Single chain TNF derivatives with individually mutated receptor binding sites reveal differential stoichiometry of ligand receptor complex formation for TNFR1 and TNFR2

Cellular Signalling

Volumn 22, Issue 7, 2010, Pages 1088-1096

  Boschert, Verena ^a   Krippner Heidenreich, Anja ^a,b   Branschädel, Marcus ^a,c   Tepperink, Jessica ^a   Aird, Andrew ^a   Scheurich, Peter ^a  

^a UNIVERSITY OF STUTTGART   (Germany)

^b NEWCASTLE UNIVERSITY   (United Kingdom)

^c APOGENIX GMBH   (Germany)

Author keywords

Avidity; Binding affinity; Binding stoichiometry; Pre ligand binding assembly domain (PLAD); TNF; TNF receptor

Indexed keywords

FAS LIGAND; LIGAND; TUMOR NECROSIS FACTOR DERIVATIVE; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2;

ARTICLE; BINDING AFFINITY; BINDING SITE; CELL STRAIN HEK293; COMPLEX FORMATION; CONTROLLED STUDY; CROSS LINKING; CYTOTOXICITY; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; PLASMID; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; STOICHIOMETRY; WESTERN BLOTTING;

ANIMALS; BINDING SITES; CELLS, CULTURED; DIMERIZATION; FAS LIGAND PROTEIN; HUMANS; LIGANDS; MICE; MUTATION; RECEPTORS, TUMOR NECROSIS FACTOR, TYPE I; RECEPTORS, TUMOR NECROSIS FACTOR, TYPE II; TUMOR NECROSIS FACTOR-ALPHA;

EID: 77952290633     PISSN: 08986568     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cellsig.2010.02.011     Document Type: Article

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