Copper induces conformational changes in the N-terminal part of cell-surface PrPC. (Q51806541)

12 April 2018

title

Copper induces conformational changes in the N-terminal part of cell-surface PrPC. (English)

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12 April 2018

3

Prusiner SB

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12 April 2018

Leclerc E

1

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12 April 2018

Serban H

series ordinal

2

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12 April 2018

Burton DR

series ordinal

4

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12 April 2018

Williamson RA

series ordinal

5

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12 April 2018

publication date

22 June 2006

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12 April 2018

number of pages

7

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based on heuristic

inferred from page(s)

published in

Archives of Virology

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12 April 2018

volume

151

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12 April 2018

issue

11

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12 April 2018

page(s)

2103-2109

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12 April 2018

https://scigraph.springernature.com/pub.10.1007/s00705-006-0804-1

exact match

0 references

cites work

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

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Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery

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Insertion in prion protein gene in familial Creutzfeldt-Jakob disease

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11 October 2022

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Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein

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Location and properties of metal-binding sites on the human prion protein.

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11 October 2022

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Mapping Cu(II) binding sites in prion proteins by diethyl pyrocarbonate modification and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometric footprinting

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Copper chelation delays the onset of prion disease

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The cellular prion protein binds copper in vivo

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11 October 2022

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Prion protein expression in Chinese hamster ovary cells using a glutamine synthetase selection and amplification system

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11 October 2022

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Prion protein selectively binds copper(II) ions

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Copper binding to the prion protein: structural implications of four identical cooperative binding sites

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11 October 2022

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Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy

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11 October 2022

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Metal ions and prion diseases

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11 October 2022

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Prion protein binds copper within the physiological concentration range

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Molecular features of the copper binding sites in the octarepeat domain of the prion protein

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11 October 2022

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XAFS study of the high-affinity copper-binding site of human PrP(91-231) and its low-resolution structure in solution

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Prion infection impairs copper binding of cultured cells

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NMR structure of the bovine prion protein

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11 October 2022

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Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie.

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11 October 2022

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Raman spectroscopic study on the copper(II) binding mode of prion octapeptide and its pH dependence

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Conformation of PrP(C) on the cell surface as probed by antibodies.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Normal prion protein has an activity like that of superoxide dismutase.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Copper stimulates endocytosis of the prion protein

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Copper and prion diseases

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Electron paramagnetic resonance evidence for binding of Cu(2+) to the C-terminal domain of the murine prion protein

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Binding of Cu(II) to non-prosthetic sites in ceruloplasmin and bovine serum albumin

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1007/S00705-006-0804-1

Identifiers

DOI

10.1007/S00705-006-0804-1

1 reference

12 April 2018

1 reference

12 April 2018