Comparison of the binding and internalization properties of 12 DOTA-coupled and 111In-labelled CCK2/gastrin receptor binding peptides: A collaborative project under COST Action BM0607

European Journal of Nuclear Medicine and Molecular Imaging

Volumn 38, Issue 8, 2011, Pages 1417-1425

  Aloj, Luigi ^a   Aurilio, Michela ^a   Rinaldi, Valentina ^a   D'ambrosio, Laura ^a   Tesauro, Diego ^b   Peitl, Petra Kolenc ^c   Maina, Theodosia ^d   Mansi, Rosalba ^e   Von Guggenberg, Elisabeth ^f   Joosten, Lieke ^g   Sosabowski, Jane K ^h   Breeman, Wouter A P ⁱ   De Blois, Erik ⁱ   Koelewijn, Stuart ⁱ   Melis, Marleen ⁱ   Waser, Beatrice ^j   Beetschen, Karin ^j   Reubi, Jean Claude ^j   De Jong, Marion ⁱ  

^a NATIONAL CANCER INSTITUTE   (Italy)

^b UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^c UNIVERSITY MEDICAL CENTRE LJUBLJANA   (Slovenia)

^d INSTITUTE OF NANOSCIENCE AND NANOTECHNOLOGY   (Greece)

^e UNIVERSITY OF FREIBURG   (Germany)

^f INNSBRUCK MEDICAL UNIVERSITY   (Austria)

^g RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

^h QUEEN MARY UNIVERSITY OF LONDON   (United Kingdom)

ⁱ ERASMUS MEDICAL CENTER   (Netherlands)

^j UNIVERSITY OF BERN   (Switzerland)

more..

Author keywords

Cholecystokinin; DOTA; Gastrin; Tumour

Indexed keywords

1,4,7,10 TETRAAZACYCLODODECANE 1,4,7,10 TETRAACETIC ACID; CHOLECYSTOKININ B RECEPTOR; GASTRIN RECEPTOR; INDIUM 111;

ANIMAL CELL; ARTICLE; AUTORADIOGRAPHY; BINDING AFFINITY; BINDING SITE; CANCER TISSUE; COMPARATIVE STUDY; CONTROLLED STUDY; DISSOCIATION CONSTANT; HUMAN; HUMAN CELL; HUMAN TISSUE; IC 50; IN VITRO STUDY; NONHUMAN; PROTEIN BINDING; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN TRANSPORT; RECEPTOR AFFINITY; RECEPTOR BINDING; THYROID MEDULLARY CARCINOMA; TISSUE SECTION;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE, TUMOR; COOPERATIVE BEHAVIOR; HETEROCYCLIC COMPOUNDS, 1-RING; HUMANS; INDIUM RADIOISOTOPES; INHIBITORY CONCENTRATION 50; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN TRANSPORT; RATS; RECEPTOR, CHOLECYSTOKININ B;

EID: 80052593793     PISSN: 16197070     EISSN: 16197089     Source Type: Journal    
DOI: 10.1007/s00259-011-1816-y     Document Type: Article

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