Year |
Citation |
Score |
2024 |
Korsten G, Osinga M, Pelle RA, Serweta AK, Hoogenberg B, Kampinga HH, Kapitein LC. Nuclear poly-glutamine aggregates rupture the nuclear envelope and hinder its repair. The Journal of Cell Biology. 223. PMID 39150509 DOI: 10.1083/jcb.202307142 |
0.463 |
|
2024 |
Adupa V, Ustyantseva E, Kampinga HH, Onck PR. Tertiary structure and conformational dynamics of the anti-amyloidogenic chaperone DNAJB6b at atomistic resolution. Nature Communications. 15: 3285. PMID 38627370 DOI: 10.1038/s41467-024-46587-z |
0.322 |
|
2024 |
Ryder BD, Ustyantseva E, Boyer DR, Mendoza-Oliva A, Kuska MI, Wydorski PM, Macierzyńska P, Morgan N, Sawaya MR, Diamond MI, Kampinga HH, Joachimiak LA. DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity. Structure (London, England : 1993). PMID 38508190 DOI: 10.1016/j.str.2024.02.015 |
0.353 |
|
2023 |
Marszalek J, De Los Rios P, Cyr D, Mayer MP, Adupa V, Andréasson C, Blatch GL, Braun JEA, Brodsky JL, Bukau B, Chapple JP, Conz C, Dementin S, Genevaux P, Genest O, ... ... Kampinga HH, et al. J-domain proteins: From molecular mechanisms to diseases. Cell Stress & Chaperones. 29: 21-33. PMID 38320449 DOI: 10.1016/j.cstres.2023.12.002 |
0.414 |
|
2023 |
Ryder BD, Boyer DR, Ustyantseva E, Mendoza-Oliva A, Kuska MI, Wydorski PM, Sawaya M, Diamond MI, Eisenberg DS, Kampinga HH, Joachimiak LA. DNAJB8 oligomerization is mediated by an aromatic-rich motif that is dispensable for substrate activity. Biorxiv : the Preprint Server For Biology. PMID 36945632 DOI: 10.1101/2023.03.06.531355 |
0.352 |
|
2022 |
Kuiper EFE, Gallardo P, Bergsma T, Mari M, Kolbe Musskopf M, Kuipers J, Giepmans BNG, Steen A, Kampinga HH, Veenhoff LM, Bergink S. The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis. Nature Cell Biology. 24: 1584-1594. PMID 36302971 DOI: 10.1038/s41556-022-01010-x |
0.404 |
|
2022 |
Mauthe M, Kampinga HH, Hipp MS, Reggiori F. Digest it all: the lysosomal turnover of cytoplasmic aggregates. Trends in Biochemical Sciences. PMID 36280494 DOI: 10.1016/j.tibs.2022.09.012 |
0.538 |
|
2022 |
Huiting W, Dekker SL, van der Lienden JCJ, Mergener R, Musskopf MK, Furtado GV, Gerrits E, Coit D, Oghbaie M, Di Stefano LH, Schepers H, van Waarde-Verhagen MAWH, Couzijn S, Barazzuol L, LaCava J, ... Kampinga HH, et al. Targeting DNA topoisomerases or checkpoint kinases results in an overload of chaperone systems, triggering aggregation of a metastable subproteome. Elife. 11. PMID 35200138 DOI: 10.7554/eLife.70726 |
0.53 |
|
2021 |
Joshi BS, Youssef SA, Bron R, de Bruin A, Kampinga HH, Zuhorn IS. DNAJB6b-enriched small extracellular vesicles decrease polyglutamine aggregation in and models of Huntington disease. Iscience. 24: 103282. PMID 34755099 DOI: 10.1016/j.isci.2021.103282 |
0.422 |
|
2021 |
Furtado GV, Yang J, Wu D, Papagiannopoulos CI, Terpstra HM, Kuiper EFE, Krauss S, Zhu WG, Kampinga HH, Bergink S. FOXO1 controls protein synthesis and transcript abundance of mutant polyglutamine proteins, preventing protein aggregation. Human Molecular Genetics. PMID 33822053 DOI: 10.1093/hmg/ddab095 |
0.529 |
|
2021 |
McMahon S, Bergink S, Kampinga HH, Ecroyd H. DNAJB chaperones suppress destabilised protein aggregation via a region unique from that used to inhibit amyloidogenesis. Journal of Cell Science. PMID 33674449 DOI: 10.1242/jcs.255596 |
0.561 |
|
2020 |
Leotti VB, de Vries JJ, Oliveira CM, de Mattos EP, Te Meerman GJ, Brunt ER, Kampinga HH, Jardim LB, Verbeek DS. CAG Repeat Size Influences the Progression Rate of Spinocerebellar Ataxia Type 3. Annals of Neurology. PMID 32978817 DOI: 10.1002/ana.25919 |
0.324 |
|
2020 |
Nachman E, Wentink AS, Madiona K, Bousset L, Katsinelos T, Allinson K, Kampinga H, McEwan WA, Jahn TR, Melki R, Mogk A, Bukau B, Nussbaum-Krammer C. Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species. The Journal of Biological Chemistry. PMID 32467226 DOI: 10.1074/Jbc.Ra120.013478 |
0.378 |
|
2020 |
Serlidaki D, van Waarde MAWH, Rohland L, Wentink AS, Dekker SL, Kamphuis MJ, Boertien JM, Brunsting JF, Nillegoda NB, Bukau B, Mayer MP, Kampinga HH, Bergink S. Functional diversity between HSP70 paralogs due to variable interactions with specific co-chaperones. The Journal of Biological Chemistry. PMID 32284329 DOI: 10.1074/Jbc.Ra119.012449 |
0.417 |
|
2020 |
Thiruvalluvan A, de Mattos EP, Brunsting JF, Bakels R, Serlidaki D, Barazzuol L, Conforti P, Fatima A, Koyuncu S, Cattaneo E, Vilchez D, Bergink S, Boddeke EHWG, Copray S, Kampinga HH. DNAJB6, a Key Factor in Neuronal Sensitivity to Amyloidogenesis. Molecular Cell. PMID 32268123 DOI: 10.1016/J.Molcel.2020.02.022 |
0.43 |
|
2020 |
De Mattos EP, Wentink A, Nussbaum-Krammer C, Hansen C, Bergink S, Melki R, Kampinga HH. Protein Quality Control Pathways at the Crossroad of Synucleinopathies. Journal of Parkinson's Disease. PMID 31985474 DOI: 10.3233/JPD-191790 |
0.439 |
|
2019 |
Kampinga HH, Mayer MP, Mogk A. Protein quality control: from mechanism to disease : EMBO Workshop, Costa de la Calma (Mallorca), Spain, April 28 - May 03, 2019. Cell Stress & Chaperones. PMID 31713048 DOI: 10.1007/s12192-019-01040-9 |
0.482 |
|
2019 |
Azkanaz M, Rodríguez López A, de Boer B, Huiting W, Angrand PO, Vellenga E, Kampinga HH, Bergink S, Martens JH, Schuringa JJ, van den Boom V. Protein quality control in the nucleolus safeguards recovery of epigenetic regulators after heat shock. Elife. 8. PMID 31199242 DOI: 10.7554/eLife.45205 |
0.348 |
|
2019 |
Wu D, Vonk JJ, Salles F, Vonk D, Haslbeck M, Melki R, Bergink S, Kampinga HH. The N terminus of the small heat shock protein HSPB7 drives its polyQ aggregation-suppressing activity. The Journal of Biological Chemistry. PMID 31097540 DOI: 10.1074/jbc.RA118.007117 |
0.471 |
|
2018 |
Meister-Broekema M, Freilich R, Jagadeesan C, Rauch JN, Bengoechea R, Motley WW, Kuiper EFE, Minoia M, Furtado GV, van Waarde MAWH, Bird SJ, Rebelo A, Zuchner S, Pytel P, Scherer SS, ... ... Kampinga HH, et al. Myopathy associated BAG3 mutations lead to protein aggregation by stalling Hsp70 networks. Nature Communications. 9: 5342. PMID 30559338 DOI: 10.1038/S41467-018-07718-5 |
0.426 |
|
2018 |
Kampinga HH, Andreasson C, Barducci A, Cheetham ME, Cyr D, Emanuelsson C, Genevaux P, Gestwicki JE, Goloubinoff P, Huerta-Cepas J, Kirstein J, Liberek K, Mayer MP, Nagata K, Nillegoda NB, et al. Function, evolution, and structure of J-domain proteins. Cell Stress & Chaperones. PMID 30478692 DOI: 10.1007/S12192-018-0948-4 |
0.311 |
|
2018 |
Bason M, Meister-Broekema M, Alberts N, Dijkers P, Bergink S, Sibon OCM, Kampinga HH. Astrocytic expression of the chaperone DNAJB6 results in non-cell autonomous protection in Huntington's disease. Neurobiology of Disease. 124: 108-117. PMID 30408590 DOI: 10.1016/j.nbd.2018.10.017 |
0.471 |
|
2018 |
Ast A, Buntru A, Schindler F, Hasenkopf R, Schulz A, Brusendorf L, Klockmeier K, Grelle G, McMahon B, Niederlechner H, Jansen I, Diez L, Edel J, Boeddrich A, Franklin SA, ... ... Kampinga HH, et al. mHTT Seeding Activity: A Marker of Disease Progression and Neurotoxicity in Models of Huntington's Disease. Molecular Cell. 71: 675-688.e6. PMID 30193095 DOI: 10.1016/J.Molcel.2018.07.032 |
0.361 |
|
2018 |
Mogk A, Bukau B, Kampinga HH. Cellular Handling of Protein Aggregates by Disaggregation Machines. Molecular Cell. 69: 214-226. PMID 29351843 DOI: 10.1016/J.Molcel.2018.01.004 |
0.559 |
|
2018 |
van Waarde-Verhagen MAWH, Kampinga HH. Measurement of Chaperone-Mediated Effects on Polyglutamine Protein Aggregation by the Filter Trap Assay. Methods in Molecular Biology (Clifton, N.J.). 1709: 59-74. PMID 29177651 DOI: 10.1007/978-1-4939-7477-1_5 |
0.564 |
|
2017 |
Carra S, Alberti S, Arrigo PA, Benesch JL, Benjamin IJ, Boelens W, Bartelt-Kirbach B, Brundel BJ, Buchner J, Bukau B, Carver JA, Ecroyd H, Emanuelsson C, Finet S, Golenhofen N, ... ... Kampinga HH, et al. The growing world of small heat shock proteins: from structure to functions. Cell Stress & Chaperones. PMID 28364346 DOI: 10.1007/S12192-017-0787-8 |
0.514 |
|
2016 |
Kakkar V, Kuiper EF, Pandey A, Braakman I, Kampinga HH. Versatile members of the DNAJ family show Hsp70 dependent anti-aggregation activity on RING1 mutant parkin C289G. Scientific Reports. 6: 34830. PMID 27713507 DOI: 10.1038/Srep34830 |
0.548 |
|
2016 |
Kakkar V, Månsson C, de Mattos EP, Bergink S, van der Zwaag M, van Waarde MA, Kloosterhuis NJ, Melki R, van Cruchten RT, Al-Karadaghi S, Arosio P, Dobson CM, Knowles TP, Bates GP, van Deursen JM, ... ... Kampinga HH, et al. The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model. Molecular Cell. PMID 27151442 DOI: 10.1016/J.Molcel.2016.03.017 |
0.497 |
|
2016 |
Kampinga HH, Bergink S. Heat shock proteins as potential targets for protective strategies in neurodegeneration. The Lancet. Neurology. 15: 748-759. PMID 27106072 DOI: 10.1016/S1474-4422(16)00099-5 |
0.637 |
|
2016 |
Eenjes E, Dragich JM, Kampinga HH, Yamamoto A. Distinguishing aggregate formation and aggregate clearance using cell based assays. Journal of Cell Science. PMID 26818841 DOI: 10.1242/Jcs.179978 |
0.538 |
|
2015 |
Vos MJ, Carra S, Kanon B, Bosveld F, Klauke K, Sibon OC, Kampinga HH. Specific protein homeostatic functions of small heat-shock proteins increase lifespan. Aging Cell. 15: 217-26. PMID 26705243 DOI: 10.1111/acel.12422 |
0.506 |
|
2015 |
Snijder PM, Baratashvili M, Grzeschik NA, Leuvenink HG, Kuijpers L, Huitema S, Schaap O, Giepmans BN, Kuipers J, Miljkovic JL, Mitrovic A, Bos EM, Szabó C, Kampinga HH, Dijkers PF, et al. Overexpression of cystathionine γ-lyase suppresses detrimental effects of spinocerebellar ataxia type 3. Molecular Medicine (Cambridge, Mass.). PMID 26467707 DOI: 10.2119/Molmed.2015.00221 |
0.434 |
|
2015 |
Dekker SL, Kampinga HH, Bergink S. DNAJs: more than substrate delivery to HSPA. Frontiers in Molecular Biosciences. 2: 35. PMID 26176011 DOI: 10.3389/fmolb.2015.00035 |
0.438 |
|
2015 |
Hussein RM, Benjamin IJ, Kampinga HH. Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners. Plos One. 10: e0126761. PMID 25961584 DOI: 10.1371/journal.pone.0126761 |
0.364 |
|
2014 |
Ma?nsson C, Arosio P, Hussein R, Kampinga HH, Hashem RM, Boelens WC, Dobson CM, Knowles TPJ, Linse S, Emanuelsson C. Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation Journal of Biological Chemistry. 289: 31066-31076. PMID 25217638 DOI: 10.1074/Jbc.M114.595124 |
0.433 |
|
2014 |
Minoia M, Grit C, Kampinga HH. HSPA1A-independent suppression of PARK2 C289G protein aggregation by human small heat shock proteins. Molecular and Cellular Biology. 34: 3570-8. PMID 25022755 DOI: 10.1128/MCB.00698-14 |
0.535 |
|
2014 |
Kakkar V, Meister-Broekema M, Minoia M, Carra S, Kampinga HH. Barcoding heat shock proteins to human diseases: looking beyond the heat shock response. Disease Models & Mechanisms. 7: 421-34. PMID 24719117 DOI: 10.1242/dmm.014563 |
0.543 |
|
2014 |
Vonk WI, Kakkar V, Bartuzi P, Jaarsma D, Berger R, Hofker MH, Klomp LW, Wijmenga C, Kampinga HH, van de Sluis B. The Copper Metabolism MURR1 domain protein 1 (COMMD1) modulates the aggregation of misfolded protein species in a client-specific manner. Plos One. 9: e92408. PMID 24691167 DOI: 10.1371/Journal.Pone.0092408 |
0.563 |
|
2014 |
Månsson C, Kakkar V, Monsellier E, Sourigues Y, Härmark J, Kampinga HH, Melki R, Emanuelsson C. DNAJB6 is a peptide-binding chaperone which can suppress amyloid fibrillation of polyglutamine peptides at substoichiometric molar ratios. Cell Stress & Chaperones. 19: 227-39. PMID 23904097 DOI: 10.1007/S12192-013-0448-5 |
0.41 |
|
2013 |
Yang J, Carra S, Zhu WG, Kampinga HH. The regulation of the autophagic network and its implications for human disease. International Journal of Biological Sciences. 9: 1121-33. PMID 24339733 DOI: 10.7150/ijbs.6666 |
0.315 |
|
2013 |
Gillis J, Schipper-Krom S, Juenemann K, Gruber A, Coolen S, Van Den Nieuwendijk R, Van Veen H, Overkleeft H, Goedhart J, Kampinga HH, Reits EA. The DNAJB6 and DNAJB8 protein chaperones prevent intracellular aggregation of polyglutamine peptides Journal of Biological Chemistry. 288: 17225-17237. PMID 23612975 DOI: 10.1074/Jbc.M112.421685 |
0.463 |
|
2013 |
Carra S, Rusmini P, Crippa V, Giorgetti E, Boncoraglio A, Cristofani R, Naujock M, Meister M, Minoia M, Kampinga HH, Poletti A. Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 368: 20110409. PMID 23530259 DOI: 10.1098/rstb.2011.0409 |
0.551 |
|
2013 |
Kakkar V, Prins LC, Kampinga HH. DNAJ proteins and protein aggregation diseases. Current Topics in Medicinal Chemistry. 12: 2479-90. PMID 23339302 DOI: 10.2174/1568026611212220004 |
0.643 |
|
2012 |
Mannini B, Cascella R, Zampagni M, Van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F. Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers Proceedings of the National Academy of Sciences of the United States of America. 109: 12479-12484. PMID 22802614 DOI: 10.1073/Pnas.1117799109 |
0.468 |
|
2011 |
Carra S, Crippa V, Rusmini P, Boncoraglio A, Minoia M, Giorgetti E, Kampinga HH, Poletti A. Alteration of protein folding and degradation in motor neuron diseases: Implications and protective functions of small heat shock proteins. Progress in Neurobiology. 97: 83-100. PMID 21971574 DOI: 10.1016/j.pneurobio.2011.09.009 |
0.43 |
|
2011 |
Hishiya A, Salman MN, Carra S, Kampinga HH, Takayama S. BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity. Plos One. 6: e16828. PMID 21423662 DOI: 10.1371/journal.pone.0016828 |
0.306 |
|
2011 |
Hageman J, van Waarde MA, Zylicz A, Walerych D, Kampinga HH. The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. The Biochemical Journal. 435: 127-42. PMID 21231916 DOI: 10.1042/BJ20101247 |
0.345 |
|
2011 |
Vos MJ, Zijlstra MP, Carra S, Sibon OC, Kampinga HH. Small heat shock proteins, protein degradation and protein aggregation diseases. Autophagy. 7: 101-3. PMID 21045566 DOI: 10.4161/auto.7.1.13935 |
0.517 |
|
2010 |
Carra S, Boncoraglio A, Kanon B, Brunsting JF, Minoia M, Rana A, Vos MJ, Seidel K, Sibon OC, Kampinga HH. Identification of the Drosophila ortholog of HSPB8: implication of HSPB8 loss of function in protein folding diseases. The Journal of Biological Chemistry. 285: 37811-22. PMID 20858900 DOI: 10.1074/jbc.M110.127498 |
0.459 |
|
2010 |
Vos MJ, Zijlstra MP, Kanon B, van Waarde-Verhagen MA, Brunt ER, Oosterveld-Hut HM, Carra S, Sibon OC, Kampinga HH. HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones. Human Molecular Genetics. 19: 4677-93. PMID 20843828 DOI: 10.1093/hmg/ddq398 |
0.347 |
|
2010 |
Kampinga HH, Craig EA. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nature Reviews. Molecular Cell Biology. 11: 579-92. PMID 20651708 DOI: 10.1038/Nrm2941 |
0.394 |
|
2010 |
Seidel K, den Dunnen WF, Schultz C, Paulson H, Frank S, de Vos RA, Brunt ER, Deller T, Kampinga HH, Rüb U. Axonal inclusions in spinocerebellar ataxia type 3. Acta Neuropathologica. 120: 449-60. PMID 20635090 DOI: 10.1007/S00401-010-0717-7 |
0.379 |
|
2010 |
Hageman J, Rujano MA, van Waarde MAWH, Kakkar V, Dirks RP, Govorukhina N, Oosterveld-Hut HMJ, Lubsen NH, Kampinga HH. A DNAJB Chaperone Subfamily with HDAC-Dependent Activities Suppresses Toxic Protein Aggregation Molecular Cell. 37: 355-369. PMID 20159555 DOI: 10.1016/j.molcel.2010.01.001 |
0.546 |
|
2009 |
Carra S, Brunsting JF, Lambert H, Landry J, Kampinga HH. HspB8 participates in protein quality control by a non-chaperone-like mechanism that requires eIF2{alpha} phosphorylation. The Journal of Biological Chemistry. 284: 5523-32. PMID 19114712 DOI: 10.1074/Jbc.M807440200 |
0.423 |
|
2008 |
Vos MJ, Hageman J, Carra S, Kampinga HH. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry. 47: 7001-11. PMID 18557634 DOI: 10.1021/bi800639z |
0.364 |
|
2008 |
Vos MJ, Kampinga HH. A PCR amplification strategy for unrestricted generation of chimeric genes. Analytical Biochemistry. 380: 338-40. PMID 18555003 DOI: 10.1016/j.ab.2008.05.031 |
0.345 |
|
2008 |
Brundel BJ, Ke L, Dijkhuis AJ, Qi X, Shiroshita-Takeshita A, Nattel S, Henning RH, Kampinga HH. Heat shock proteins as molecular targets for intervention in atrial fibrillation. Cardiovascular Research. 78: 422-8. PMID 18326558 DOI: 10.1093/Cvr/Cvn060 |
0.33 |
|
2007 |
Rujano MA, Bosveld F, Salomons FA, Dijk F, van Waarde MA, van der Want JJ, de Vos RA, Brunt ER, Sibon OC, Kampinga HH. Polarised asymmetric inheritance of accumulated protein damage in higher eukaryotes. Plos Biology. 4: e417. PMID 17147470 DOI: 10.1371/journal.pbio.0040417 |
0.548 |
|
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