Hochschulschrift
Eigenschaften des Insulinrezeptors in isolierten Rattenhepatocyten, Untersuchungen zur Struktur des Rezeptors und zur Internalisierung von Insulin und Rezeptor
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Maße
-
21 cm
- Umfang
-
150 S.
- Sprache
-
Deutsch
- Anmerkungen
-
Ill., graph. Darst.
Tübingen, Univ., Diss., 1984
- Schlagwort
-
Leberzelle
Insulinrezeptoren
Leberepithelzelle
Insulinrezeptor
- Urheber
-
Klotz, Karl-Norbert
- Inhaltsverzeichnis
- Rechteinformation
-
Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.
- Letzte Aktualisierung
-
11.06.2025, 14:01 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Objekttyp
- Hochschulschrift
Beteiligte
- Klotz, Karl-Norbert
Ähnliche Objekte (12)
Regulation von G-Protein-gekoppelten Rezeptoren
Physical coupling of N-formyl peptide chemoattractant receptors to G protein is not affected by desensitization
Neutrophil chemoattractant receptors and the membrane skeleton
Cytoskeletal regulation of chemotactic receptors: Molecular complexation of N-formyl peptide receptors with G proteins and actin
The glycoprotein nature of A1 adenosine receptors
A\(_2B}\) adenosine receptor signaling in MDA-MB-231 breast cancer cells: Mechanism of A\(_2B}\)-mediated reduction of ERK1/2 phosphorylation
Der A2B-Adenosinrezeptor und MAP-Kinase Aktivität in MDA-MB-231-Brustkrebszellen
The interaction of N-formyl peptide chemoattractant receptors with the membrane skeleton is energy-dependent
Functional characterization of A1 adenoosine receptors by photoaffinity labelling
Agonist photoaffinity labeling of A1 adenosine receptors: Persistent activation reveals spare receptors
Mechanism of A2 adenosine receptor activation. I. Blockade of A2 adenosine receptors by photoaffinity labeling
G protein coupled A1 adenosine receptors in coated vesicles of mammalian brain. Characterization by radioligand binding and photoaffinity labeling
Regulation von G-Protein-gekoppelten Rezeptoren
Physical coupling of N-formyl peptide chemoattractant receptors to G protein is not affected by desensitization
Neutrophil chemoattractant receptors and the membrane skeleton
Cytoskeletal regulation of chemotactic receptors: Molecular complexation of N-formyl peptide receptors with G proteins and actin
The glycoprotein nature of A1 adenosine receptors
A\(_2B}\) adenosine receptor signaling in MDA-MB-231 breast cancer cells: Mechanism of A\(_2B}\)-mediated reduction of ERK1/2 phosphorylation
Der A2B-Adenosinrezeptor und MAP-Kinase Aktivität in MDA-MB-231-Brustkrebszellen
The interaction of N-formyl peptide chemoattractant receptors with the membrane skeleton is energy-dependent
Functional characterization of A1 adenoosine receptors by photoaffinity labelling
Agonist photoaffinity labeling of A1 adenosine receptors: Persistent activation reveals spare receptors
Mechanism of A2 adenosine receptor activation. I. Blockade of A2 adenosine receptors by photoaffinity labeling
G protein coupled A1 adenosine receptors in coated vesicles of mammalian brain. Characterization by radioligand binding and photoaffinity labeling
Regulation von G-Protein-gekoppelten Rezeptoren
Physical coupling of N-formyl peptide chemoattractant receptors to G protein is not affected by desensitization
Neutrophil chemoattractant receptors and the membrane skeleton
Cytoskeletal regulation of chemotactic receptors: Molecular complexation of N-formyl peptide receptors with G proteins and actin
The glycoprotein nature of A1 adenosine receptors
A\(_2B}\) adenosine receptor signaling in MDA-MB-231 breast cancer cells: Mechanism of A\(_2B}\)-mediated reduction of ERK1/2 phosphorylation
Der A2B-Adenosinrezeptor und MAP-Kinase Aktivität in MDA-MB-231-Brustkrebszellen
The interaction of N-formyl peptide chemoattractant receptors with the membrane skeleton is energy-dependent
Functional characterization of A1 adenoosine receptors by photoaffinity labelling
Agonist photoaffinity labeling of A1 adenosine receptors: Persistent activation reveals spare receptors
Mechanism of A2 adenosine receptor activation. I. Blockade of A2 adenosine receptors by photoaffinity labeling