Research Topics
| Hilal A LashuelSummaryAffiliation: Harvard University Country: USA Publications
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Detail Information
Publications
In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synucleinHilal A Lashuel
Center for Neurologic Diseases, Brigham and Women's Hospital and Department of Neurology, Harvard Medical School, Boston, MA, USA
Methods Mol Biol 299:19-33. 2005....- New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's diseaseHilal A Lashuel
Center for Neurologic Diseases, Brigham and Women s Hospital and Department of Neurology, Harvard Medical School, Cambridge, Massachusetts 02139, USA
J Biol Chem 277:42881-90. 2002..The inhibitory properties of the compounds presented suggest a new class of small molecules that could serve as a scaffold for the design of more efficient inhibitors of Abeta amyloidogenesis in vivo... - Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid poresHilal A Lashuel
Harvard Center for Neurodegeneration and Repair, 65 Landsdowne St, Cambridge, MA 02139, USA
J Mol Biol 332:795-808. 2003..An increase in the ratio of Abeta(WT)/Abeta(MUT(Arctic)), therefore, may result in the accumulation of potential neurotoxic protofibrils and acceleration of disease progression in familial Alzheimer's disease mutation carriers... - Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrilsHilal A Lashuel
Center for Neurologic Diseases, Brigham and Women s Hospital and Department of Neurology, Harvard Medical School, Cambridge, MA 02139, USA
J Mol Biol 322:1089-102. 2002..The formation of pore-like oligomeric structures may explain the membrane permeabilization activity of alpha-synuclein protofibrils. These structures may contribute to the pathogenesis of PD... - The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric statesRoss A Fredenburg
Center for Neurologic Diseases, Brigham and Women s Hospital and Department of Neurology, Harvard Medical School, 65 Landsdowne Street, Cambridge, Massachusetts 02139, USA
Biochemistry 46:7107-18. 2007.... - Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactionsTerunaga Nakagawa
The Picower Center for Learning and Memory, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA
Neuron 44:453-67. 2004..Thus SAP97 has a broader role than its close relative, PSD-95, in the maintenance of synaptic function... - Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's diseaseJean Christophe Rochet
Center for Neurologic Diseases, Brigham and Women s Hospital, Department of Neurology, Harvard Medical School, Cambridge, MA 02139, USA
J Mol Neurosci 23:23-34. 2004..These variants might be useful to test whether membrane binding by alpha-synuclein is necessary for neurodegeneration in transgenic animal models of PD... - A century-old debate on protein aggregation and neurodegeneration enters the clinicPeter T Lansbury
Department of Neurology, Harvard Medical School and Brigham and Women s Hospital, 65 Landsdowne Street, Cambridge, Massachusetts 02139, USA
Nature 443:774-9. 2006..The clinical trials could also settle the century-old debate about causality... - Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell lineYichin Liu
Center for Neurologic Diseases, Brigham and Women's Hospital, 65 Landsdowne Street, Cambridge, MA 02139, USA
Chem Biol 10:837-46. 2003..The molecular mechanism of this response remains to be determined... - The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibilityYichin Liu
Center for Neurologic Diseases, Brigham and Women s Hospital, Department of Neurology, Harvard Medical School, Cambridge, MA 02139, USA
Cell 111:209-18. 2002..Thus, the ligase activity as well as the hydrolase activity of UCH-L1 may play a role in proteasomal protein degradation, a critical process for neuronal health... - Neurodegenerative disease: amyloid pores from pathogenic mutationsHilal A Lashuel
Center for Neurologic Diseases, Brigham and Women s Hospital and Department of Neurology, Harvard Medical School, 65 Landsdowne Street, Cambridge, Massachusetts 02139, USA
Nature 418:291. 2002.... - Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesisHilal A Lashuel
Center for Neurologic Diseases, Brigham and Women's Hospital and Department of Neurology, Harvard Medical School, Boston, MA, USA
Methods Mol Biol 299:81-101. 2005..An overview of the strength and limitations of these techniques as tools for elucidating the structural basis of amyloid fibril formation will be presented... - A molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerizationGal Bitan
Center for Neurologic Diseases, Brigham and Women's Hospital, Boston, MA 02115, USA
J Am Chem Soc 125:15359-65. 2003..Preventing assembly of toxic Abeta42 paranuclei through selective oxidation of Met(35) thus represents a potential therapeutic approach for AD... - Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesisGabriele Tuchscherer
Institute of Chemical Sciences and Engineering, Ecole Polytechnique Federale de Lausanne, EPFL, CH 1015 Lausanne, Switzerland
Biopolymers 88:239-52. 2007.... - Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?Hilal A Lashuel
Laboratory of Molecular Neurobiology and Neuroproteomics, Brain Mind Institute, Ecole Polytechnique Federale de Lausanne, CH 1015 Lausanne, Switzerland
Q Rev Biophys 39:167-201. 2006..The purpose of this review is to summarize the existing supportive circumstantial evidence and to stimulate further studies designed to test the validity of this hypothesis... - Lead (Pb) exposure and its effect on APP proteolysis and Abeta aggregationMd Riyaz Basha
Department of Biomedical and Pharmaceutical Sciences, University of Rhode Island, Kingston, RI 02881, USA
FASEB J 19:2083-4. 2005..The aforementioned results provide further evidence for the developmental basis of amyloidogenesis and late-life disturbances in AD-associated proteins by environmental agents... - Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregationSidhartha M Chafekar
Neurogenetics Laboratory, Academic Medical Center, P O Box 22660, 1100 DD Amsterdam, The Netherlands
Chembiochem 8:1857-64. 2007..Our data lead us to propose that conjugates that bear multiple copies of KLVFF might be useful as therapeutic agents for the treatment of Alzheimer's disease... - Membrane permeabilization: a common mechanism in protein-misfolding diseasesHilal A Lashuel
Integrative Biosciences Institute, Laboratory of Molecular Neurobiology and Neuroproteomics, Ecole Polytechnique Federale de Lausanne EPFL, CH 1015 Lausanne, Switzerland
Sci Aging Knowledge Environ 2005:pe28. 2005..quot;.. 
Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channelLimin Wang
Department of Chemistry, Rensselaer Polytechnic Institute, 110 8th Street, Troy, NY 12180, USA
Proc Natl Acad Sci U S A 99:15947-52. 2002..1 forms a membrane channel and have important implications for understanding the 3D structure, multiple functions, and pathological roles of this highly conserved protein...- Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch conceptRichard Mimna
Institute of Chemical Sciences and Engineering, , 1015 Lausanne, Switzerland
Angew Chem Int Ed Engl 46:2681-4. 2007 - Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synucleinCristian Follmer
Instituto de Bioquimica Medica, Programa de Biologia Estrutural, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21941 590, Brazil
Biochemistry 46:472-82. 2007..These results suggest that strategies aimed at breaking and/or clearing these aggregates is promising in alleviating the symptoms of PD... - Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavitiesDebora Foguel
Departamento de Bioquimica Medica, Instituto de Ciencias Biomedicas, Universidade Federal do Rio de Janeiro, Rio de Janeiro, 21941 590, Brazil
Proc Natl Acad Sci U S A 100:9831-6. 2003..Finally, the HHP-induced formation of fibrils from TTR is relatively fast (approximately 60 min), a quality that allows screening of antiamyloidogenic drugs... - Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson's diseaseHilal A Lashuel
Laboratory of Molecular Neurobiology and Neuroproteomics, Brain Mind Institute, Ecole Polytechnique Federale de Lausanne, Station 15, CH 1015 Lausanne, Switzerland
ACS Chem Biol 1:420-4. 2006..Overexpression of proteins that are known to enhance ER-to-Golgi transport rescue defective trafficking in yeast, worm, fly, and cellular models of PD... - Abeta protofibrils possess a stable core structure resistant to hydrogen exchangeIndu Kheterpal
Graduate School of Medicine, University of Tennessee, 1924 Alcoa Highway, Knoxville, Tennessee 37920, USA
Biochemistry 42:14092-8. 2003..These and other data are interpreted and discussed in terms of the role of protofibrils in fibril assembly and in disease... - Production and characterization of astrocyte-derived human apolipoprotein E isoforms from immortalized astrocytes and their interactions with amyloid-betaMasayuki Morikawa
Department of Neurology, Washington University School of Medicine, St. Louis, MO 63130, USA
Neurobiol Dis 19:66-76. 2005..These immortalized astrocytes will be useful for studying mechanisms underlying the isoform-specific effects of apoE in the CNS... - Amyloid fibril formation by macrophage migration inhibitory factorHilal A Lashuel
Integrative Biosciences Institute, Laboratory of Molecular Neurobiology and Neuroproteomics, Swiss Federal Institute of Technology EPFL, CH 1015 Lausanne, Switzerland
Biochem Biophys Res Commun 338:973-80. 2005.... - From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperatureLimin Wang
Memorial Sloan Kettering Cancer Center, NY 10021, USA
Amyloid 12:139-48. 2005..2's inability to cause amyloidosis may be related to other factors, such as the stabilization of hexameric SAA2.2 (possibly through ligand binding), and/or the slow kinetics of aberrant misfolding and self-assembly... - Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitorsVibha B Oza
Department of Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, BCC 265, La Jolla, California 92037, USA
J Med Chem 45:321-32. 2002..High-resolution X-ray crystal structures of four of the active compounds bound to TTR were obtained. These demonstrate the significant flexibility with which TTR can accommodate ligands within its two binding sites...