(Q35886826)

English

ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.

scientific article published on 6 January 2016

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scholarly article

1 reference

Europe PubMed Central

10 August 2017

ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43. (English)

1 reference

Europe PubMed Central

10 August 2017

prion protein family

0 references

amyotrophic lateral sclerosis

1 reference

based on heuristic

inferred from title

TAR DNA binding protein

1 reference

GOA release 2020-03-11

identical protein binding

1 reference

GOA release 2020-03-11

1 reference

based on heuristic

inferred from title

object named as

Jianxing Song

4

0 references

object named as

Yuanyuan Wei

2

0 references

author name string

Liangzhong Lim

1

1 reference

Europe PubMed Central

10 August 2017

Yimei Lu

3

1 reference

Europe PubMed Central

10 August 2017

language of work or name

0 references

publication date

6 January 2016

1 reference

Europe PubMed Central

10 August 2017

1 reference

Europe PubMed Central

10 August 2017

14

1 reference

Europe PubMed Central

10 August 2017

1

1 reference

Europe PubMed Central

10 August 2017

e1002338

1 reference

Europe PubMed Central

10 August 2017

copyright license

Creative Commons Attribution 4.0 International

6 January 2016

1 reference

April 2022 Public Data File from Crossref

copyright status

0 references

In Search of Aggregation Pathways of IAPP and Other Amyloidogenic Proteins: Finding Answers through NMR Spectroscopy.

1 reference

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An ALS-mutant TDP-43 neurotoxic peptide adopts an anti-parallel β-structure and induces TDP-43 redistribution.

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Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease.

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"Structural characterization of the minimal segment of TDP-43 competent for aggregation".

1 reference

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Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

1 reference

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Abnormal mitochondrial transport and morphology are common pathological denominators in SOD1 and TDP43 ALS mouse models

1 reference

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Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis

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The ALS disease-associated mutant TDP-43 impairs mitochondrial dynamics and function in motor neurons

1 reference

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Structural transformation of the amyloidogenic core region of TDP-43 protein initiates its aggregation and cytoplasmic inclusion

1 reference

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Stress granules as crucibles of ALS pathogenesis.

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The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation

1 reference

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Membrane disordering is not sufficient for membrane permeabilization by islet amyloid polypeptide: studies of IAPP(20-29) fragments

1 reference

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Protein amyloids develop an intrinsic fluorescence signature during aggregation

1 reference

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1 reference

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NMR View: A computer program for the visualization and analysis of NMR data

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Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels

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The seeds of neurodegeneration: prion-like spreading in ALS

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1 reference

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TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity

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Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity

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Fine structural analysis of the neuronal inclusions of frontotemporal lobar degeneration with TDP-43 proteinopathy.

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Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation

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11 July 2018

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Islet amyloid development in a mouse strain lacking endogenous islet amyloid polypeptide (IAPP) but expressing human IAPP

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11 July 2018

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Molecular dissection of TDP-43 proteinopathies.

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Human, Drosophila, and C.elegans TDP43: nucleic acid binding properties and splicing regulatory function

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Nuclear TDP-43 causes neuronal toxicity by escaping from the inhibitory regulation by hnRNPs

1 reference

https://pubmed.ncbi.nlm.nih.gov/26735904

12 December 2020

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10.1371/JOURNAL.PBIO.1002338

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Europe PubMed Central

10 August 2017

1 reference

Europe PubMed Central

10 August 2017

1 reference

Europe PubMed Central

10 August 2017

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