A citation-based method for searching scientific literature

Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.
Stanislav A Bondarev, Kirill S Antonets, Andrey V Kajava, Anton A Nizhnikov, Galina A Zhouravleva. Int J Mol Sci 2018
Times Cited: 18






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List of co-cited articles
102 articles co-cited >1



Times Cited
  Times     Co-cited
Similarity


Molecular mechanisms of protein aggregation from global fitting of kinetic models.
Georg Meisl, Julius B Kirkegaard, Paolo Arosio, Thomas C T Michaels, Michele Vendruscolo, Christopher M Dobson, Sara Linse, Tuomas P J Knowles. Nat Protoc 2016
332
5
27

Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides.
Georg Meisl, Xiaoting Yang, Erik Hellstrand, Birgitta Frohm, Julius B Kirkegaard, Samuel I A Cohen, Christopher M Dobson, Sara Linse, Tuomas P J Knowles. Proc Natl Acad Sci U S A 2014
290
4
22

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.
Samuel I A Cohen, Sara Linse, Leila M Luheshi, Erik Hellstrand, Duncan A White, Luke Rajah, Daniel E Otzen, Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles. Proc Natl Acad Sci U S A 2013
816
4
22

A new era for understanding amyloid structures and disease.
Matthew G Iadanza, Matthew P Jackson, Eric W Hewitt, Neil A Ranson, Sheena E Radford. Nat Rev Mol Cell Biol 2018
363
4
22

Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
Michael R Sawaya, Shilpa Sambashivan, Rebecca Nelson, Magdalena I Ivanova, Stuart A Sievers, Marcin I Apostol, Michael J Thompson, Melinda Balbirnie, Jed J W Wiltzius, Heather T McFarlane,[...]. Nature 2007
1585
4
22

Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.
Fabrizio Chiti, Christopher M Dobson. Annu Rev Biochem 2017
1244
4
22

Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation.
Alexander K Buell, Céline Galvagnion, Ricardo Gaspar, Emma Sparr, Michele Vendruscolo, Tuomas P J Knowles, Sara Linse, Christopher M Dobson. Proc Natl Acad Sci U S A 2014
391
3
16

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.
Marcus D Tuttle, Gemma Comellas, Andrew J Nieuwkoop, Dustin J Covell, Deborah A Berthold, Kathryn D Kloepper, Joseph M Courtney, Jae K Kim, Alexander M Barclay, Amy Kendall,[...]. Nat Struct Mol Biol 2016
561
3
16

Protein folding and misfolding.
Christopher M Dobson. Nature 2003
3051
3
16

Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.
Dmitry S Kryndushkin, Ilya M Alexandrov, Michael D Ter-Avanesyan, Vitaly V Kushnirov. J Biol Chem 2003
346
3
16

Fundamentals of cross-seeding of amyloid proteins: an introduction.
Baiping Ren, Yanxian Zhang, Mingzhen Zhang, Yonglan Liu, Dong Zhang, Xiong Gong, Zhangqi Feng, Jianxin Tang, Yung Chang, Jie Zheng. J Mater Chem B 2019
54
3
16

The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure.
David R Boyer, Binsen Li, Chuanqi Sun, Weijia Fan, Kang Zhou, Michael P Hughes, Michael R Sawaya, Lin Jiang, David S Eisenberg. Proc Natl Acad Sci U S A 2020
71
3
16

Amyloid-Beta Peptides Trigger Aggregation of Alpha-Synuclein In Vitro.
Janett Köppen, Anja Schulze, Lisa Machner, Michael Wermann, Rico Eichentopf, Max Guthardt, Angelika Hähnel, Jessica Klehm, Marie-Christin Kriegeskorte, Maike Hartlage-Rübsamen,[...]. Molecules 2020
31
3
16

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel.
Binsen Li, Peng Ge, Kevin A Murray, Phorum Sheth, Meng Zhang, Gayatri Nair, Michael R Sawaya, Woo Shik Shin, David R Boyer, Shulin Ye,[...]. Nat Commun 2018
288
3
16

Secondary nucleation in amyloid formation.
Mattias Törnquist, Thomas C T Michaels, Kalyani Sanagavarapu, Xiaoting Yang, Georg Meisl, Samuel I A Cohen, Tuomas P J Knowles, Sara Linse. Chem Commun (Camb) 2018
186
3
16

Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology.
Magdalena I Ivanova, Yuxi Lin, Young-Ho Lee, Jie Zheng, Ayyalusamy Ramamoorthy. Biophys Chem 2021
65
3
16

Chemical kinetics for drug discovery to combat protein aggregation diseases.
Paolo Arosio, Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles. Trends Pharmacol Sci 2014
153
3
16

Nucleated polymerisation in the presence of pre-formed seed filaments.
Samuel I A Cohen, Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles. Int J Mol Sci 2011
38
2
11

Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide.
Samuel I A Cohen, Risto Cukalevski, Thomas C T Michaels, Anđela Šarić, Mattias Törnquist, Michele Vendruscolo, Christopher M Dobson, Alexander K Buell, Tuomas P J Knowles, Sara Linse. Nat Chem 2018
89
2
11

The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.
Alexander K Buell, Christopher M Dobson, Tuomas P J Knowles. Essays Biochem 2014
44
2
11

Nucleated polymerization with secondary pathways. I. Time evolution of the principal moments.
Samuel I A Cohen, Michele Vendruscolo, Mark E Welland, Christopher M Dobson, Eugene M Terentjev, Tuomas P J Knowles. J Chem Phys 2011
224
2
11

Role of elongation and secondary pathways in S6 amyloid fibril growth.
Nikolai Lorenzen, Samuel I A Cohen, Søren B Nielsen, Therese W Herling, Gunna Christiansen, Christopher M Dobson, Tuomas P J Knowles, Daniel Otzen. Biophys J 2012
29
2
11

An analytical solution to the kinetics of breakable filament assembly.
Tuomas P J Knowles, Christopher A Waudby, Glyn L Devlin, Samuel I A Cohen, Adriano Aguzzi, Michele Vendruscolo, Eugene M Terentjev, Mark E Welland, Christopher M Dobson. Science 2009
717
2
11

Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism.
W P Esler, E R Stimson, J M Jennings, H V Vinters, J R Ghilardi, J P Lee, P W Mantyh, J E Maggio. Biochemistry 2000
295
2
11

Amyloid cross-seeding raises new dimensions to understanding of amyloidogenesis mechanism.
Paramita Chaudhuri, Kailash P Prajapati, Bibin G Anand, Kriti Dubey, Karunakar Kar. Ageing Res Rev 2019
25
2
11

Physical Determinants of Amyloid Assembly in Biofilm Formation.
Maria Andreasen, Georg Meisl, Jonathan D Taylor, Thomas C T Michaels, Aviad Levin, Daniel E Otzen, Matthew R Chapman, Christopher M Dobson, Steve J Matthews, Tuomas P J Knowles. mBio 2019
44
2
11

Seeding specificity in amyloid growth induced by heterologous fibrils.
Brian O'Nuallain, Angela D Williams, Per Westermark, Ronald Wetzel. J Biol Chem 2004
315
2
11

Amyloid-like fibril elongation follows michaelis-menten kinetics.
Katazyna Milto, Akvile Botyriute, Vytautas Smirnovas. PLoS One 2013
14
2
14

High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates.
Takahiro Watanabe-Nakayama, Kenjiro Ono, Masahiro Itami, Ryoichi Takahashi, David B Teplow, Masahito Yamada. Proc Natl Acad Sci U S A 2016
121
2
11

Polymorph-specific kinetics and thermodynamics of β-amyloid fibril growth.
Wei Qiang, Kevin Kelley, Robert Tycko. J Am Chem Soc 2013
117
2
11

Cryo-EM structures of tau filaments from Alzheimer's disease.
Anthony W P Fitzpatrick, Benjamin Falcon, Shaoda He, Alexey G Murzin, Garib Murshudov, Holly J Garringer, R Anthony Crowther, Bernardino Ghetti, Michel Goedert, Sjors H W Scheres. Nature 2017
977
2
11

Fibril structure of amyloid-β(1-42) by cryo-electron microscopy.
Lothar Gremer, Daniel Schölzel, Carla Schenk, Elke Reinartz, Jörg Labahn, Raimond B G Ravelli, Markus Tusche, Carmen Lopez-Iglesias, Wolfgang Hoyer, Henrike Heise,[...]. Science 2017
514
2
11

polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction.
Anusri M Bhattacharyya, Ashwani K Thakur, Ronald Wetzel. Proc Natl Acad Sci U S A 2005
127
2
11

Branching in amyloid fibril growth.
Christian Beyschau Andersen, Hisashi Yagi, Mauro Manno, Vincenzo Martorana, Tadato Ban, Gunna Christiansen, Daniel Erik Otzen, Yuji Goto, Christian Rischel. Biophys J 2009
108
2
11

Cryo-EM structure of alpha-synuclein fibrils.
Ricardo Guerrero-Ferreira, Nicholas Mi Taylor, Daniel Mona, Philippe Ringler, Matthias E Lauer, Roland Riek, Markus Britschgi, Henning Stahlberg. Elife 2018
284
2
11

Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies.
Aaron Ciechanover, Yong Tae Kwon. Exp Mol Med 2015
470
2
11

Purification and analysis of prion and amyloid aggregates.
Vitaly V Kushnirov, Ilya M Alexandrov, Olga V Mitkevich, Irina S Shkundina, Michael D Ter-Avanesyan. Methods 2006
64
2
11

Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes.
F W Studier, B A Moffatt. J Mol Biol 1986
5448
2
11

Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].
Y O Chernoff, S L Lindquist, B Ono, S G Inge-Vechtomov, S W Liebman. Science 1995
853
2
11

Prions in yeast.
Susan W Liebman, Yury O Chernoff. Genetics 2012
281
2
11

Protein misfolding, evolution and disease.
C M Dobson. Trends Biochem Sci 1999
1429
2
11

Trafficking and proteolytic processing of APP.
Christian Haass, Christoph Kaether, Gopal Thinakaran, Sangram Sisodia. Cold Spring Harb Perspect Med 2012
655
2
11

Initiation and synergistic fibrillization of tau and alpha-synuclein.
Benoit I Giasson, Mark S Forman, Makoto Higuchi, Lawrence I Golbe, Charles L Graves, Paul T Kotzbauer, John Q Trojanowski, Virginia M-Y Lee. Science 2003
638
2
11

The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosis.
Jixi Li, Thomas McQuade, Ansgar B Siemer, Johanna Napetschnig, Kenta Moriwaki, Yu-Shan Hsiao, Ermelinda Damko, David Moquin, Thomas Walz, Ann McDermott,[...]. Cell 2012
745
2
11

Co-aggregation of pro-inflammatory S100A9 with α-synuclein in Parkinson's disease: ex vivo and in vitro studies.
Istvan Horvath, Igor A Iashchishyn, Roman A Moskalenko, Chao Wang, Sebastian K T S Wärmländer, Cecilia Wallin, Astrid Gräslund, Gabor G Kovacs, Ludmilla A Morozova-Roche. J Neuroinflammation 2018
29
2
11

From macroscopic measurements to microscopic mechanisms of protein aggregation.
Samuel I A Cohen, Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles. J Mol Biol 2012
302
2
11

Structural Insights into α-Synuclein Fibril Polymorphism: Effects of Parkinson's Disease-Related C-Terminal Truncations.
Xiaodan Ni, Ryan P McGlinchey, Jiansen Jiang, Jennifer C Lee. J Mol Biol 2019
63
2
11

Cross-seeding effects of amyloid β-protein and α-synuclein.
Kenjiro Ono, Ryoichi Takahashi, Tokuhei Ikeda, Masahito Yamada. J Neurochem 2012
135
2
11

Cryo-EM structure of full-length α-synuclein amyloid fibril with Parkinson's disease familial A53T mutation.
Yunpeng Sun, Shouqiao Hou, Kun Zhao, Houfang Long, Zhenying Liu, Jing Gao, Yaoyang Zhang, Xiao-Dong Su, Dan Li, Cong Liu. Cell Res 2020
55
2
11

Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs.
David R Boyer, Binsen Li, Chuanqi Sun, Weijia Fan, Michael R Sawaya, Lin Jiang, David S Eisenberg. Nat Struct Mol Biol 2019
78
2
11


Co-cited is the co-citation frequency, indicating how many articles cite the article together with the query article. Similarity is the co-citation as percentage of the times cited of the query article or the article in the search results, whichever is the lowest. These numbers are calculated for the last 100 citations when articles are cited more than 100 times.

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