000 01597 a2200409 4500
005 20250512022134.0
264 0 _c19880907
008 198809s 0 0 eng d
022 _a0027-8424
024 7 _a10.1073/pnas.85.15.5478
_2doi
040 _aNLM
_beng
_cNLM
100 1 _aFraser, C M
245 0 0 _aSite-directed mutagenesis of human beta-adrenergic receptors: substitution of aspartic acid-130 by asparagine produces a receptor with high-affinity agonist binding that is uncoupled from adenylate cyclase.
_h[electronic resource]
260 _bProceedings of the National Academy of Sciences of the United States of America
_cAug 1988
300 _a5478-82 p.
_bdigital
500 _aPublication Type: Journal Article
650 0 4 _aAdenylyl Cyclases
_xmetabolism
650 0 4 _aAnimals
650 0 4 _aAsparagine
_xgenetics
650 0 4 _aAspartic Acid
_xgenetics
650 0 4 _aBase Sequence
650 0 4 _aBinding, Competitive
650 0 4 _aCatecholamines
_xmetabolism
650 0 4 _aCell Line
650 0 4 _aGene Expression Regulation
650 0 4 _aGuanine Nucleotides
_xpharmacology
650 0 4 _aHumans
650 0 4 _aMolecular Sequence Data
650 0 4 _aMutation
650 0 4 _aReceptors, Adrenergic, beta
_xgenetics
650 0 4 _aSequence Homology, Nucleic Acid
700 1 _aChung, F Z
700 1 _aWang, C D
700 1 _aVenter, J C
773 0 _tProceedings of the National Academy of Sciences of the United States of America
_gvol. 85
_gno. 15
_gp. 5478-82
856 4 0 _uhttps://doi.org/10.1073/pnas.85.15.5478
_zAvailable from publisher's website
999 _c2846527
_d2846527