Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 232,525,200 papers from all fields of science
Search
Sign In
Create Free Account
beta-Adrenergic Receptor Kinases
Known as:
Receptor Kinases, beta-Adrenergic
, beta-Adrenergic Receptor Kinases [Chemical/Ingredient]
, beta adrenergic receptor kinase
Expand
G-protein-coupled receptor kinases that mediate agonist-dependent PHOSPHORYLATION and desensitization of BETA-ADRENERGIC RECEPTORS.
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
7 relations
In Blood
Process of secretion
antagonists & inhibitors
aspects of radiation effects
Expand
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2005
2005
Adenovirus-Mediated Expression of &bgr;-Adrenergic Receptor Kinase C-Terminus Reduces Intimal Hyperplasia and Luminal Stenosis of Arteriovenous Polytetrafluoroethylene Grafts in Pigs
Zhengyu Luo
,
G. Akita
,
+6 authors
Canwen Jiang
Circulation
2005
Corpus ID: 34209077
Background—Hemodialysis vascular access dysfunction is the single most important cause of morbidity in kidney hemodialysis…
Expand
2004
2004
Altered β2‐adrenergic regulation of T cell activity after allergen challenge in asthma
I. Heijink
,
M. van den Berge
,
E. Vellenga
,
J. D. de Monchy
,
D. Postma
,
H. Kauffman
Clinical and Experimental Allergy
2004
Corpus ID: 22038657
Background Airway inflammation in asthma is orchestrated by recruitment of T helper (Th)2 lymphocytes to the lung and subsequent…
Expand
1997
1997
Heterogeneity in beta-adrenergic receptor kinase expression in the lung accounts for cell-specific desensitization of the beta2-adrenergic receptor.
D. McGraw
,
S. Liggett
Journal of Biological Chemistry
1997
Corpus ID: 20572870
The principal mechanism of homologous desensitization of the beta-adrenergic receptor (beta2AR) is phosphorylation of the…
Expand
1996
1996
G-protein βγ Subunits Mediate Specific Phosphorylation of the Protein-tyrosine Phosphatase SH-PTP1 Induced by Lysophosphatidic Acid*
F. Gaits
,
R. Li
,
J. Bigay
,
A. Ragab
,
J. Ragab-Thomas
,
H. Chap
Journal of Biological Chemistry
1996
Corpus ID: 43019706
SH-PTP1 is a protein-tyrosine phosphatase preferentially expressed in hematopoietic cells and bearing two SH2 (rc homology-2…
Expand
Highly Cited
1996
Highly Cited
1996
Interactions of Phosducin with Defined G Protein -Subunits (*)
S. Müller
,
A. Straub
,
S. Schröder
,
P. Bauer
,
M. Lohse
Journal of Biological Chemistry
1996
Corpus ID: 3040626
Phosducin has recently been identified as a cytosolic protein that interacts with the β-subunits of G proteins and thereby may…
Expand
1996
1996
Partially Purified RhoA‐Stimulated Phospholipase D Activity Specifically Binds to Phosphatidylinositol 4,5‐Bisphosphate
T. Yokozeki
,
H. Kuribara
,
T. Katada
,
K. Touhara
,
Y. Kanaho
Journal of Neurochemistry
1996
Corpus ID: 454082
Abstract: Phosphatidylinositol 4,5‐bisphosphate (PIP2) is absolutely required for the ADP‐ribosylation factor‐stimulated…
Expand
1994
1994
An approach to the study of G-protein-coupled receptor kinases: an in vitro-purified membrane assay reveals differential receptor specificity and regulation by G beta gamma subunits.
G. Pei
,
M. Tiberi
,
M. Caron
,
R. Lefkowitz
Proceedings of the National Academy of Sciences…
1994
Corpus ID: 43466844
Phosphorylation of GTP-binding-regulatory (G)-protein-coupled receptors by specific G-protein-coupled receptor kinases (GRKs) is…
Expand
1994
1994
Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes.
G. Calabrese
,
M. Sallese
,
A. Stornaiuolo
,
L. Stuppia
,
G. Palka
,
A. de Blasi
Genomics
1994
Corpus ID: 23085608
Two types of proteins play a major role in determining homologous desensitization of G-coupled receptors: beta-adrenergic…
Expand
1994
1994
Structure of the pleckstrin homology domain from beta-spectrin.
M. Macias
,
A. Musacchio
,
H. Ponstingl
,
M. Nilges
,
M. Saraste
,
H. Oschkinat
Nature
1994
Corpus ID: 25905429
The 'pleckstrin homology' or PH domain is a 100-residue protein module. It is present in many kinases, different isoforms of…
Expand
1989
1989
Substitution of an extracellular cysteine in the beta 2-adrenergic receptor enhances agonist-promoted phosphorylation and receptor desensitization.
S. Liggett
,
M. Bouvier
,
B. O'dowd
,
M. Caron
,
R. Lefkowitz
,
A. Deblasi
Biochemical and Biophysical Research…
1989
Corpus ID: 12796343
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE