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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface
Christopher A. G. Söderberg, Cecilia Månsson, Katja Bernfur, et al.
Scientific Reports (2018) Vol. 8, Iss. 1
Open Access | Times Cited: 56

Showing 1-25 of 56 citing articles:

Function, evolution, and structure of J-domain proteins
Harm H. Kampinga, Claes Andréasson, Alessandro Barducci, et al.
Cell Stress and Chaperones (2018) Vol. 24, Iss. 1, pp. 7-15
Open Access | Times Cited: 154
Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis
Theodoros K. Karamanos, Vitali Tugarinov, G. Marius Clore
Proceedings of the National Academy of Sciences (2019) Vol. 116, Iss. 43, pp. 21529-21538
Open Access | Times Cited: 87
Modulation of Amyloid States by Molecular Chaperones
Anne S. Wentink, Carmen Nussbaum‐Krammer, Bernd Bukau
Cold Spring Harbor Perspectives in Biology (2019) Vol. 11, Iss. 7, pp. a033969-a033969
Open Access | Times Cited: 79
Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results
J. Sarparanta, Per Harald Jonson, Sabita Kawan, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 4, pp. 1409-1409
Open Access | Times Cited: 71
J-domain protein chaperone circuits in proteostasis and disease
Ruobing Zhang, Duccio Malinverni, Douglas Cyr, et al.
Trends in Cell Biology (2022) Vol. 33, Iss. 1, pp. 30-47
Open Access | Times Cited: 48
The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis
E. F. Elsiena Kuiper, Paola Gallardo, Tessa Bergsma, et al.
Nature Cell Biology (2022) Vol. 24, Iss. 11, pp. 1584-1594
Open Access | Times Cited: 39
Amyloid inhibition by molecular chaperones in vitro can be translated to Alzheimer's pathology in vivo
Axel Abelein, Jan Johansson
RSC Medicinal Chemistry (2023) Vol. 14, Iss. 5, pp. 848-857
Open Access | Times Cited: 17
DNAJB6 mutants display toxic gain of function through unregulated interaction with Hsp70 chaperones
Meital Abayev-Avraham, Yehuda Salzberg, Dar Gliksberg, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 17
Conserved S/T Residues of the Human Chaperone DNAJB6 Are Required for Effective Inhibition of Aβ42 Amyloid Fibril Formation
Cecilia Månsson, Remco T. P. van Cruchten, Ulrich Weininger, et al.
Biochemistry (2018) Vol. 57, Iss. 32, pp. 4891-4902
Closed Access | Times Cited: 53
Amyloid-β oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation
Nicklas Österlund, Martin Lundqvist, Leopold L. Ilag, et al.
Journal of Biological Chemistry (2020) Vol. 295, Iss. 24, pp. 8135-8144
Open Access | Times Cited: 42
The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70
Lorea Velasco‐Carneros, Jorge Cuéllar, Leire Dublang, et al.
Nature Communications (2023) Vol. 14, Iss. 1
Open Access | Times Cited: 13
The Ability of DNAJB6b to Suppress Amyloid Formation Depends on the Chaperone Aggregation State
Andreas Carlsson, Emil Axell, Cecilia Emanuelsson, et al.
ACS Chemical Neuroscience (2024) Vol. 15, Iss. 9, pp. 1732-1737
Open Access | Times Cited: 4
Regulatory inter-domain interactions influence Hsp70 recruitment to the DnaJB8 chaperone
Bryan D. Ryder, Irina Matlahov, Sofia Bali, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 27
Identification of a HTT-specific binding motif in DNAJB1 essential for suppression and disaggregation of HTT
Sara María Ayala Mariscal, Maria Lucia Pigazzini, Yasmin Richter, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 18
Specification of Hsp70 Function by Hsp40 Co-chaperones
Douglas Cyr, Carlos H.I. Ramos
Sub-cellular biochemistry/Subcellular biochemistry (2022), pp. 127-139
Closed Access | Times Cited: 18
On the thermal and chemical stability of DNAJB6b and its globular domains
Celia Fricke, Jelica Milošević, Andreas Carlsson, et al.
Biophysical Chemistry (2025) Vol. 320-321, pp. 107401-107401
Open Access
Structural, functional relevance of DNAJBs in protein aggregation and associated neurodegenerative diseases
Siraj Fatima, Priyanka Pandey, Sandeep Sharma, et al.
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (2025), pp. 141074-141074
Closed Access
Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function
Laura Troussicot, Björn M. Burmann, Mikael Molin
Structure (2021) Vol. 29, Iss. 7, pp. 640-654
Open Access | Times Cited: 21
A FRET-based method for monitoring structural transitions in protein self-organization
Qi Wan, Sara N. Mouton, Liesbeth M. Veenhoff, et al.
Cell Reports Methods (2022) Vol. 2, Iss. 3, pp. 100184-100184
Open Access | Times Cited: 15
Astrocytic expression of the chaperone DNAJB6 results in non-cell autonomous protection in Huntington’s disease
Matteo Bason, Melanie Meister-Broekema, Niels Alberts, et al.
Neurobiology of Disease (2018) Vol. 124, pp. 108-117
Open Access | Times Cited: 26
DNAJB chaperones suppress destabilised protein aggregation via a region distinct from that used to inhibit amyloidogenesis
Shannon McMahon, Steven Bergink, Harm H. Kampinga, et al.
Journal of Cell Science (2021) Vol. 134, Iss. 7
Open Access | Times Cited: 20
J-domain proteins interaction with neurodegenerative disease-related proteins
Sara María Ayala Mariscal, Janine Kirstein
Experimental Cell Research (2021) Vol. 399, Iss. 2, pp. 112491-112491
Closed Access | Times Cited: 19
High-Efficiency Expression and Purification of DNAJB6b Based on the pH-Modulation of Solubility and Denaturant-Modulation of Size
Sara Linse
Molecules (2022) Vol. 27, Iss. 2, pp. 418-418
Open Access | Times Cited: 13
The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation
Ya-Lan Chang, Chan-Chih Yang, Yun-Yu Huang, et al.
BMC Biology (2023) Vol. 21, Iss. 1
Open Access | Times Cited: 8
The C-terminal domain of the antiamyloid chaperone DNAJB6 binds to amyloid-β peptide fibrils and inhibits secondary nucleation
Nicklas Österlund, Rebecca Frankel, Andreas Carlsson, et al.
Journal of Biological Chemistry (2023) Vol. 299, Iss. 11, pp. 105317-105317
Open Access | Times Cited: 7
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