المؤلفون: Joshi, P, Perni, M, Limbocker, R, Mannini, B, Casford, S, Chia, S, Habchi, J, Labbadia, J, Dobson, CM, Vendruscolo, M

المصدر: Communications Biology , 4 (1) , Article 843. (2021)

مصطلحات موضوعية: Molecular biology, Neuroscience

وصف الملف: text

Relation: https://discovery.ucl.ac.uk/id/eprint/10131516/1/s42003-021-02218-7.pdf; https://discovery.ucl.ac.uk/id/eprint/10131516/

الاتاحة: https://discovery.ucl.ac.uk/id/eprint/10131516/1/s42003-021-02218-7.pdf
https://discovery.ucl.ac.uk/id/eprint/10131516/

المؤلفون: Limbocker, R., Mannini, B., Ruggeri, F.S., Cascella, R., Xu, C.K., Perni, M., Chia, S., Chen, S.W., Habchi, J., Bigi, A., Kreiser, R.P., Wright, A.K., Albright, J.A., Kartanas, T., Kumita, J.R., Cremades, N., Zasloff, M., Cecchi, C., Knowles, T.P.J., Chiti, F., Vendruscolo, M., Dobson, C.M.

وصف الملف: application/pdf

Relation: http://zaguan.unizar.es/record/95470

الاتاحة: http://zaguan.unizar.es/record/95470
https://doi.org/10.1038/s42003-020-01140-8

المؤلفون: Aprile, FA, Sormanni, P, Podpolny, M, Chhangur, S, Needham, L-M, Ruggeri, FS, Perni, M, Limbocker, R, Heller, GT, Sneideris, T, Scheidt, T, Mannini, B, Habchi, J, Lee, SF, Salinas, PC, Knowles, TPJ, Dobson, CM, Vendruscolo, M

المصدر: Proceedings of the National Academy of Sciences , 117 (24) pp. 13509-13518. (2020)

مصطلحات موضوعية: Alzheimer’s disease, amyloid, protein aggregation, protein design

وصف الملف: text

Relation: https://discovery.ucl.ac.uk/id/eprint/10106995/1/13509.full.pdf; https://discovery.ucl.ac.uk/id/eprint/10106995/

الاتاحة: https://discovery.ucl.ac.uk/id/eprint/10106995/1/13509.full.pdf
https://discovery.ucl.ac.uk/id/eprint/10106995/

المؤلفون: Kalash, L, Cresser-Brown, J, Habchi, J, Morgan, C, Miller, DJ, Glen, RC, Allemann, RK, Bender, A

المصدر: 1275 ; 1264

مصطلحات موضوعية: Science & Technology, Life Sciences & Biomedicine, Chemistry, Medicinal, Pharmacology & Pharmacy, Allosteric inhibition, PEF(S), Calpain-1 inhibitors, Structure-based design, Docking, ASSAY INTERFERENCE COMPOUNDS, CALPASTATIN, DATABASE, PROTEIN, PAINS, Allosteric Regulation, Calpain, Dose-Response Relationship, Drug, Drug Design, Glycoproteins, Humans, Molecular Structure, Structure-Activity Relationship

Relation: European Journal of Medicinal Chemistry; http://hdl.handle.net/10044/1/65181; https://dx.doi.org/10.1016/j.ejmech.2018.08.049

الاتاحة: http://hdl.handle.net/10044/1/65181
https://doi.org/10.1016/j.ejmech.2018.08.049

المؤلفون: Kodera, N, Noshiro, D, Dora, S, Mori, T, Habchi, J, Blocquel, D, Gruet, A, Dosnon, M, Salladini, E, Bignon, C, Fujioka, Y, Oda, T, Noda, N, Sato, M, Lotti, M, Mizuguchi, M, Longhi, S, Ando, T, Kodera N., Noshiro D., Dora S. K., Mori T., Habchi J., Blocquel D., Gruet A., Dosnon M., Salladini E., Bignon C., Fujioka Y., Oda T., Noda N. N., Sato M., Lotti M., Mizuguchi M., Longhi S., Ando T.

مصطلحات الفهرس: Intrinsically disordered proteins, conformation, disorder to order transition, high speed atomic force microscopy, info:eu-repo/semantics/article

URL: https://hdl.handle.net/10281/295727
info:eu-repo/semantics/altIdentifier/pmid/33230318
info:eu-repo/semantics/altIdentifier/wos/WOS:000592027200001
volume:16
issue:2
firstpage:181
lastpage:189
numberofpages:9
journal:NATURE NANOTECHNOLOGY

المؤلفون: D'URZO, ANNALISA, Konijnenberg, A, Rossetti, G, Habchi, J, Li, J, Carloni, P, Sobott, F, Longhi, S, GRANDORI, RITA

المساهمون: D'Urzo, A, Konijnenberg, A, Rossetti, G, Habchi, J, Li, J, Carloni, P, Sobott, F, Longhi, S, Grandori, R

مصطلحات موضوعية: Conformational ensemble, Hydrophobic Interaction, Ion mobility, Measles viru, Native mass spectrometry, Ntail-Pxd complex, Hydrophobic and Hydrophilic Interaction, Intrinsically Disordered Protein, Protein Conformation, Recombinant Protein, Spectrometry, Mass, Electrospray Ionization, Viral Protein, Models, Molecular, Structural Biology, Spectroscopy, Medicine (all), BIO/10 - BIOCHIMICA, FIS/07 - FISICA APPLICATA (A BENI CULTURALI, AMBIENTALI, BIOLOGIA E MEDICINA), CHIM/01 - CHIMICA ANALITICA

Relation: info:eu-repo/semantics/altIdentifier/pmid/25510932; info:eu-repo/semantics/altIdentifier/wos/WOS:000350106100011; volume:26; issue:3; firstpage:472; lastpage:481; numberofpages:10; journal:JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY; http://hdl.handle.net/10281/95754; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84923285656

الاتاحة: http://hdl.handle.net/10281/95754
https://doi.org/10.1007/s13361-014-1048-z
https://pubs.acs.org/doi/full/10.1021/jasms.8b04981

المؤلفون: Granata, Daniele, Laio, Alessandro, Baftizadeh, F., Habchi, J., Galvagnion, C., De Simone, A., Camilloni, C., Vendruscolo, M.

المساهمون: Granata, Daniele, Baftizadeh, F., Habchi, J., Galvagnion, C., De Simone, A., Camilloni, C., Laio, Alessandro, Vendruscolo, M.

مصطلحات موضوعية: amyloid-beta-protein, molecular-dynamics simulation, atomic-level characterization, temperature-induced collapse, x-ray-scattering, alzheimers-disease, unfolded protein, unstructured protein, cold denaturation, dipolar couplings

Relation: info:eu-repo/semantics/altIdentifier/wos/WOS:000363394700001; volume:5; firstpage:1; lastpage:15; numberofpages:15; journal:SCIENTIFIC REPORTS; http://hdl.handle.net/20.500.11767/12547; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84945292167

الاتاحة: https://hdl.handle.net/20.500.11767/12547
https://doi.org/10.1038/srep15449

المؤلفون: Habchi, J, Chia, S, Limbocker, R, Mannini, B, Ahn, M, Perni, M, Hansson, O, Arosio, P, Kumita, JR, Challa, PK, Cohen, SIA, Linse, S, Dobson, CM, Knowles, TPJ, Vendruscolo, M

المصدر: Proceedings of the National Academy of Sciences , 114 (2) E200-E208. (2017)

مصطلحات موضوعية: Alzheimer’s disease, amyloid-β peptide, protein misfolding, drug discovery, protein aggregation

وصف الملف: text

Relation: https://discovery.ucl.ac.uk/id/eprint/10072363/1/Ahn_Systematic%20development%20of%20small%20molecules%20to%20inhibit%20specific%20microscopic%20steps%20of%20A%CE%B242%20aggregation%20in%20Alzheimer%E2%80%99s%20disease_VoR.pdf; https://discovery.ucl.ac.uk/id/eprint/10072363/

الاتاحة: https://discovery.ucl.ac.uk/id/eprint/10072363/1/Ahn_Systematic%20development%20of%20small%20molecules%20to%20inhibit%20specific%20microscopic%20steps%20of%20A%CE%B242%20aggregation%20in%20Alzheimer%E2%80%99s%20disease_VoR.pdf
https://discovery.ucl.ac.uk/id/eprint/10072363/

المؤلفون: Kodera N., Noshiro D., Dora S. K., Mori T., Habchi J., Blocquel D., Gruet A., Dosnon M., Salladini E., Bignon C., Fujioka Y., Oda T., Noda N. N., Sato M., Lotti M., Mizuguchi M., Longhi S., Ando T.

المساهمون: Kodera, N, Noshiro, D, Dora, S, Mori, T, Habchi, J, Blocquel, D, Gruet, A, Dosnon, M, Salladini, E, Bignon, C, Fujioka, Y, Oda, T, Noda, N, Sato, M, Lotti, M, Mizuguchi, M, Longhi, S, Ando, T

مصطلحات موضوعية: Intrinsically disordered proteins, conformation, disorder to order transition, high speed atomic force microscopy

Relation: info:eu-repo/semantics/altIdentifier/pmid/33230318; info:eu-repo/semantics/altIdentifier/wos/WOS:000592027200001; volume:16; issue:2; firstpage:181; lastpage:189; numberofpages:9; journal:NATURE NANOTECHNOLOGY; https://hdl.handle.net/10281/295727; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-85096441009

الاتاحة: https://hdl.handle.net/10281/295727
https://doi.org/10.1038/s41565-020-00798-9

المؤلفون: Testa, L, Habchi, J, Longhi, S, Uversky, VN, BROCCA, STEFANIA, SANTAMBROGIO, CARLO, D'URZO, ANNALISA, GRANDORI, RITA

المساهمون: Testa, L, Brocca, S, Santambrogio, C, D'Urzo, A, Habchi, J, Longhi, S, Uversky, V, Grandori, R

مصطلحات موضوعية: native mass spectrometry, charge-state distributions, charge-to-mass relation, protein folding, solvent-accessible surface area, IDP compaction, intrinsically folded structural units, proteomics, Sic1, α-synuclein

Relation: info:eu-repo/semantics/altIdentifier/pmid/28516012; volume:1; issue:1; journal:INTRINSICALLY DISORDERED PROTEINS; http://hdl.handle.net/10281/52036

الاتاحة: http://hdl.handle.net/10281/52036
https://doi.org/10.4161/idp.25068

المؤلفون: Habchi, J., Londergan, Casey H., Longhi, S., Yang, Hailiu, '11

المصدر: Faculty Publications

Relation: https://scholarship.haverford.edu/chemistry_facpubs/116

الاتاحة: https://scholarship.haverford.edu/chemistry_facpubs/116

المؤلفون: Halgand, Frédéric, Habchi, J., Cravello, Laetitia, Martinho, Marlène, Guigliarelli, Bruno, Longhi, Sonia

المساهمون: Laboratoire de Spectrometrie de Masse des Proteines, Université Joseph Fourier - Grenoble 1 (UJF), Bioénergétique et Ingénierie des Protéines (BIP), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Architecture et fonction des macromolécules biologiques (AFMB), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)

المصدر: ISSN: 0003-2700.

مصطلحات موضوعية: [CHIM.ANAL]Chemical Sciences/Analytical chemistry

الاتاحة: https://hal.science/hal-00677256

المؤلفون: D'Urzo, A, Konijnenberg, A, Rossetti, G, Habchi, J, Li, J, Carloni, P, Sobott, F, Longhi, S, Grandori, R, D'URZO, ANNALISA, GRANDORI, RITA

مصطلحات الفهرس: Conformational ensemble, Hydrophobic Interaction, Ion mobility, Measles viru, Native mass spectrometry, Ntail-Pxd complex, Hydrophobic and Hydrophilic Interaction, Intrinsically Disordered Protein, Protein Conformation, Recombinant Protein, Spectrometry, Mass, Electrospray Ionization, Viral Protein, Models, Molecular, Structural Biology, Spectroscopy, Medicine (all), BIO/10 - BIOCHIMICA, FIS/07 - FISICA APPLICATA (A BENI CULTURALI, AMBIENTALI, BIOLOGIA E MEDICINA), CHIM/01 - CHIMICA ANALITICA, info:eu-repo/semantics/article

URL: http://hdl.handle.net/10281/95754
https://pubs.acs.org/doi/full/10.1021/jasms.8b04981
info:eu-repo/semantics/altIdentifier/pmid/25510932
info:eu-repo/semantics/altIdentifier/wos/WOS:000350106100011
volume:26
issue:3
firstpage:472
lastpage:481
numberofpages:10
journal:JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY

المؤلفون: Peter Tompa, Habchi, J., Longhi, S., Vn Uversky

المساهمون: Structural Biology Brussels

المصدر: Vrije Universiteit Brussel

مصطلحات موضوعية: Disorder Protein

URL الوصول: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::423f9a1571101f95e95f7954af251558
https://researchportal.vub.be/en/publications/547e2b83-28b9-4eca-a1ec-67caa0f17d2f

المؤلفون: Habchi, Johnny

Thesis Advisors: Aix-Marseille, Longhi, Sonia

مصطلحات موضوعية: Paramyxovirus, Désordre structural, Nucléoprotéine, Phosphoprotéine, Repliement induit, Nipah, Hendra, Rougeole, Paramyxoviruses, Structural disorder, Nucleoprotein, Phosphoprotein, Induced folding, Measles

الاتاحة: http://www.theses.fr/2012AIXM4091

المؤلفون: Edoardo Salladini, Yuko Fujioka, Marina Lotti, David Blocquel, Antoine Gruet, Noriyuki Kodera, Daisuke Noshiro, Nobuo N. Noda, Mineyuki Mizuguchi, Tetsuya Mori, Mamoru Sato, Marion Dosnon, Christophe Bignon, Takashi Oda, Sonia Longhi, Johnny Habchi, Sujit Kumar Dora, Toshio Ando

المساهمون: Kodera, N, Noshiro, D, Dora, S, Mori, T, Habchi, J, Blocquel, D, Gruet, A, Dosnon, M, Salladini, E, Bignon, C, Fujioka, Y, Oda, T, Noda, N, Sato, M, Lotti, M, Mizuguchi, M, Longhi, S, Ando, T, Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Aix Marseille Université (AMU), Kanazawa University (KU), Academy of Performing Arts [Prague] (AMU), The Institute of Statistical Mathematics (Tokyo ), Yokohama National University, Università degli Studi di Milano-Bicocca [Milano] (UNIMIB), University of Toyama

المصدر: Nature Nanotechnology
Nature Nanotechnology, 2021, 16 (2), pp.181-189. ⟨10.1038/s41565-020-00798-9⟩
Nature Nanotechnology, Nature Publishing Group, 2021, 16 (2), pp.181-189. ⟨10.1038/s41565-020-00798-9⟩

مصطلحات موضوعية: Protein Folding, Materials science, Protein Conformation, Biomedical Engineering, Quantitative Structure-Activity Relationship, Bioengineering, 02 engineering and technology, 010402 general chemistry, Intrinsically disordered proteins, Microscopy, Atomic Force, 01 natural sciences, Protein structure, Microscopy, Molecule, Humans, General Materials Science, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Electrical and Electronic Engineering, Intrinsically disordered proteins, conformation, disorder to order transition, high speed atomic force microscopy, ComputingMilieux_MISCELLANEOUS, Atomic force microscopy, Dynamics (mechanics), 021001 nanoscience & nanotechnology, Condensed Matter Physics, Atomic and Molecular Physics, and Optics, 0104 chemical sciences, Molecular Imaging, Intrinsically Disordered Proteins, Chemical physics, Mutation, Protein folding, 0210 nano-technology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4f5c66b7933600b9a34f968937c68cd
http://hdl.handle.net/10281/295727

المؤلفون: Fahimeh Baftizadeh, Johnny Habchi, Carlo Camilloni, Alfonso De Simone, Alessandro Laio, Daniele Granata, Céline Galvagnion, Michele Vendruscolo

المساهمون: Massachusetts Institute of Technology. Department of Chemical Engineering, Baftizadeh, Fahimeh, Granata, D., Baftizadeh, F., Habchi, J., Galvagnion, C., De Simone, A., Camilloni, C., Laio, A., Vendruscolo, M.

المصدر: Nature Publishing Group
Scientific Reports

مصطلحات موضوعية: Circular dichroism, Magnetic Resonance Spectroscopy, Globular protein, Protein Conformation, atomic-level characterization, Peptide, amyloid-beta-protein, molecular-dynamics simulations, temperature-induced collapse, x-ray-scattering, alzheimers-disease, unfolded proteins, unstructured proteins, cold denaturation, dipolar couplings, Molecular Dynamics Simulation, Intrinsically disordered proteins, Article, Molecular dynamics, Protein structure, Protein secondary structure, chemistry.chemical_classification, Physics, Quantitative Biology::Biomolecules, Multidisciplinary, Circular Dichroism, Energy landscape, Intrinsically Disordered Proteins, chemistry, Chemical physics, Chromatography, Gel, Thermodynamics

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::286ad8f172b7be5a75a9f1098e50dfcf
http://hdl.handle.net/1721.1/100502

المؤلفون: Lorenzo Testa, Vladimir N. Uversky, Stefania Brocca, Rita Grandori, Johnny Habchi, Annalisa D'Urzo, Carlo Santambrogio, Sonia Longhi

المساهمون: Testa, L, Brocca, S, Santambrogio, C, D'Urzo, A, Habchi, J, Longhi, S, Uversky, V, Grandori, R

المصدر: Intrinsically Disordered Proteins

مصطلحات موضوعية: native mass spectrometry, charge-state distributions, charge-to-mass relation, protein folding, solvent-accessible surface area, IDP compaction, intrinsically folded structural units, proteomics, Sic1, α-synuclein, Chemistry, native mass spectrometry, Electrospray ionization, solvent-accessible surface area, Review, charge-state distributions, intrinsically folded structural units, Mass spectrometry, Proteomics, Intrinsically disordered proteins, IDP compaction, Industrial and Manufacturing Engineering, Characterization (materials science), Crystallography, proteomics, α-synuclein, Chemical physics, Sic1, charge-to-mass relation, Ionization, protein folding, Protein folding, Conformational ensembles

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdf368b17ecffb5620d684db8d665f85
http://europepmc.org/articles/PMC5424789