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The 3D profile method for identifying fibril-forming segments of proteins

The 3D profile method for identifying fibril-forming segments of proteins

http://www.wikidata.org/entity/Q24545011

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Protein folding: then and now The Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD / NMR study Yeast prions and human prion-like proteins: sequence features and prediction methods The relationship between amyloid structure and cytotoxicity Ubiquitous amyloids Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)Molecular mechanisms for protein-encoded inheritance Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation Molecular basis for amyloid- polymorphism Atomic View of a Toxic Amyloid Small Oligomer Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis Aggregation propensity of the human proteome Prediction of Peptide and Protein Propensity for Amyloid Formation AMYPdb: a database dedicated to amyloid precursor proteins On the role of aggregation prone regions in protein evolution, stability, and enzymatic catalysis: insights from diverse analyses.Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic tools Practically useful: what the Rosetta protein modeling suite can do for you Using structural bioinformatics to investigate the impact of non synonymous SNPs and disease mutations: scope and limitations.Insight into the structure of amyloid fibrils from the analysis of globular proteins.Prediction of amyloidogenic and disordered regions in protein chains AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Bacterial inclusion bodies contain amyloid-like structure Prediction of amyloid fibril-forming segments based on a support vector machine Amyloidogenic determinants are usually not buried Amyloidogenic regions and interaction surfaces overlap in globular proteins related to conformational diseases.Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spine Protein aggregation profile of the bacterial cytosol.Identifying the amylome, proteins capable of forming amyloid-like fibrils The clustering and spatial arrangement of beta-sheet sequence, but not order, govern alpha-synuclein fibrillogenesis PASTA 2.0: an improved server for protein aggregation prediction.Analysis of the Amyloidogenic Potential of Pufferfish (Takifugu rubripes) Islet Amyloid Polypeptide Highlights the Limitations of Thioflavin-T Assays and the Difficulties in Defining Amyloidogenicity An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins.Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation Discriminating early stage A{beta}42 monomer structures using chirality-induced 2DIR spectroscopy in a simulation study.Exploiting heterogeneous features to improve in silico prediction of peptide status - amyloidogenic or non-amyloidogenic.Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau.Amyloid fibrils composed of hexameric peptides attenuate neuroinflammation.Two-dimensional ultraviolet (2DUV) spectroscopic tools for identifying fibrillation propensity of protein residue sequences

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The 3D profile method for identifying fibril-forming segments of proteins

http://www.wikidata.org/entity/Q24545011

description

2006 nî lūn-bûn

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2006 թուականի Մարտին հրատարակուած գիտական յօդուած

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2006 թվականի մարտին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

The 3D profile method for identifying fibril-forming segments of proteins

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The 3D profile method for identifying fibril-forming segments of proteins

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The 3D profile method for identifying fibril-forming segments of proteins

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The 3D profile method for identifying fibril-forming segments of proteins

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The 3D profile method for identifying fibril-forming segments of proteins

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The 3D profile method for identifying fibril-forming segments of proteins

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Proceedings of the National Academy of Sciences of the United States of America

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The 3D profile method for identifying fibril-forming segments of proteins

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David Baker

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John Karanicolas

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Magdalena I Ivanova

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Michael J Thompson

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Stuart A Sievers

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P2860

Structure of the cross-beta spine of amyloid-like fibrils

Native protein sequences are close to optimal for their structures

Dissection of the functional role of structural elements of tyrosine-63 in the catalytic action of human lysozyme

An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloid

A method to identify protein sequences that fold into a known three-dimensional structure

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Amyloid fibril formation by an SH3 domain.

Sequence determinants of amyloid fibril formation

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103

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David Eisenberg

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16537487

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1449648

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