An ankyrin repeat chaperone targets toxic oligomers during amyloidogenesis
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T. Chou | Arpit Gupta | S. Shan | Feng Wang | Chuqi Lu
[1] Karla P. Zepeda,et al. Efficacy and Safety of Ensovibep for Adults Hospitalized With COVID-19 , 2022, Annals of Internal Medicine.
[2] F. Lombardo,et al. Safety and Efficacy of Monoclonal Antibodies for Alzheimer’s Disease: A Systematic Review and Meta-Analysis of Published and Unpublished Clinical Trials , 2022, Journal of Alzheimer's disease : JAD.
[3] B. Grimm,et al. Chloroplast SRP43 autonomously protects chlorophyll biosynthesis proteins against heat shock , 2021, Nature Plants.
[4] A. El-Alfy,et al. Aducanumab , 2021, Reactions Weekly.
[5] S. Linse,et al. Charge Regulation during Amyloid Formation of α-Synuclein , 2021, Journal of the American Chemical Society.
[6] A. Caflisch,et al. Thermostable designed ankyrin repeat proteins (DARPins) as building blocks for innovative drugs , 2021, bioRxiv.
[7] M. Nielsen,et al. Improved prediction of HLA antigen presentation hotspots: Applications for immunogenicity risk assessment of therapeutic proteins , 2020, Immunology.
[8] C. Dobson,et al. Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies , 2020, Nature Structural & Molecular Biology.
[9] Morten Nielsen,et al. NetMHCpan-4.1 and NetMHCIIpan-4.0: improved predictions of MHC antigen presentation by concurrent motif deconvolution and integration of MS MHC eluted ligand data , 2020, Nucleic Acids Res..
[10] K. Staras,et al. Misfolded amyloid-β-42 impairs the endosomal–lysosomal pathway , 2020, Cellular and Molecular Life Sciences.
[11] J. Shorter,et al. Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations , 2020, bioRxiv.
[12] A. Plückthun,et al. Chaperone-assisted structure elucidation with DARPins. , 2020, Current opinion in structural biology.
[13] Ben A Meinen,et al. SERF engages in a fuzzy complex that accelerates primary nucleation of amyloid proteins , 2019, Proceedings of the National Academy of Sciences.
[14] B. Kuppermann,et al. Abicipar pegol: the non-monoclonal antibody anti-VEGF , 2019, Eye.
[15] Y. Sugimoto,et al. Dynamic Properties of Human α-Synuclein Related to Propensity to Amyloid Fibril Formation. , 2019, Journal of molecular biology.
[16] C. Dobson,et al. Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates , 2019, Science Advances.
[17] B. Bukau,et al. Modulation of Amyloid States by Molecular Chaperones. , 2019, Cold Spring Harbor perspectives in biology.
[18] S. Shan,et al. Substrate relay in an Hsp70‐cochaperone cascade safeguards tail‐anchored membrane protein targeting , 2018, The EMBO journal.
[19] Sandeep Kumar Dhanda,et al. Predicting HLA CD4 Immunogenicity in Human Populations , 2018, Front. Immunol..
[20] Maya A. Wright,et al. Cooperative Assembly of Hsp70 Subdomain Clusters , 2018, Biochemistry.
[21] B. Grimm,et al. Chloroplast SRP43 acts as a chaperone for glutamyl-tRNA reductase, the rate-limiting enzyme in tetrapyrrole biosynthesis , 2018, Proceedings of the National Academy of Sciences.
[22] Sandeep Kumar Dhanda,et al. Development of a strategy and computational application to select candidate protein analogues with reduced HLA binding and immunogenicity , 2018, Immunology.
[23] Karsten Melcher,et al. Amyloid beta: structure, biology and structure-based therapeutic development , 2017, Acta Pharmacologica Sinica.
[24] S. Khare,et al. A pH-dependent switch promotes β-synuclein fibril formation via glutamate residues , 2017, The Journal of Biological Chemistry.
[25] E. Wanker,et al. Amyloid-β(1–42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity * , 2016, The Journal of Biological Chemistry.
[26] Michele Vendruscolo,et al. Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation , 2016, Nature Communications.
[27] P. Wright,et al. Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release , 2016, Proceedings of the National Academy of Sciences.
[28] Michele Vendruscolo,et al. Molecular mechanisms of protein aggregation from global fitting of kinetic models , 2016, Nature Protocols.
[29] Sara Linse,et al. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides , 2014, Proceedings of the National Academy of Sciences.
[30] Michele Vendruscolo,et al. Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation , 2014, Proceedings of the National Academy of Sciences.
[31] C. Geula,et al. A Lifespan Observation of a Novel Mouse Model: In Vivo Evidence Supports Aβ Oligomer Hypothesis , 2014, PloS one.
[32] Laiq-Jan Saidi,et al. Molecular chaperones and protein folding as therapeutic targets in Parkinson’s disease and other synucleinopathies , 2013, Acta neuropathologica communications.
[33] P. Goloubinoff,et al. Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides , 2013, FEBS letters.
[34] Yujin E. Kim,et al. Molecular chaperone functions in protein folding and proteostasis. , 2013, Annual review of biochemistry.
[35] Michele Vendruscolo,et al. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism , 2013, Proceedings of the National Academy of Sciences.
[36] David A Bennett,et al. Brain amyloid-β oligomers in ageing and Alzheimer's disease. , 2013, Brain : a journal of neurology.
[37] Xiaofei Han,et al. Soluble oligomers and fibrillar species of amyloid β-peptide differentially affect cognitive functions and hippocampal inflammatory response. , 2012, Biochemical and biophysical research communications.
[38] Andreas Bracher,et al. Molecular chaperones in protein folding and proteostasis , 2011, Nature.
[39] C. Ramos,et al. An overview of the role of molecular chaperones in protein homeostasis. , 2011, Protein and peptide letters.
[40] Richard I. Morimoto,et al. Chaperone networks: Tipping the balance in protein folding diseases , 2010, Neurobiology of Disease.
[41] J. Yates,et al. Progressive accumulation of amyloid‐β oligomers in Alzheimer’s disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins , 2010, The FEBS journal.
[42] Chunjiang Yu,et al. Endocytic pathways mediating oligomeric Aβ42 neurotoxicity , 2010, Molecular Neurodegeneration.
[43] Tony Z. Jia,et al. ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP , 2010, Nature Structural &Molecular Biology.
[44] Tim D. Jones,et al. Prediction of Immunogenicity of Therapeutic Proteins , 2010, BioDrugs.
[45] Sara Linse,et al. Amyloid β-protein aggregation produces highly reproducible kinetic data and occurs by a two-phase process. , 2010, ACS chemical neuroscience.
[46] Tuomas P. J. Knowles,et al. An Analytical Solution to the Kinetics of Breakable Filament Assembly , 2009, Science.
[47] Peter M. Douglas,et al. Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways , 2009, Prion.
[48] Sara Linse,et al. A facile method for expression and purification of the Alzheimer’s disease-associated amyloid β-peptide , 2009, The FEBS journal.
[49] C. Olanow. Can we achieve neuroprotection with currently available anti-parkinsonian interventions? , 2009, Neurology.
[50] A. Schapira,et al. Why have we failed to achieve neuroprotection in Parkinson's disease? , 2008, Annals of neurology.
[51] Elizabeth A Komives,et al. Folding landscapes of ankyrin repeat proteins: experiments meet theory. , 2008, Current opinion in structural biology.
[52] P. Jaru-Ampornpan,et al. Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA. , 2007, Molecular biology of the cell.
[53] C. Dobson,et al. Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.
[54] Andreas Plückthun,et al. Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. , 2003, Journal of molecular biology.
[55] A. Plückthun,et al. A novel strategy to design binding molecules harnessing the modular nature of repeat proteins , 2003, FEBS letters.
[56] N. Hoffman,et al. The L18 Domain of Light-harvesting Chlorophyll Proteins Binds to Chloroplast Signal Recognition Particle 43* , 2000, The Journal of Biological Chemistry.
[57] M. Moore,et al. A novel precursor recognition element facilitates posttranslational binding to the signal recognition particle in chloroplasts. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[58] F. Hartl. Molecular chaperones in cellular protein folding , 1996, Nature.
[59] C. Dobson,et al. Dynamics and Control of Peptide Self-Assembly and Aggregation. , 2019, Advances in experimental medicine and biology.
[60] Michelle E. Hung,et al. Designed Ankyrin Repeat Proteins ( DARPins ) : Binding Proteins for Research , Diagnostics , and Therapy , 2015 .
[61] P. McLean,et al. Molecular chaperones in Parkinson's disease--present and future. , 2011, Journal of Parkinson's disease.
[62] Robert A. Grothe,et al. Structure of the cross-beta spine of amyloid-like fibrils. , 2005, Nature.
[63] Claudio Soto,et al. Unfolding the role of protein misfolding in neurodegenerative diseases , 2003, Nature Reviews Neuroscience.