(Q30156069)

English

High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .

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scholarly article

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Europe PubMed Central

PMC publication ID

31 October 2017

High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure . (English)

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

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Cait E. MacPhee

4

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

object named as

Thorsten Maly

2

0 references

5

object named as

Christopher M Dobson

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

Robert G. Griffin

6

object named as

Robert G Griffin

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

author name string

Neil R Birkett

3

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

language of work or name

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publication date

1 September 2010

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Europe PubMed Central

PMC publication ID

31 October 2017

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

49

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

35

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

7474-7484

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies

1 reference

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Solid-state NMR studies of HIV-1 capsid protein assemblies.

1 reference

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Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy

1 reference

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Experimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation

1 reference

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3 June 2018

Dipolar truncation in magic-angle spinning NMR recoupling experiments

1 reference

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Solid-state NMR evidence for inequivalent GvpA subunits in gas vesicles

1 reference

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Amyloid formation by globular proteins under native conditions

1 reference

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Determination of protein structures in the solid state from NMR chemical shifts

1 reference

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Direct characterization of amyloidogenic oligomers by single-molecule fluorescence

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Native conformation at specific residues in recombinant inclusion body protein in whole cells determined with solid-state NMR spectroscopy

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The Zyggregator method for predicting protein aggregation propensities

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Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils

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Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

1 reference

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3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraints

1 reference

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3 June 2018

Role of intermolecular forces in defining material properties of protein nanofibrils

1 reference

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3 June 2018

Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p.

1 reference

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3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR.

1 reference

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NMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain

1 reference

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3 June 2018

Molecular structure of amyloid fibrils: insights from solid-state NMR.

1 reference

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3 June 2018

Protein misfolding, functional amyloid, and human disease

1 reference

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Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide

1 reference

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Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils

1 reference

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3 June 2018

Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation

1 reference

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3 June 2018

Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.

1 reference

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3 June 2018

Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

3 June 2018

Parallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

3 June 2018

Molecular recycling within amyloid fibrils

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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Protein structure determination by high-resolution solid-state NMR spectroscopy: application to microcrystalline ubiquitin.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

3 June 2018

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

3 June 2018

Conformational constraints for amyloid fibrillation: the importance of being unfolded

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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A neuronal isoform of the aplysia CPEB has prion-like properties

1 reference

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Protein folding and misfolding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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Rationalization of the effects of mutations on peptide and protein aggregation rates.

1 reference

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3 June 2018

Chemical shift referencing in MAS solid state NMR.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis

1 reference

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RefDB: a database of uniformly referenced protein chemical shifts

1 reference

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Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril

1 reference

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1 reference

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Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy

1 reference

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Insights into the origin of the tendency of the PI3-SH3 domain to form amyloid fibrils

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy.

1 reference

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Therapeutic strategies for human amyloid diseases

1 reference

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Role of Escherichia coli curli operons in directing amyloid fiber formation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2932965

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Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain

1 reference

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Nucleated conformational conversion and the replication of conformational information by a prion determinant

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Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis

1 reference

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Salt-induced detour through compact regions of the protein folding landscape

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De novo amyloid proteins from designed combinatorial libraries

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From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.

1 reference

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Amyloid fibril formation by an SH3 domain

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Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

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1H and 15N assignments and secondary structure of the PI3K SH3 domain

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NMR Nomenclature: Nuclear Spin Properties and Conventions for Chemical Shifts. IUPAC Recommendations 2001.

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The protofilament substructure of amyloid fibrils11Edited by F. E. Cohen

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https://pubmed.ncbi.nlm.nih.gov/20707313

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based on heuristic

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Preparation and Characterization of Purified Amyloid Fibrils

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https://pubmed.ncbi.nlm.nih.gov/20707313

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inferred from PubMed ID database lookup

Minimalist protein model as a diagnostic tool for misfolding and aggregation

1 reference

https://pubmed.ncbi.nlm.nih.gov/20707313

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based on heuristic

inferred from PubMed ID database lookup

Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh

1 reference

https://pubmed.ncbi.nlm.nih.gov/20707313

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based on heuristic

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1 reference

https://pubmed.ncbi.nlm.nih.gov/20707313

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Adiabatic dipolar recoupling in solid-state NMR: the DREAM scheme

1 reference

https://pubmed.ncbi.nlm.nih.gov/20707313

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

1 reference

https://pubmed.ncbi.nlm.nih.gov/20707313

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

1 reference

https://pubmed.ncbi.nlm.nih.gov/20707313

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

NMR nomenclature. Nuclear spin properties and conventions for chemical shifts (IUPAC Recommendations 2001)

1 reference

20 August 2023

https://opencitations.net/index/coci/api/v1/citations/10.1351/PAC200173111795

Identifiers

10.1021/BI100864T

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

31 October 2017

ResearchGate publication ID

0 references

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