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For: Sharma S, Modi P, Sharma G, Deep S. Kinetics theories to understand the mechanism of aggregation of a protein and to design strategies for its inhibition. Biophys Chem 2021;278:106665. [PMID: 34419715 DOI: 10.1016/j.bpc.2021.106665] [Cited by in Crossref: 20] [Cited by in F6Publishing: 21] [Article Influence: 20.0] [Reference Citation Analysis]
Number Citing Articles
1 Nirwal S, Saravanan P, Bajpai A, Meshram VD, Raju G, Deeksha W, Prabusankar G, Patel BK. In Vitro Interaction of a C-Terminal Fragment of TDP-43 Protein with Human Serum Albumin Modulates Its Aggregation. J Phys Chem B 2022. [DOI: 10.1021/acs.jpcb.2c04469] [Reference Citation Analysis]
2 Kumari M, Sharma S, Deep S. Tetrabutylammonium based ionic liquids (ILs) inhibit the amyloid aggregation of superoxide dismutase 1 (SOD1). Journal of Molecular Liquids 2022;353:118761. [DOI: 10.1016/j.molliq.2022.118761] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
3 Beasley M, Frazee N, Groover S, Valentine SJ, Mertz B, Legleiter J. Physicochemical Properties Altered by the Tail Group of Lipid Membranes Influence Huntingtin Aggregation and Lipid Binding. J Phys Chem B 2022. [PMID: 35439000 DOI: 10.1021/acs.jpcb.1c10254] [Reference Citation Analysis]
4 Chakrabarti P, Chakravarty D. Intrinsically disordered proteins/regions and insight into their biomolecular interactions. Biophysical Chemistry 2022;283:106769. [DOI: 10.1016/j.bpc.2022.106769] [Cited by in Crossref: 6] [Cited by in F6Publishing: 7] [Article Influence: 6.0] [Reference Citation Analysis]
5 Dharmaraj GL, Arigo FD, Young KA, Martins R, Mancera RL, Bharadwaj P. Novel Amylin Analogues Reduce Amyloid-β Cross-Seeding Aggregation and Neurotoxicity. J Alzheimers Dis 2022. [PMID: 35275530 DOI: 10.3233/JAD-215339] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
6 Lye YS, Chen YR. TAR DNA-binding protein 43 oligomers in physiology and pathology. IUBMB Life 2022. [PMID: 35229461 DOI: 10.1002/iub.2603] [Reference Citation Analysis]
7 Zhang S, Yoo S, Snyder DT, Katz BB, Henrickson A, Demeler B, Wysocki VH, Kreutzer AG, Nowick JS. A Disulfide-Stabilized Aβ that Forms Dimers but Does Not Form Fibrils. Biochemistry 2022. [PMID: 35080857 DOI: 10.1021/acs.biochem.1c00739] [Reference Citation Analysis]
8 Rasmussen HØ, Otzen DE, Pedersen JS. Induction, inhibition, and incorporation: Different roles for anionic and zwitterionic lysolipids in the fibrillation of the functional amyloid FapC. J Biol Chem 2022;:101569. [PMID: 35007533 DOI: 10.1016/j.jbc.2022.101569] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
9 Tang H, Li Y, Kakinen A, Andrikopoulos N, Sun Y, Kwak E, Davis TP, Ding F, Ke PC. Graphene quantum dots obstruct the membrane axis of Alzheimer's amyloid beta. Phys Chem Chem Phys 2021;24:86-97. [PMID: 34878460 DOI: 10.1039/d1cp04246g] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 3.0] [Reference Citation Analysis]
10 Ben-Zichri S, Malishev R, Oren O, Bloch DN, Taube R, Papo N, Jelinek R. Bcl-2-Homology-Only Proapoptotic Peptides Modulate β-Amyloid Aggregation and Toxicity. ACS Chem Neurosci 2021;12:4554-63. [PMID: 34806861 DOI: 10.1021/acschemneuro.1c00611] [Reference Citation Analysis]
11 Fritzsch J, Korn A, Surendran D, Krueger M, Scheidt HA, Mote KR, Madhu PK, Maiti S, Huster D. Probing the Influence of Single-Site Mutations in the Central Cross-β Region of Amyloid β (1-40) Peptides. Biomolecules 2021;11:1848. [PMID: 34944492 DOI: 10.3390/biom11121848] [Reference Citation Analysis]
12 Zhang Q, Wang B, Zhang Y, Yang J, Deng B, Ding B, Zhong D. Probing Intermolecular Interactions of Amyloidogenic Fragments of SOD1 by Site-Specific Tryptophan and Its Noncanonical Derivative. J Phys Chem B 2021;125:13088-98. [PMID: 34812635 DOI: 10.1021/acs.jpcb.1c07175] [Cited by in F6Publishing: 1] [Reference Citation Analysis]
13 Gadhe L, Sakunthala A, Mukherjee S, Gahlot N, Bera R, Sawner AS, Kadu P, Maji SK. Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis. Biophys Chem 2021;281:106736. [PMID: 34923391 DOI: 10.1016/j.bpc.2021.106736] [Cited by in Crossref: 10] [Cited by in F6Publishing: 9] [Article Influence: 10.0] [Reference Citation Analysis]
14 Pomier KM, Ahmed R, Melacini G. Interactions of intrinsically disordered proteins with the unconventional chaperone human serum albumin: From mechanisms of amyloid inhibition to therapeutic opportunities. Biophysical Chemistry 2021. [DOI: 10.1016/j.bpc.2021.106743] [Cited by in Crossref: 3] [Cited by in F6Publishing: 4] [Article Influence: 3.0] [Reference Citation Analysis]
15 Tang Y, Zhang D, Gong X, Zheng J. A mechanistic survey of Alzheimer's disease. Biophys Chem 2021;281:106735. [PMID: 34894476 DOI: 10.1016/j.bpc.2021.106735] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 6.0] [Reference Citation Analysis]
16 Ahmad A, Mishra R. Differential effect of polyol and sugar osmolytes on the refolding of homologous alpha amylases: A comparative study. Biophys Chem 2021;281:106733. [PMID: 34864226 DOI: 10.1016/j.bpc.2021.106733] [Cited by in Crossref: 4] [Cited by in F6Publishing: 3] [Article Influence: 4.0] [Reference Citation Analysis]
17 Krishnarjuna B, Ivanova MI, Ramamoorthy A. Aggregation and the Intrinsic Structural Disorder of Dipeptide Repeat Peptides of C9orf72-Related Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Characterized by NMR. J Phys Chem B 2021;125:12446-56. [PMID: 34751579 DOI: 10.1021/acs.jpcb.1c08149] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]
18 Shukla S, Agarwal P, Kumar A. Disordered regions tune order in chromatin organization and function. Biophys Chem 2021;281:106716. [PMID: 34844028 DOI: 10.1016/j.bpc.2021.106716] [Cited by in Crossref: 5] [Cited by in F6Publishing: 6] [Article Influence: 5.0] [Reference Citation Analysis]
19 Lewkowicz E, Gursky O. Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis. Biophys Chem 2022;280:106699. [PMID: 34773861 DOI: 10.1016/j.bpc.2021.106699] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
20 Prabhu MPT, Sarkar N. Inhibitory effects of carbon quantum dots towards hen egg white lysozyme amyloidogenesis through formation of a stable protein complex. Biophys Chem 2022;280:106714. [PMID: 34749221 DOI: 10.1016/j.bpc.2021.106714] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 2.0] [Reference Citation Analysis]