Web Images Videos Maps News Shopping Gmail more »
Sign in
Scholar Home  
  Advanced Scholar Search
Scholar Preferences
Scholar Results 1 - 10 of about 101 related to Suzuki: Structure, activation, and biology of calpain. (0.08 sec) 

Structure, activation, and biology of calpain

- diabetesjournals.org
K Suzuki, S Hata, Y Kawabata, H Sorimachi - Diabetes, 2004 - Am Diabetes Assoc
Variation in the calpain 10 gene has recently been shown to be associated with
type 2 diabetes by positional cloning. Since then, studies on calpain 10 have
been started in correlation with diabetes and insulin-mediated signaling. ...
Cited by 105 - Related articles - BL Direct - All 4 versions

Interaction of calpastatin with calpain: a review


A Wendt, VF Thompson, DE Goll - Biological Chemistry, 2004 - reference-global.com
Calpastatin is a multiheaded inhibitor capable of inhibit- ing more than one
calpain molecule. Each inhibitory domain of calpastatin has three subdomains, A,
B, and C; A binds to domain IV and C binds to domain VI of the calpains. ...
Cited by 52 - Related articles - BL Direct - All 5 versions

The structure of calpain


H Sorimachi, K Suzuki - JOURNAL OF BIOCHEMISTRY-TOKYO-, 2001 - wwwsoc.nii.ac.jp
Recent very rapid developments in genome and EST projects have identified an
increasing number of gene products homologous to those that were previously
identified by other methods. Calpain is no exception. At the time this ...
Cited by 175 - Related articles - Cached - BL Direct - All 6 versions

Domain III of calpain is a Ca2+-regulated phospholipid-binding domain


P Tompa, Y Emori, H Sorimachi, K Suzuki, P … - Biochemical and Biophysical Research …, 2001 - Elsevier
The X-ray structure of m-calpain shows that domain III of the large subunit is
structurally related to C2 domains, Ca 2+ -regulated lipid binding modules in
many enzymes. To address whether this structural similarity entails ...
Cited by 101 - Related articles - BL Direct - All 6 versions

Calpain-related diseases


D Branca - Biochemical and Biophysical Research …, 2004 - Elsevier
Calpains are calcium-modulated proteases which respond to Ca 2+ signals by
removing limited portions of protein substrates, thereby irreversibly modifying
their function(s). Members of this protease family are present in a variety ...
Cited by 32 - Related articles - All 5 versions

The calpain family and human disease

- cell.com
Y Huang, KKW Wang - Trends in Molecular Medicine, 2001 - Elsevier
The number of mammalian calpain protease family members has grown to 14 on last
count. Overactivation of calpain 1 and calpain 2 (and their small subunit) has
long been tied to acute neurological disorders (eg stroke and traumatic ...
Cited by 226 - Related articles - All 10 versions

Contribution of distinct structural elements to activation of calpain by Ca2+ ions

- jbc.org
A Alexa, Z Bozoky, A Farkas, P Tompa, P … - Journal of Biological Chemistry, 2004 - ASBMB
The effect of Ca 2+ in calpain activation is mediated via several binding sites
in the enzyme molecule. To test the contribution of structural elements
suspected to be part of this Ca 2+ relay system, we made a site-directed ...
Cited by 24 - Related articles - BL Direct - All 4 versions

カルパインと病態


反町洋之, 川畑順子 - 日本薬理学雑誌, 2003 - J-STAGE
度が異なり,相同性の高いそれぞれの大サブユニットμCL,
mCL と,共通の小サブユニット30K からなるヘテロダ
イマーとして機能する(図1,2). ...
Related articles

The calpain system

- physiology.org
DE Goll, VF Thompson, H Li, WEI Wei, J Cong - Physiological reviews, 2003 - Am Physiological Soc
A great deal of information has been obtained on properties of the calpain
system since purification in 1976 of the protein that was later named m-calpain
(83, 84). Books dedicated to Ca 2+ -dependent proteases and the calpains ...
Cited by 779 - Related articles - BL Direct - All 3 versions

The crystal structure of calcium-free human m-calpain suggests an electrostatic switch …

- pnas.org
S Strobl, C Fernandez-Catalan, M Braun, R … - Proceedings of the National Academy of Sciences, 2000 - National Acad Sciences
Calpains (calcium-dependent cytoplasmic cysteine proteinases) are implicated in
processes such as cytoskeleton remodeling and signal transduction. The 2.3-Å
crystal structure of full-length heterodimeric [80-kDa (dI-dIV) + 30-kDa ...
Cited by 226 - Related articles - BL Direct - All 9 versions


Result Page: 

1

2

3

4

5

6

7

8

9

10

Next


 


Go to Google Home - About Google - About Google Scholar

©2009 Google