Copper Sensing with a Prion Protein Modified Nanopipette. (Q36459164)

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20 February 2020

title

Copper Sensing with a Prion Protein Modified Nanopipette (English)

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20 February 2020

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2

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20 February 2020

author name string

Paolo Actis

1

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20 February 2020

David Beeler

3

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20 February 2020

Boaz Vilozny

4

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20 February 2020

Glenn Millhauser

5

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20 February 2020

Nader Pourmand

6

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20 February 2020

publication date

1 January 2012

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20 February 2020

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20 February 2020

volume

2

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20 February 2020

issue

31

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20 February 2020

page(s)

11638-11640

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Voltage controlled nano-injection system for single-cell surgery

20 February 2020

cites work

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Reversible cation response with a protein-modified nanopipette

30 September 2017

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30 September 2017

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Voltage-Controlled Metal Binding on Polyelectrolyte-Functionalized Nanopores

30 September 2017

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Development of a Troponin I Biosensor Using a Peptide Obtained through Phage Display

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Engineered voltage-responsive nanopores.

30 September 2017

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EPR of Cu2 prion protein constructs at 2 GHz using the g(perpendicular) region to characterize nitrogen ligation

30 September 2017

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Label-free biosensing with functionalized nanopipette probes

30 September 2017

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Nanoscale live-cell imaging using hopping probe ion conductance microscopy

30 September 2017

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Trace elements and prion diseases: a review of the interactions of copper, manganese and zinc with the prion protein

30 September 2017

1 reference

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Copper and the prion protein: methods, structures, function, and disease

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3519431

Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3519431

Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry

30 September 2017

1 reference

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Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3519431

30 September 2017

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Molecular biology of prion diseases

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3519431

The prion protein is a combined zinc and copper binding protein: Zn2 alters the distribution of Cu2 coordination modes

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3519431

The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4.

28 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3519431

Ablation of the metal ion-induced endocytosis of the prion protein by disease-associated mutation of the octarepeat region

28 June 2018

1 reference

Crossref

https://api.crossref.org/works/10.1039/C2RA21730A

Copper binding to the octarepeats of the prion protein. Affinity, specificity, folding, and cooperativity: insights from circular dichroism

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1039/C2RA21730A

Nanopore detection of antibody prion interactions

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1039/C2RA21730A

Nanopore analysis of the interaction of metal ions with prion proteins and peptides

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/23243499

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1039/C2RA21730A

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23243499 AND SRC:MED&resulttype=core&format=json

20 February 2020

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20 February 2020

PubMed publication ID

23243499

1 reference