., Bigi, I., Tripathy, V., Tiago, T., Cimino, M., Leo, G., et al. (2021) · EMBO Reports · doi:10.15252/embr.202051740 · Cited by 74 · see citing works

The Role of the Heat Shock Protein B8 (HSPB8) in Motoneuron Diseases

Rusmini, P., Cristofani, R., Galbiati, M., Cicardi, M. E., Meroni, M., Ferrari, V., Vezzoli, G., Tedesco, B., Messi, E., Piccolella, M., et al. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00176 · Cited by 69 · see citing works

Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8

Arrigo, A., & Gibert, B. (2013) · International Journal of Hyperthermia · doi:10.3109/02656736.2013.792956 · Cited by 68 · see citing works

A synergy between site-specific and transient interactions drives the phase separation of a disordered, low-complexity domain

Mohanty, P., Shenoy, J., Rizuan, A., Ortiz, J. F. M., Fawzi, N. L., & Mittal, J. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2305625120 · Cited by 67 · see citing works

Solid-State NMR Reveals the Structural Transformation of the TDP-43 Amyloidogenic Region upon Fibrillation

Zhuo, X.-F., Wang, J., Zhang, J., Jiang, L., Hu, H., & Lu, J. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10736 · Cited by 66 · see citing works

Hsp70 exhibits a liquid-liquid phase separation ability and chaperones condensed FUS against amyloid aggregation

Li, Y., Gu, J., Wang, C., Hu, J., Zhang, S., Liu, C., Zhang, S., Fang, Y., & Li, D. (2022) · iScience · doi:10.1016/j.isci.2022.104356 · Cited by 62 · see citing works

Structural genomics of human proteins – target selection and generation of a public catalogue of expression clones

Büssow, K., Scheich, C., Sievert, V., Harttig, U., Schultz, J., Simon, B., Peer Bork, B., Lehrach, H. R., & Heinemann, U. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-21 · Cited by 61 · see citing works

Some properties of human small heat shock protein Hsp22 (H11 or HspB8)

Kim, M. V., Seit‐Nebi, A. S., Marston, S. B., & Gusev, N. B. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.01.130 · Cited by 60 · see citing works

The Role of HSPB8, a Component of the Chaperone-Assisted Selective Autophagy Machinery, in Cancer

Cristofani, R., Piccolella, M., Crippa, V., Tedesco, B., Marelli, M. M., Poletti, A., & Moretti, R. M. (2021) · Cells · doi:10.3390/cells10020335 · Cited by 56 · see citing works

Chemical cross‐linking of the chloroplast localized small heat‐shock protein, Hsp21, and the model substrate citrate synthase

Åhrman, E., Lambert, W., Aquilina, J. A., Robinson, C. V., & Emanuelsson, C. S. (2007) · Protein Science · doi:10.1110/ps.072831607 · Cited by 54 · see citing works

Cryoelectron Microscopy and EPR Analysis of Engineered Symmetric and Polydisperse Hsp16.5 Assemblies Reveals Determinants of Polydispersity and Substrate Binding

Shi, J. R., Koteiche, H. A., Mchaourab, H. S., & Stewart, P. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608322200 · Cited by 51 · see citing works

An insoluble frontotemporal lobar degeneration-associated TDP-43 C-terminal fragment causes neurodegeneration and hippocampus pathology in transgenic mice

Walker, A. K., Tripathy, K., Restrepo, C. R., Ge, G., Xu, Y., Kwong, L. K., Trojanowski, J. Q., & Lee, V. M. ‐. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv424 · Cited by 48 · see citing works

Regulation of small heat-shock proteins by hetero-oligomer formation

Mymrikov, E. V., Riedl, M., Peters, C., Weinkauf, S., Haslbeck, M., & Büchner, J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011143 · Cited by 48 · see citing works

Identification of the Rigid Core for Aged Liquid Droplets of an RNA-Binding Protein Low Complexity Domain

Fonda, B. D., Jami, K. M., Boulos, N. R., & Murray, D. T. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c02424 · Cited by 38 · see citing works

Effects of oxidative and thermal stresses on stress granule formation in human induced pluripotent stem cells

Palangi, F., Samuel, S. M., Thompson, I. R., Triggle, C. R., & Emara, M. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182059 · Cited by 35 · see citing works

Cytoplasmic localization of amyotrophic lateral sclerosis‐related TDP‐43 proteins modulates stress granule formation

Besnard‐Guérin, C. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14762 · Cited by 30 · see citing works

Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble

Mühlhofer, M., Peters, C., Kriehuber, T., Kreuzeder, M. A., Kazman, P., Rodina, N. P., Reif, B., Haslbeck, M., Weinkauf, S., & Büchner, J. (2021) · Nature Communications · doi:10.1038/s41467-021-27036-7 · Cited by 30 · see citing works

The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces

Scheidt, T., Carozza, J. A., Kolbe, C. C., Aprile, F. A., Tkachenko, O., Bellaiche, M. M. J., Meisl, G., Peter, Q. A. E., Herling, T. W., Ness, S., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2108790118 · Cited by 26 · see citing works

The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8

Shatov, V. M., Weeks, S. D., Strelkov, S. V., & Gusev, N. B. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19072112 · Cited by 25 · see citing works

Liquid Droplet Aging and Seeded Fibril Formation of the Cytotoxic Granule Associated RNA Binding Protein TIA1 Low Complexity Domain

Wittmer, Y., Jami, K. M., Stowell, R. K., Le, T., Hung, I., & Murray, D. T. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c08596 · Cited by 24 · see citing works

Phosphorylation of human small heat shock protein HspB8 (Hsp22) by ERK1 protein kinase

Shemetov, A. A., Seit‐Nebi, A. S., & Gusev, N. B. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-0837-y · Cited by 22 · see citing works

Amyloid-like aggregation and fibril core determination of TDP-43 C-terminal domain

Chang, Z., Deng, J., Zhao, W., & Yang, J. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.08.096 · Cited by 21 · see citing works

Structure-Based Analysis of the β8 Interactive Sequence of Human αB Crystallin

Ghosh, J. G., Estrada, M. R., & Clark, J. I. (2006) · Biochemistry · doi:10.1021/bi060970k · Cited by 21 · see citing works

The Heterooligomerization of Human Small Heat Shock Proteins Is Controlled by Conserved Motif Located in the N-Terminal Domain

Shatov, V. M., Strelkov, S. V., & Gusev, N. B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124248 · Cited by 20 · see citing works

Chaperone‐like activity and surface hydrophobicity of 70S ribosome

Singh, R., & Rao, C. M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03243-x · Cited by 19 · see citing works

Pathological C‐terminal phosphomimetic substitutions alter the mechanism of liquid–liquid phase separation of TDP‐43 low complexity domain

Haider, R., Shipley, B., Surewicz, K. A., Hinczewski, M., & Surewicz, W. K. (2024) · Protein Science · doi:10.1002/pro.5179 · Cited by 17 · see citing works

Phosphoproteome Analysis Reveals Dynamic Heat Shock Protein 27 Phosphorylation in Tanshinone IIA-Induced Cell Death

Yin, C.-F., Kao, S.-C., Hsu, C., Chang, Y.-W., Cheung, C. H. Y., Huang, H., & Juan, H. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00836 · Cited by 13 · see citing works

Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners

Hussein, R. M., Benjamin, I. J., & Kampinga, H. H. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126761 · Cited by 13 · see citing works

Oxidized GroEL can function as a chaperonin

Melkani, G. C. (2004) · Frontiers in bioscience · doi:10.2741/1258 · Cited by 12 · see citing works

The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin

Jovcevski‬, B., Aquilina, J. A., Benesch, J. L. P., & Ecroyd, H. W. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-018-0889-y · Cited by 9 · see citing works

Replacement of Arg in the conserved N-terminal RLFDQxFG motif affects physico-chemical properties and chaperone-like activity of human small heat shock protein HspB8 (Hsp22)

Shatov, V. M., Sluchanko, N. N., & Gusev, N. B. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253432 · Cited by 8 · see citing works

Biophysical Studies of LLPS and Aggregation of TDP-43 LCD

Babinchak, W. M., & Surewicz, W. K. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2597-2_31 · Cited by 3 · see citing works

Evolution towards simplicity in bacterial small heat shock protein system

Karaś, P., Kochanowicz, K., Pitek, M., Domanski, P., Obuchowski, I., Tomiczek, B., & Liberek, K. (2023) · eLife · doi:10.7554/elife.89813 · Cited by 2 · see citing works

Droplet growth, Ostwald’s rule, and emergence of order in Fused in Sarcoma

Maksudov, F., Mugnai, M. L., Domı́nguez, L., Makarov, D. E., & Thirumalai, D. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2519135123 · Cited by 4 · see citing works

UBQLN2 links proteotoxicity with lipid metabolism in neurodegeneration

Liu, Y., Huang, Z., hsu, Y.-W., Deme, P., Frankenfield, A. M., Wu, S., Zhao, X., Liu, H., Zhang, T., Alexander, E. J., et al. (2026) · Nature Neuroscience · doi:10.1038/s41593-026-02226-y · Cited by 4 · see citing works

Small heat shock proteins HspB1 and HspB5 differentially alter the condensation and aggregation of the TDP ‐43 low‐complexity domain

Walker, T. B., Trowbridge, J. W., McMahon, S., Marzano, N. R., Rice, L. J., Yerbury, J. J., Ecroyd, H. W., & McAlary, L. (2026) · Protein Science · doi:10.1002/pro.70539 · Cited by 3 · see citing works

Examining the role of small heat shock proteins in regulating the phase separation and aggregation of TDP-43

Walker, T. A. (2026) · Research Online (University of Wollongong) · doi:10.71747/uow-r3gk326m.31343503

Role of HSPB8 in the Proteostasis Network: From Protein Synthesis to Protein Degradation and Beyond

Poletti, A., & Carra, S. (2015) · Heat shock proteins · doi:10.1007/978-3-319-16077-1_21 · Cited by 1 · see citing works

The chaperone HSPB8 reduces the accumulation of truncated TDP-43 species in cells and protects against TDP-43-mediated toxicity

Crippa, V., Cicardi, M. E., Ramesh, N., Seguin, S. J., Ganassi, M., Bigi, I., Diacci, C., Zelotti, E., Baratashvili, M., Gregory, J. M., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw232 · Cited by 95 · see citing works

Significance of Small Heat Shock Proteins HSPB1 and HSPB5 in Aggregation and Degradation of Amyloid Proteins

Ojha, J. (2011)