Kenneth A. Jacobson

Dr. Kenneth A. Jacobson

National Institutes of Health, Bethesda, Maryland, USA
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Research Focus & Metrics

Academic Career Length

45Years (1982-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 December 2001 in Pharmacological Reviews
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BFBertil B. Fredholm
Bertil B. Fredholm
AIAdriaan P. Ijzerman
Adriaan P. Ijzerman
Kenneth A. JacobsonKenneth A. Jacobson
Kenneth A. Jacobson
KKKarl-Norbert Klotz
Karl-Norbert Klotz
JLJoel Linden
Joel Linden

1 March 2006 in Nature Reviews Drug Discovery
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Kenneth A. JacobsonKenneth A. Jacobson
Kenneth A. Jacobson
ZGZhan-Guo Gao
Zhan-Guo Gao

1 March 2011 in Pharmacological Reviews
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BFBertil B. Fredholm
Bertil B. Fredholm
AIAdriaan P. Ijzerman
Adriaan P. Ijzerman
Kenneth A. JacobsonKenneth A. Jacobson
Kenneth A. Jacobson
JLJoel Linden
Joel Linden
CMChrista Müller
Christa Müller
In the 10 years since our previous International Union of Basic and Clinical Pharmacology report on the nomenclature and classification of adenosine receptors, no developments have led to major changes in the recommendations. However, there have been so many other developments that an update is needed. The fact that the structure of one of the adenosine receptors has recently been solved has already led to new ways of in silico screening of ligands. The evidence that adenosine receptors can form homo- and heteromultimers has accumulated, but the functional significance of such complexes remains unclear. The availability of mice with genetic modification of all the adenosine receptors has led to a clarification of the functional roles of adenosine, and to excellent means to study the specificity of drugs. There are also interesting associations between disease and structural variants in one or more of the adenosine receptors. Several new selective agonists and antagonists have become available. They provide improved possibilities for receptor classification. There are also developments hinting at the usefulness of allosteric modulators. Many drugs targeting adenosine receptors are in clinical trials, but the established therapeutic use is still very limited.

1 September 2006 in Pharmacological Reviews
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MAMaria Abbracchio
Maria Abbracchio
Geoffrey BurnstockGeoffrey Burnstock
Geoffrey Burnstock
JBJean-Marie Boeynaems
Jean-Marie Boeynaems
EBEric A. Barnard
Eric A. Barnard
JBJosé L. Boyer
José L. Boyer
GWGary A. Weisman
Gary A. Weisman
There have been many advances in our knowledge about different aspects of P2Y receptor signaling since the last review published by our International Union of Pharmacology subcommittee. More receptor subtypes have been cloned and characterized and most orphan receptors deorphanized, so that it is now possible to provide a basis for a future subdivision of P2Y receptor subtypes. More is known about the functional elements of the P2Y receptor molecules and the signaling pathways involved, including interactions with ion channels. There have been substantial developments in the design of selective agonists and antagonists to some of the P2Y receptor subtypes. There are new findings about the mechanisms underlying nucleotide release and ectoenzymatic nucleotide breakdown. Interactions between P2Y receptors and receptors to other signaling molecules have been explored as well as P2Y-mediated control of gene transcription. The distribution and roles of P2Y receptor subtypes in many different cell types are better understood and P2Y receptor-related compounds are being explored for therapeutic purposes. These and other advances are discussed in the present review.

15 April 2011 in Science
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FXFei Xu
Fei Xu
HWHuixian Wu
Huixian Wu
Vsevolod KatritchVsevolod Katritch
Vsevolod Katritch
GHGye Won Han
Gye Won Han
Kenneth A. JacobsonKenneth A. Jacobson
Kenneth A. Jacobson
RSRaymond Charles Stevens
Raymond Charles Stevens
Activation of G protein–coupled receptors upon agonist binding is a critical step in the signaling cascade for this family of cell surface proteins. We report the crystal structure of the A2A adenosine receptor (A2AAR) bound to an agonist UK-432097 at 2.7 angstrom resolution. Relative to inactive, antagonist-bound A2AAR, the agonist-bound structure displays an outward tilt and rotation of the cytoplasmic half of helix VI, a movement of helix V, and an axial shift of helix III, resembling the changes associated with the active-state opsin structure. Additionally, a seesaw movement of helix VII and a shift of extracellular loop 3 are likely specific to A2AAR and its ligand. The results define the molecule UK-432097 as a “conformationally selective agonist” capable of receptor stabilization in a specific active-state configuration.

4 April 2007 in Nature
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SKSchuichi Koizumi
Schuichi Koizumi
YSYukari Shigemoto-Mogami
Yukari Shigemoto-Mogami
KNKaoru Nasu-Tada
Kaoru Nasu-Tada
YSYouichi Shinozaki
Youichi Shinozaki
KOKeiko Ohsawa
Keiko Ohsawa
KIKazuhide Inoue
Kazuhide Inoue