scispace - formally typeset
L

Lutz Birnbaumer

Researcher at National Institutes of Health

Publications -  524
Citations -  46988

Lutz Birnbaumer is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Adenylyl cyclase & G protein. The author has an hindex of 114, co-authored 511 publications receiving 44901 citations. Previous affiliations of Lutz Birnbaumer include Research Triangle Park & The Catholic University of America.

Papers
More filters
Journal ArticleDOI

Receptor-effector coupling by G proteins

TL;DR: To facilitate the reading of this review, the various subtopics of this rapidly expanding field are presented, each of which is organized as a self-contained sub-chapter that can be read independently of the others.
Journal ArticleDOI

Letter to the EditorNomenclature of Voltage-Gated Calcium Channels

TL;DR: A new nomen-ties of the channel complex, the pharmacological and clature of voltage-gated Ca 2ϩ channels, which electrophysiological diversity of Ca 2 ϩ channels arises is more systematic and mimics the well-defined K ϩ primarily from the existence of multiple forms of ␣ 1 sub-channel nomenclature.
Journal ArticleDOI

The TRP channels, a remarkably functional family.

TL;DR: TRP cation channels display an extraordinary assortment of selectivities and activation mechanisms, some of which represent previously unrecognized modes for regulating ion channels.
Journal ArticleDOI

The Glucagon-sensitive Adenyl Cyclase System in Plasma Membranes of Rat Liver V. AN OBLIGATORY ROLE OF GUANYL NUCLEOTIDES IN GLUCAGON ACTION

TL;DR: It is concluded that guanyl nucleotides play a specific and obligatory role in the activation of adenyl cyclase by glucagon, and bind at sites, distinct from the glucagon binding sites, that appear to regulate both the response ofadenyl cycling to glucagon and the actions of fluoride ion on this system.
Journal ArticleDOI

trp, a Novel Mammalian Gene Family Essential for Agonist-Activated Capacitative Ca2+ Entry

TL;DR: It is proposed that trp homologs are subunits of CCE channels, not unlike those of classical voltage-gated ion channels.