Tampé, Robert 1961-
Tampé, Robert
Robert Tampé deutscher Biochemiker
VIAF ID: 9691149068473965730006 (Personal)
Permalink: http://viaf.org/viaf/9691149068473965730006
Preferred Forms
- 100 0 _ ‡a Robert Tampé ‡c deutscher Biochemiker
- 100 1 _ ‡a Tampé, Robert ‡d 1961-
-
- 100 1 _ ‡a Tampé, Robert
4xx's: Alternate Name Forms (6)
5xx's: Related Names (3)
- 551 _ _ ‡a Frankfurt am Main ‡4 ortw ‡4 https://d-nb.info/standards/elementset/gnd#placeOfActivity
- 510 2 _ ‡a Goethe-Universität Frankfurt am Main ‡4 affi ‡4 https://d-nb.info/standards/elementset/gnd#affiliation ‡e Affiliation
- 551 _ _ ‡a Seligenstadt ‡4 ortg ‡4 https://d-nb.info/standards/elementset/gnd#placeOfBirth
Works
Title | Sources |
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3rd Giessen-Marburg-Göttinger Transport Colloquium : [abstracts] : conference of the Gesellschaft für Biochemie und Molekularbiologie : Rauischholzhausen, May 17-18, 2001 | |
Asymmetric ATP hydrolysis cycle of the heterodimeric multidrug ABC transport complex TmrAB from Thermus thermophilus | |
ATP hydrolysis cycle of the nucleotide-binding domain of the mitochondrial ATP-binding cassette transporter Mdl1p | |
binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter | |
Charakterisierung thylakoidärer TatBC-Rezeptorkomplexe | |
Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP | |
Dynamic in situ confinement triggers ligand-free neuropeptide receptor signaling | |
Engineering ATPase activity in the isolated ABC cassette of human TAP1 | |
epidermal growth factor receptor is a relevant host factor in the early stages of the Zika virus life cycle in vitro | |
Epistatic interactions promote persistence of NS3-Q80K in HCV infection by compensating for protein folding instability | |
Extended interaction networks with HCV protease NS3-4A substrates explain the lack of adaptive capability against protease inhibitors | |
Fucosylated lipid nanocarriers loaded with antibiotics efficiently inhibit mycobacterial propagation in human myeloid cells | |
Identification of a lysosomal peptide transport system induced during dendritic cell development | |
Light control of the peptide-loading complex synchronizes antigen translocation and MHC I trafficking | |
Mechanism of substrate sensing and signal transmission within an ABC transporter: use of a Trojan horse strategy | |
Mechanism of the MHC I chaperone TAPBPR and its role in promoting UGGT1-mediated quality control | |
Mechanistic insights into ribosome recycling and quality control in mRNA translation | |
Molecular analysis of the ribosome recycling factor ABCE1 bound to the 30S post-splitting complex | |
On the molecular organization of a succinyl-CoA-producing cell-free system : a cryo-EM and computational approach | |
PAKC: A novel panel of HLA class I antigen presentation machinery knockout cells from the same genetic origin | |
Peptide specificity and lipid activation of the lysosomal transport complex ABCB9 (TAPL) | |
Purification and reconstitution of the antigen transport complex TAP: a prerequisite for determination of peptide stoichiometry and ATP hydrolysis | |
Sensitizer-enhanced two-photon patterning of biomolecules in photoinstructive hydrogels | |
Signaling of a varicelloviral factor across the endoplasmic reticulum membrane induces destruction of the peptide-loading complex and immune evasion | |
Specific lipids modulate the transporter associated with antigen processing (TAP) | |
Specific orientation and two-dimensional crystallization of the proteasome at metal-chelating lipid interfaces | |
Structural and functional analysis of the MHC I–tapasin–ERp57 multi-chaperone complex in antigen processing and presentation | |
Structural basis of substrate recognition by human tRNA splicing endonuclease TSEN | |
Structure and dynamics of membrane-associated ICP47, a viral inhibitor of the MHC I antigen-processing machinery | |
Synthetic protein-conductive membrane nanopores built with DNA | |
Viral immune evasins impact antigen presentation by allele-specific trapping of MHC I at the peptide-loading complex | |
Zur Wechselwirkung von Glycophorin mit Lipidkomponenten in künstlichen Phospholipid-Doppelschichten : eine spektroskopische, elektronenmikroskopische und kaloirmetrische Studie zur Lipid-Protein-Wechselwirkung |