Molecular Pain 本书特色
Molecular Pain is the first book to focus on molecular and synaptic
mechanisms for pain transmission, modulation and plasticity. Unlike
traditional textbooks about pain, this book covers recent progress in
neuroscience and relates these developments to the basic mechanisms of
chronic pain. The book also discusses current pain medicine and alternative
pain treatments such as acupuncture.
Edited by a leading neuroscientist and pain researcher, Molecular Pain
includes contributions by more than thirty international science experts
from eight different countries. The book's thirty-four chapters cover a wide
spectrum of pain, analgesia, and neuroscience, and present chronic pain as a
major health concern and a dynamic area of research.
Complete with 165 illustrations, Molecular Pain is a concise and
comprehensive review of recent progress in the field of pain. This book
is an invaluable reference work and textbook for advanced undergraduate
students, graduate and medical students, and researchers in neuroscience,
pain, animal behavior, anesthesiology and medicine.
Min Zhuo, PhD, is a Full Professor in the Department of Physiology,
Faculty of Medicine, and the Centre for the Study of Pain at the University
of Toronto, Ontario, Canada. He is Canada Research Chair Tier I in Pain
and Cognition and EJLB-CIHR Michael Smith Chair in Neurosciences and
Mental Health: He is also the Changjiang Scholar at Fudan University in
Shanghai, China. He acts as Editor-in-Chief of Molecular Pain, the first
online journal in the field (http://www. molecularpain.com).
Molecular Pain 节选
otein Kinases and
P h osp h atas es
Ronald A. Merrill, Stefan Strack
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Dr. Strack is an Associate Professor in the Department of
Pharmacology, University of Iowa, Iowa City, USA. He gradu-
ated from the University of W'tirzburg and obtained a M.S. in
Computer Science at the University at Albany, State University
of New York. After gaining a Ph.D. in Biology at the same
institution, he pursued postdoctoral training at Vanderbilt Uni-
versity.
MAJOR CONTRIBUTIONS
1. Strack S, Ruediger R, Walter G, Dagda RK, Barwacz CA,
Cribbs JT. 2002. Protein phosphatase 2A holoenzyme assem-
bly. Identification of contacts between B-family regulatory
and scaffolding A subunits. JBiol Chern, 277(23):20750-20755.
2. Strack S. 2002. Overexpression of the protein phosphatase
2A regulatory subunit B[gamma] promotes neuronal differ-
entiation by activating the MAP kinase cascade. JBiol Chem,
277(44):41525-41532.
3. Dagda RK, Zaucha JA, Wadzinski BE, Strack S. 2003. A
developmentally regulated, neuron-specific splice variant of
the variable subunit B-beta targets protein phosphatase 2A to
mitochondria and modulates apoptosis, d Biol Chem,
278:24976-24985.
4. Strack S, Cribbs JT, Gomez L. 2004. Critical role for protein
phosphatase 2A heterotrimers in mammalian cell survival, d
Biol Chem, 279:47732-47739.
5. Dagda RK, Barwacz CA, Cribbs JT, Strack S. 2005. Un-
folding-resistant translocase targeting: a novel mechanism
for outer mitochondrial membrane localization exempli-
fied by the Bβ2 regulatory subunit of protein phosphatase
2A. J Biol Chem, 280:27375-27382.
MAIN TOPICS
Classification
Kinases
Phosphatases
Structure and catalytic mechanisms
Kinases
Phosphatases
Substrate specificity
Regulation
Kinases
Phosphatases
Phosphorylation in long-term synaptic plasticity
Kinase/phosphatase complexes in synaptic plasticity
Receptor tyrosine kinases in neuronal function and
plasticity
Kinases and phosphatases in addiction
SUMMARY
Reversible protein phosphorylation is the most
prominent posttranslational regulatory mechanism
in eukaryotes. Protein kinases catalyze the addition
of a phosphoester group to proteins while protein
phosphatases oppose kinase activity by removing
phosphates. The recent sequencing of numerous
genomes has allowed for the identification and
classification of most if not all kinases and phos-
phatases. Kinases represent a large group of en-
zymes (>500 in humans) and are classified by se-
quence similarity, with most kinases containing a
conserved catalytic domain. Phosphatases are a
smaller group (-140 in humans) and are classified
by their catalytic mechanisms, as well as sequence
similarity. Most kinases and phosphatases contain
domains involved in intramolecular regulation of
the catalytic domain. In contras
