Deamidation accelerates amyloid formation and alters amylin fiber structure - Wikidata - wikimedia - TriplyDB

Deamidation accelerates amyloid formation and alters amylin fiber structure

Deamidation accelerates amyloid formation and alters amylin fiber structure

http://www.wikidata.org/entity/Q41814945

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Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitus Mechanisms of islet amyloidosis toxicity in type 2 diabetes Insight of brain degenerative protein modifications in the pathology of neurodegeneration and dementia by proteomic profiling Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Post-translational modifications in PrP expand the conformational diversity of prions in vivo Heat-induced irreversible denaturation of the camelid single domain VHH antibody is governed by chemical modifications.Detection of Helical Intermediates During Amyloid Formation by Intrinsically Disordered Polypeptides and Proteins.In Vitro Studies of Membrane Permeability Induced by Amyloidogenic Polypeptides Using Large Unilamellar Vesicles.Deamidation reactions of protonated asparagine and glutamine investigated by ion spectroscopy.Deamidation Reactions of Asparagine- and Glutamine-Containing Dipeptides Investigated by Ion Spectroscopy.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Asparagine deamidation reduces DNA-binding affinity of the Drosophila melanogaster Scr homeodomain.Dementia-linked amyloidosis is associated with brain protein deamidation as revealed by proteomic profiling of human brain tissues.A strongly absorbing class of non-natural labels for probing protein electrostatics and solvation with FTIR and 2D IR spectroscopies.Lessons from two prevalent amyloidoses-what amylin and Aβ have in common Intrinsic structural heterogeneity and long-term maturation of amyloid β peptide fibrils Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology.Protein truncation as a common denominator of human neurodegenerative foldopathies.Early engineering approaches to improve peptide developability and manufacturability.Future of the Genetic Code.Structural Properties of Human IAPP Dimer in Membrane Environment Studied by All-Atom Molecular Dynamics Simulations.Suppression of amyloid fibrils using the GroEL apical domain.An alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin.How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy.L-Asparagine crystals with wide gap semiconductor features: optical absorption measurements and density functional theory computations.Factors affecting the physical stability (aggregation) of peptide therapeutics.Islet Amyloid Polypeptide Membrane Interactions: Effects of Membrane Composition.Deamidation of Protonated Asparagine-Valine Investigated by a Combined Spectroscopic, Guided Ion Beam, and Theoretical Study.Isotope-Labeled Amyloids via Synthesis, Expression, and Chemical Ligation for Use in FTIR, 2D IR, and NMR Studies.Transition Dipoles from 1D and 2D Infrared Spectroscopy Help Reveal the Secondary Structures of Proteins: Application to Amyloids.Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR Implications of Metal Binding and Asparagine Deamidation for Amyloid Formation

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P2860

Deamidation accelerates amyloid formation and alters amylin fiber structure

http://www.wikidata.org/entity/Q41814945

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

@yue

2012年論文

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2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

2012年论文

@zh

2012年论文

@zh-cn

name

Deamidation accelerates amyloid formation and alters amylin fiber structure

@en

type

label

Deamidation accelerates amyloid formation and alters amylin fiber structure

@en

prefLabel

Deamidation accelerates amyloid formation and alters amylin fiber structure

@en

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P1433

Journal of the American Chemical Society

P1476

Deamidation accelerates amyloid formation and alters amylin fiber structure

@en

P2093

Emily B Dunkelberger

http://www.w3.org/2001/XMLSchema#string

Martin T Zanni

http://www.w3.org/2001/XMLSchema#string

Peter Marek

http://www.w3.org/2001/XMLSchema#string

Ping Cao

http://www.w3.org/2001/XMLSchema#string

P2860

Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus

Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells

Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients

Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)

Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation

Proteomic analysis of post-translational modifications

Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes

Molecular clocks

Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation.

Residue-specific structural kinetics of proteins through the union of isotope labeling, mid-IR pulse shaping, and coherent 2D IR spectroscopy.

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12658-12667

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scholarly article

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10.1021/JA3039486

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P433

30

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134

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Daniel P Raleigh

Lauren E. Buchanan

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2012-07-17T00:00:00Z

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22734583

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3410046

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