We study spectral and transport properties of interacting quantum dots with
spin. Two particular model systems are investigated: Lateral multilevel and two
parallel quantum dots. In both cases different paths through the system can
give rise to interference. We demonstrate that this strengthens the multilevel
Kondo effect for which a simple two-stage mechanism is proposed. In parallel
dots we show under which conditions the peak of an interference-induced orbital
Kondo effect can be split.Comment: 8 pages, 8 figure

Ferrari, D.

Kramer, B.

Monnat, J.

Neuhaus, E.

Pop, M.

Soldati, T.

English

arXiv

Boese, Daniel

Hofstetter, Walter

Schoeller, Herbert

RWTH Publications

Interference in interacting quantum dots with spin

Daniel Boese

Walter Hofstetter

Herbert Schoeller

MUCC (Crossref)

Localization of soluble endoplasmic reticulum (ER) resident proteins is likely achieved by the complementary action of retrieval and retention mechanisms. Whereas the machinery involving the H/KDEL and related retrieval signals in targeting escapees back to the ER is well characterized, other mechanisms including retention are still poorly understood. We have identified a protein disulfide isomerase (Dd-PDI) lacking the HDEL retrieval signal normally found at the C terminus of ER residents in Dictyostelium discoideum. Here we demonstrate that its 57 residue C-terminal domain is necessary for intracellular retention of Dd-PDI and sufficient to localize a green fluorescent protein (GFP) chimera to the ER, especially to the nuclear envelope. Dd-PDI and GFP-PDI57 are recovered in similar cation-dependent complexes. The overexpression of GFP-PDI57 leads to disruption of endogenous PDI complexes and induces the secretion of PDI, whereas overexpression of a GFP-HDEL chimera induces the secretion of endogenous calreticulin, revealing the presence of two independent and saturable mechanisms. Finally, low-level expression of Dd-PDI but not of PDI truncated of its 57 C-terminal residues complements the otherwise lethal yeast TRG1/PDI1 null mutation, demonstrating functional disulfide isomerase activity and ER localization. Altogether, these results indicate that the PDI57 peptide contains ER localization determinants recognized by a conserved machinery present in D. discoideum and Saccharomyces cerevisiae

Monnat, Jean

Neuhaus, Eva M.

Pop, Marius S.

Ferrari, David M.

Kramer, Barbara

Soldati, Thierry

Max Planck Society eDoc Server

Identification of a novel saturable endoplasmic reticulum localization mechanism mediated by the C-terminus of a Dictyostelium protein disulfide isomerase

Interference in interacting quantum dots with spin

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RWTH Publications

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Max Planck Society eDoc Server

MUCC (Crossref)

MUCC (Crossref)

MUCC (Crossref)

MUCC (Crossref)