Research graph
References from Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches. Local targets link to admitted publications; unresolved targets remain external evidence.
Protein aggregation-pathways and influencing factors
10.1016/j.ijpharm.2010.02.025 · 2010 · External reference
10.1126/science.181.4096.223
10.1126/science.181.4096.223 · External reference
10.1016/s1359-0278(98)00002-9
10.1016/s1359-0278(98)00002-9 · External reference
10.1016/j.abb.2007.05.015
10.1016/j.abb.2007.05.015 · External reference
Molecular chaperone functions of heat-shock proteins
10.1146/annurev.bi.62.070193.002025 · 1993 · External reference
The role of molecular chaperones in protein folding
10.1096/fasebj.9.15.8529835 · 1995 · External reference
Ultrastructural studies in Alzheimer’s presenile dementia
1964 · External reference
10.1016/s0925-4439(00)00029-6
10.1016/s0925-4439(00)00029-6 · External reference
10.1126/science.276.5321.2045
10.1126/science.276.5321.2045 · External reference
10.1146/annurev-biochem-061516-045115
10.1146/annurev-biochem-061516-045115 · External reference
10.1146/annurev.biochem.75.101304.123901
10.1146/annurev.biochem.75.101304.123901 · External reference
Outline of a theory of cellular heterogeneity
10.1073/pnas.81.16.5126 · 1984 · External reference
10.1016/j.sbi.2020.05.006
10.1016/j.sbi.2020.05.006 · External reference
10.1126/science.aar5839
10.1126/science.aar5839 · External reference
Single-molecule fluorescence microscopy review: shedding new light on old problems
10.1042/bsr20170031 · 2017 · External reference
10.1016/j.bbrc.2005.06.025
10.1016/j.bbrc.2005.06.025 · External reference
10.1016/j.copbio.2010.10.002
10.1016/j.copbio.2010.10.002 · External reference
Watching cellular machinery in action, one molecule at a time
10.1083/jcb.201610025 · 2016 · External reference
10.1134/s0006297914130057
10.1134/s0006297914130057 · External reference
10.1038/nature03680
10.1038/nature03680 · External reference
10.1016/j.sbi.2019.09.001
10.1016/j.sbi.2019.09.001 · External reference
10.1038/s41586-019-1026-5
10.1038/s41586-019-1026-5 · External reference
10.1038/nature05695
10.1038/nature05695 · External reference
10.1016/0003-2697(89)90046-8
10.1016/0003-2697(89)90046-8 · External reference
Molecular Rotors: what lies behind the high sensitivity of the Thioflavin-T fluorescent marker
10.1021/ar300053p · 2012 · External reference
10.1021/bi002555c
10.1021/bi002555c · External reference
alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease
10.1074/jbc.274.28.19509 · 1999 · External reference
10.4161/pri.28125
10.4161/pri.28125 · External reference
10.1039/c6tb00319b
10.1039/c6tb00319b · External reference
10.1073/pnas.1315346111
10.1073/pnas.1315346111 · External reference
The protofilament structure of insulin amyloid fibrils
10.1073/pnas.142459399 · 2002 · External reference
10.1016/j.jmb.2008.11.005
10.1016/j.jmb.2008.11.005 · External reference
10.1038/s41467-018-03164-5
10.1038/s41467-018-03164-5 · External reference
From the polymorphism of amyloid fibrils to their assembly mechanism and cytotoxicity
10.1016/s0065-3233(06)73007-8 · 2006 · External reference
10.1021/acs.jpcb.7b10233
10.1021/acs.jpcb.7b10233 · External reference
10.1016/j.sbi.2019.05.003
10.1016/j.sbi.2019.05.003 · External reference
10.1126/science.aao2825
10.1126/science.aao2825 · External reference
Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy
2018 · External reference
10.1002/ana.10795
10.1002/ana.10795 · External reference
10.1111/jnc.12806
10.1111/jnc.12806 · External reference
10.1038/s41467-019-12683-8
10.1038/s41467-019-12683-8 · External reference
10.1073/pnas.1100976108
10.1073/pnas.1100976108 · External reference
Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy
10.1073/pnas.97.2.571 · 2000 · External reference
10.1039/c9sc06501f
10.1039/c9sc06501f · External reference
Kinetic diversity of amyloid oligomers
10.1073/pnas.1922267117 · 2020 · External reference
10.1021/jacs.7b10439
10.1021/jacs.7b10439 · External reference
Insight into the structure of amyloid fibrils from the analysis of globular proteins
10.1371/journal.pcbi.0020170 · 2006 · External reference
10.1063/1.3608917
10.1063/1.3608917 · External reference
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
10.1073/pnas.1218402110 · 2013 · External reference
Dynamics of protein aggregation and oligomer formation governed by secondary nucleation
10.1063/1.4927655 · 2015 · External reference
Toxic species in amyloid disorders: oligomers or mature fibrils
10.4103/0972-2327.144284 · 2015 · External reference
10.1007/s12551-017-0289-z
10.1007/s12551-017-0289-z · External reference
10.1073/pnas.2002956117
10.1073/pnas.2002956117 · External reference
Molecular insights into the surface-catalyzed secondary nucleation of amyloid-β40 (Aβ40) by the peptide fragment Aβ16–22
10.1126/sciadv.aav8216 · 2019 · External reference
10.1021/acschemneuro.9b00594
10.1021/acschemneuro.9b00594 · External reference
10.1126/sciadv.1700488
10.1126/sciadv.1700488 · External reference
10.1038/nrm3810
10.1038/nrm3810 · External reference
10.4161/pri.4.1.11378
10.4161/pri.4.1.11378 · External reference
10.1126/science.1178250
10.1126/science.1178250 · External reference
10.1021/acschemneuro.8b00094
10.1021/acschemneuro.8b00094 · External reference
10.1016/j.isci.2020.101512
10.1016/j.isci.2020.101512 · External reference
Length dependence of rate constants for end-to-end association and dissociation of equilibrium linear aggregates
10.1016/s0006-3495(83)84301-x · 1983 · External reference
10.1074/jbc.m116.734707
10.1074/jbc.m116.734707 · External reference
The aggregation conditions define whether EGCG is an inhibitor or enhancer of α-synuclein amyloid fibril formation
10.3390/ijms21061995 · 2020 · External reference
10.1515/pac-2018-1017
10.1515/pac-2018-1017 · External reference
10.1159/000109760
10.1159/000109760 · External reference
10.1016/s0092-8674(00)81223-4
10.1016/s0092-8674(00)81223-4 · External reference
10.1038/s41586-020-2904-6
10.1038/s41586-020-2904-6 · External reference
10.1074/jbc.ra120.013478
10.1074/jbc.ra120.013478 · External reference
10.1016/j.molcel.2015.07.012
10.1016/j.molcel.2015.07.012 · External reference
10.1091/mbc.e15-10-0693
10.1091/mbc.e15-10-0693 · External reference
10.1073/pnas.1903268116
10.1073/pnas.1903268116 · External reference
Protein-remodeling factors as potential therapeutics for neurodegenerative disease
2017 · External reference
The HSP110/HSP70 disaggregation system generates spreading-competent toxic α-synuclein species
10.15252/embj.2019103954 · 2020 · External reference
10.1371/journal.pone.0026319
10.1371/journal.pone.0026319 · External reference
10.1021/acs.analchem.5b01811
10.1021/acs.analchem.5b01811 · External reference
10.1016/j.cell.2012.03.037
10.1016/j.cell.2012.03.037 · External reference
Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson’s disease genetically related mutants
10.1038/srep16696 · 2015 · External reference
Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones
10.1021/bi301277k · 2012 · External reference
The structure of amyloid fibrils by electron microscopy and X-ray diffraction
10.1016/s0065-3233(08)60320-4 · 1997 · External reference
Structural polymorphism of amyloid oligomers and fibrils underlies different fibrillization pathways: immunogenicity and cytotoxicity
10.2174/138920310791330631 · 2010 · External reference
Alpha-synuclein structure and Parkinson’s disease – lessons and emerging principles
10.1186/s13024-019-0329-1 · 2019 · External reference
10.1038/s41467-019-13564-w
10.1038/s41467-019-13564-w · External reference
10.1126/science.1116702
10.1126/science.1116702 · External reference
10.1126/science.282.5395.1877
10.1126/science.282.5395.1877 · External reference
Two-step amyloid aggregation: sequential lag phase intermediates
10.1038/srep40065 · 2017 · External reference
10.1016/j.bbagen.2019.05.005
10.1016/j.bbagen.2019.05.005 · External reference
10.1039/c1cs15113d
10.1039/c1cs15113d · External reference
Aggregation-induced emission of 1-methyl-1,2,3,4,5-pentaphenylsilole
10.1039/b105159h · 2001 · External reference
10.1038/3311
10.1038/3311 · External reference
Initiation and propagation of α-synuclein aggregation in the nervous system
10.1186/s13024-020-00368-6 · 2020 · External reference
Basic confocal microscopy
10.1002/0471142727.mb1411s81 · 2008 · External reference
10.1117/1.jbo.25.7.071203
10.1117/1.jbo.25.7.071203 · External reference
10.1016/b978-0-12-809283-5.00723-0
10.1016/b978-0-12-809283-5.00723-0 · 2005 · External reference
10.1364/ol.22.001905
10.1364/ol.22.001905 · External reference
10.1021/acsnano.0c07322
10.1021/acsnano.0c07322 · External reference
Real-time detection of single molecules in solution by confocal fluorescence microscopy
10.1021/ac00113a019 · 1995 · External reference
10.1038/s41592-018-0291-9
10.1038/s41592-018-0291-9 · External reference
Total Internal Reflection Fluorescence (TIRF) Microscopy
2009 · External reference
10.1016/j.celrep.2017.01.043
10.1016/j.celrep.2017.01.043 · External reference
10.1042/bst0380914
10.1042/bst0380914 · External reference
An alternative framework for fluorescence correlation spectroscopy
10.1038/s41467-019-11574-2 · 2019 · External reference
Total internal inflection fluorescent microscopy
10.1111/j.1365-2818.1983.tb04158.x · 1983 · External reference
10.1247/csf.27.357
10.1247/csf.27.357 · External reference
10.3791/3892
10.3791/3892 · External reference
10.1002/adma.201401356
10.1002/adma.201401356 · External reference
10.1021/acs.analchem.7b02090
10.1021/acs.analchem.7b02090 · External reference
10.1021/acschemneuro.0c00478
10.1021/acschemneuro.0c00478 · External reference
Aggregation-induced emission: phenomenon, mechanism and applications
10.1039/b904665h · 2009 · External reference
10.1016/j.bbapap.2016.07.007
10.1016/j.bbapap.2016.07.007 · External reference
10.1126/science.283.5408.1676
10.1126/science.283.5408.1676 · External reference
10.1074/jbc.m117.813865
10.1074/jbc.m117.813865 · External reference
10.1016/j.jmb.2004.09.078
10.1016/j.jmb.2004.09.078 · External reference
10.1021/ar050074l
10.1021/ar050074l · External reference
10.1016/0003-2697(87)90157-6
10.1016/0003-2697(87)90157-6 · External reference
10.1021/acs.nanolett.8b02916
10.1021/acs.nanolett.8b02916 · External reference
Spectroscopic studies of nile red in organic solvents and polymers
10.1016/1010-6030(95)04140-0 · 1996 · External reference
Nile red fluorescence for quantitative monitoring of micropolarity and microviscosity of pluronic F127 in aqueous media
10.1039/c6pp00123h · 2016 · External reference
10.1016/j.celrep.2018.05.074
10.1016/j.celrep.2018.05.074 · External reference
Single-molecule imaging of individual amyloid protein aggregates in human biofluids
10.1021/acschemneuro.5b00324 · 2016 · External reference
Fluorescence quantum yield of thioflavin T in rigid isotropic solution and incorporated into the amyloid fibrils
10.1371/journal.pone.0015385 · 2010 · External reference
Metachromatic properties of amyloid in solution
10.1177/17.4.258 · 1969 · External reference
10.1038/s41467-019-09477-3
10.1038/s41467-019-09477-3 · External reference
Interaction of thioflavin T with amyloid fibrils: fluorescence quantum yield of bound dye
10.1021/jp2083055 · 2012 · External reference
Origin of the stokes shift: a geometrical model of exciton spectra in 2D semiconductors
10.1103/physrevlett.70.323 · 1993 · External reference
The structure and protein binding of amyloid-specific dye reagents
10.18388/abp.2003_3645 · 2003 · External reference
Computational study of Thioflavin T torsional relaxation in the excited state
2007 · External reference
10.1007/s12154-013-0094-5
10.1007/s12154-013-0094-5 · External reference
10.1016/j.bpj.2018.12.010
10.1016/j.bpj.2018.12.010 · External reference
10.1016/j.chembiol.2012.02.003
10.1016/j.chembiol.2012.02.003 · External reference
Amyloid-β oligomerization monitored by single-molecule stepwise photobleaching
10.1016/j.ymeth.2020.06.007 · 2020 · External reference
Polyphenolic biflavonoids inhibit amyloid-β fibrillation and disaggregate preformed amyloid-β fibrils
10.4062/biomolther.2019.113 · 2020 · External reference
10.1016/j.febslet.2011.03.046
10.1016/j.febslet.2011.03.046 · External reference
Natural polyphenols effects on protein aggregates in Alzheimer's and Parkinson's prion-like diseases
10.4103/1673-5374.233432 · 2018 · External reference
Photobleaching of organic fluorophores: quantitative characterization, mechanisms, protection
2020 · External reference
Unresolved reference
2013 · External reference
10.1529/biophysj.107.117689
10.1529/biophysj.107.117689 · External reference
Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules
10.1021/bi00745a020 · 1973 · External reference
Inferring subunit stoichiometry from single molecule photobleaching
10.1085/jgp.201310988 · 2013 · External reference
10.1002/cphc.201301092
10.1002/cphc.201301092 · External reference
Determination of the oligomer size of amyloidogenic protein β-amyloid(1–40) by single-molecule spectroscopy
10.1016/j.bpj.2009.05.035 · 2009 · External reference
Direct observation of single amyloid-β(1–40) oligomers on live cells: binding and growth at physiological concentrations
10.1371/journal.pone.0023970 · 2011 · External reference
Automatic classification and segmentation of single-molecule fluorescence time traces with deep learning
10.1038/s41467-020-19673-1 · 2020 · External reference
Correction of systematic bias in single molecule photobleaching measurements
10.1016/j.bpj.2019.12.034 · 2020 · External reference
10.1039/d0cp00450b
10.1039/d0cp00450b · External reference
10.1073/pnas.0803086105
10.1073/pnas.0803086105 · External reference
10.1021/ac061122y
10.1021/ac061122y · External reference
10.1038/nsmb.2191
10.1038/nsmb.2191 · External reference
10.1021/ja1117123
10.1021/ja1117123 · External reference
The off-rate of monomers dissociating from amyloid-β protofibrils
10.1074/jbc.m113.513432 · 2013 · External reference
10.1016/j.ymeth.2014.01.010
10.1016/j.ymeth.2014.01.010 · External reference
Using fluorescence correlation spectroscopy to study conformational changes in denatured proteins
10.1529/biophysj.107.120220 · 2008 · External reference
10.1002/bies.10118
10.1002/bies.10118 · External reference
Fluorescence Correlation Spectroscopy: A tool to study protein oligomerization and aggregation in vitro and in vivo
10.1007/978-1-4939-2978-8_5 · 2015 · External reference
Ultrasensitive detection and identification of fluorescent molecules by FCS: Impact for immunobiology
10.1073/pnas.181337998 · 2001 · External reference
10.3390/ijms19040964
10.3390/ijms19040964 · External reference
Fluorescence correlation spectroscopy: molecular complexing in solution and in living cells
10.1016/b978-0-12-407761-4.00021-x · 2013 · External reference
Hydrodynamic radii and diffusion coefficients of particle aggregates derived from the bead model
10.1016/j.jcis.2010.03.066 · 2010 · External reference
10.1038/nrneurol.2012.263
10.1038/nrneurol.2012.263 · External reference
Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution
10.1038/s41598-018-37584-6 · 2019 · External reference
10.2976/1.2760023
10.2976/1.2760023 · External reference
10.1074/jbc.m109.069542
10.1074/jbc.m109.069542 · External reference
10.1038/srep00700
10.1038/srep00700 · External reference
10.1042/bj20150159
10.1042/bj20150159 · External reference
Rapid acquisition of β-sheet structure in the prion protein prior to multimer formation
10.1515/bchm.1998.379.11.1307 · 1998 · External reference
10.1016/s1074-5521(99)80020-9
10.1016/s1074-5521(99)80020-9 · External reference
Measuring size distribution in highly heterogeneous systems with fluorescence correlation spectroscopy
10.1016/s0006-3495(03)75006-1 · 2003 · External reference
Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change
10.1016/j.bpj.2009.12.4290 · 2010 · External reference
Fluorescence correlation spectroscopy for particle sizing in highly concentrated protein solutions
10.1007/978-1-4939-9678-0_12 · 2019 · External reference
10.1038/s41598-018-19961-3
10.1038/s41598-018-19961-3 · External reference
10.1021/ar0401348
10.1021/ar0401348 · External reference
10.1073/pnas.0401690101
10.1073/pnas.0401690101 · External reference
Pulsed interleaved excitation-based line-scanning spatial correlation spectroscopy (PIE-lsSCS)
10.1038/s41598-018-35146-4 · 2018 · External reference
10.1529/biophysj.105.064766
10.1529/biophysj.105.064766 · External reference
10.3390/ijms13089400
10.3390/ijms13089400 · External reference
Energy migration and fluorescence. 1946
10.1117/1.jbo.17.1.011002 · 2012 · External reference
10.3390/s16091488
10.3390/s16091488 · External reference
10.1146/annurev-biochem-072909-094736
10.1146/annurev-biochem-072909-094736 · External reference
10.1016/j.sbi.2017.03.010
10.1016/j.sbi.2017.03.010 · External reference
10.1038/s41592-018-0085-0
10.1038/s41592-018-0085-0 · External reference
Immobilization of proteins for single-molecule fluorescence resonance energy transfer measurements of conformation and dynamics
10.1007/978-1-4614-3704-8_1 · 2012 · External reference
Efficient use of single molecule time traces to resolve kinetic rates, models and uncertainties
10.1063/1.5006604 · 2017 · External reference
Confocal single-molecule FRET for protein conformational dynamics
10.1007/978-1-62703-658-0_3 · 2014 · External reference
10.1007/s12551-017-0366-3
10.1007/s12551-017-0366-3 · External reference
10.1021/bi010616g
10.1021/bi010616g · External reference
10.1371/journal.pone.0012529
10.1371/journal.pone.0012529 · External reference
10.1371/journal.pbio.2006660
10.1371/journal.pbio.2006660 · External reference
Single-molecule interaction microscopy reveals antibody binding kinetics
2020 · External reference
10.3390/molecules24030491
10.3390/molecules24030491 · External reference
10.1016/j.jmb.2018.05.021
10.1016/j.jmb.2018.05.021 · External reference
10.1021/cr400326k
10.1021/cr400326k · External reference
10.1016/j.bbrc.2006.10.085
10.1016/j.bbrc.2006.10.085 · External reference
10.1038/42166
10.1038/42166 · External reference
10.1038/nrn1587
10.1038/nrn1587 · External reference
10.1126/science.1067389
10.1126/science.1067389 · External reference
10.1006/nbdi.2001.0443
10.1006/nbdi.2001.0443 · External reference
10.1021/acschembio.7b01039
10.1021/acschembio.7b01039 · External reference
Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro
10.1074/jbc.m208926200 · 2002 · External reference
10.1074/jbc.rev118.002809
10.1074/jbc.rev118.002809 · External reference
A novel mechanism for small heat shock proteins to function as molecular chaperones
10.1038/srep08811 · 2015 · External reference
Single-molecule fluorescence-based approach reveals novel mechanistic insights into human small heat shock protein chaperone function
10.1074/jbc.ra120.015419 · 2021 · External reference
10.1096/fj.06-7986com
10.1096/fj.06-7986com · External reference
10.1016/0006-8993(91)91092-f
10.1016/0006-8993(91)91092-f · External reference
Cerebral amyloid angiopathy in the brains of patients with Alzheimer's disease: the CERAD experience, Part XV
10.1212/wnl.46.6.1592 · 1996 · External reference
Apolipoprotein E epsilon 4 allele as a major risk factor for sporadic early and late-onset forms of Alzheimer's disease: analysis of the 19q13.2 chromosomal region
10.1093/hmg/3.4.569 · 1994 · External reference
10.1074/jbc.m112.411900
10.1074/jbc.m112.411900 · External reference
10.1021/bi5008172
10.1021/bi5008172 · External reference
10.1007/s12035-020-01873-x
10.1007/s12035-020-01873-x · External reference
10.1371/journal.pbio.1001346
10.1371/journal.pbio.1001346 · External reference
10.1016/j.molcel.2015.07.012
10.1016/j.molcel.2015.07.012 · External reference
10.1073/pnas.0510496103
10.1073/pnas.0510496103 · External reference
10.3390/ijms20092334
10.3390/ijms20092334 · External reference
10.1371/journal.pone.0012270
10.1371/journal.pone.0012270 · External reference
10.1038/s41467-020-17149-w
10.1038/s41467-020-17149-w · External reference
