| P50 | author | Ramón A Lorca | Q81223246 |
| P2093 | author name string | María Inés Barría | |
| | J. Pablo Huidobro-Toro | |
| | Nibaldo C. Inestrosa | |
| | Marcelo Chacón | |
| P2860 | cites work | Molecular features of the copper binding sites in the octarepeat domain of the prion protein | Q24292484 |
| | Metal ion chaperone function of the soluble Cu(I) receptor Atx1. | Q27934215 |
| | Evidence of presynaptic location and function of the prion protein | Q28145703 |
| | Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability | Q28253718 |
| | Receptors for purines and pyrimidines | Q28283941 |
| | Zinc and copper modulate differentially the P2X4 receptor | Q28374487 |
| | Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein | Q28570280 |
| | Distinct Localization of P2X receptors at excitatory postsynaptic specializations | Q28583428 |
| | Copper stimulates endocytosis of the prion protein | Q28589040 |
| | Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase | Q29619948 |
| | Copper binding to the prion protein: structural implications of four identical cooperative binding sites | Q30558995 |
| | Molecular cloning of a candidate chicken prion protein | Q33191659 |
| | Metallochaperones, an intracellular shuttle service for metal ions | Q33902264 |
| | Function, structure, and mechanism of intracellular copper trafficking proteins | Q34275487 |
| | Copper and prion disease | Q34317924 |
| | Normal prion protein has an activity like that of superoxide dismutase. | Q34505606 |
| | Zn2+ potentiates excitatory action of ATP on mammalian neurons | Q36520493 |
| | Location and properties of metal-binding sites on the human prion protein. | Q37104327 |
| | Toxic effects of heavy metals on ionic channels | Q40396892 |
| | Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy | Q41983149 |
| | The beta A4 amyloid precursor protein binding to copper. | Q42281770 |
| | Raman spectroscopic study on the copper(II) binding mode of prion octapeptide and its pH dependence | Q43553322 |
| | Formation of carnosine-Cu(II) complexes prevents and reverts the inhibitory action of copper in P2X4 and P2X7 receptors. | Q43883817 |
| | Role for P2X receptors in long-term potentiation. | Q44156146 |
| | Copper-induced conformational change in a marsupial prion protein repeat peptide probed using FTIR spectroscopy | Q45711430 |
| | Prion protein selectively binds copper(II) ions | Q46492410 |
| | Prion protein is necessary for normal synaptic function | Q48087355 |
| | Differential modulation by copper and zinc of P2X2 and P2X4 receptor function | Q48918694 |
| | The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I) | Q53320133 |
| | The cellular prion protein binds copper in vivo | Q56058857 |
| | The N-terminal tandem repeat region of human prion protein reduces copper: role of tryptophan residues | Q73525251 |
| | Prion protein binds copper within the physiological concentration range | Q73692926 |
| | Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein | Q78170240 |
| P433 | issue | 3 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | biochemistry | Q7094 |
| | prion protein family | Q24724413 |
| | purinergic P2 receptor antagonists | Q50430427 |
| P304 | page(s) | 709-716 | |
| P577 | publication date | 2003-05-01 | |
| P1433 | published in | Journal of Neurochemistry | Q6295643 |
| P1476 | title | The human prion octarepeat fragment prevents and reverses the inhibitory action of copper in the P2X4 receptor without modifying the zinc action | |
| P478 | volume | 85 | |