Results 191 to 200 of about 77,245 (243)

Universal modules for decoding amplitude and frequency of Ca ²⁺ signals in plants

Vergara-Valladares F, Rubio-Meléndez ME, Charpentier M, Michard E, Dreyer I.   +4 more
europepmc   +1 more source

Some of the next articles are maybe not open access.

Related searches:

PEST sequences in calmodulin-binding proteins

Molecular and Cellular Biochemistry, 1995
Many short-lived proteins which are devoid of proteolytic activity contain PEST sequences which are segments along the polypeptide chain that are rich in proline (P), glutamate (E), serine (S) and threonine (T). These designated PEST sequences are believed to be putative intramolecular signals for rapid proteolytic degradation.
Aldrin Gomes, Junor A Barnes
exaly   +3 more sources

CaMBOT: profiling and characterizing calmodulin-binding proteins

Cellular Signalling, 2003
Calmodulin (CaM) is an essential calcium-binding protein that binds to and activates a diverse population of downstream targets (calmodulin-binding proteins; CaMBPs) that carry out its critical signalling functions. In spite of the central importance of CaM in Ca(2+)-mediated signal transduction pathways in all eukaryotes, many CaMBPs remain to be ...
Danton O'Day
exaly   +3 more sources

Calmodulin-binding proteins: A journey of 40 years

Cell Calcium, 2018
The proteins which bind to calmodulin in a Ca2+-dependent and reversible manner are known as calmodulin-binding proteins. These proteins are involved in a multitude of processes in which Ca2+ and calmodulin play crucial roles. Our group elucidated the mechanism and importance of these proteins in normal and diseased conditions.
Rajendra K, Sharma, Sreejit, Parameswaran   +1 more
exaly   +3 more sources

Nuclear Calmodulin-Binding Proteins in Rat Neurons

Journal of Neurochemistry, 1993
Abstract: By using a 125I‐calmodulin overlay assay, three major high‐affinity calmodulin‐binding proteins, showing apparent molecular masses of 135, 60, and 50 kDa, have been detected in purified nuclear fractions isolated from rat neurons. It has been shown that after extraction of the nuclei with nucleases and high salt, all these proteins remain ...
M J Pujol, M Vendrell, J Serratosa
exaly   +3 more sources

PLANT-SPECIFIC CALMODULIN-BINDING PROTEINS

Annual Review of Plant Biology, 2005
Calmodulin CaM is a ubiquitous Ca2+sensor protein (16 to 18 kD) with no catalytic activity that can, upon binding Ca2+, activate target proteins involved in various cellular processes. The CaM prototype is comprised of two globular domains connected with a long flexible helix. Each globular domain contains a pair of intimately linked EF hands.
Bouche, Nicolas, Yellin, Ayelet, Snedden, Wayne A., Fromm, Hillel   +3 more
openaire   +4 more sources

Calmodulin-binding proteins of Saccharomycescerevisiae

Biochemical and Biophysical Research Communications, 1990
The subcellular distribution of calmodulin-binding proteins in the soluble, plasma membrane, and nuclear fractions of Saccharomyces cerevisiae was analyzed with a gel binding assay using 125I-labeled calmodulin. Over 20 binding proteins were detected. The calmodulin-binding protein profiles were markedly different among the fractions.
Y S, Liu, Y, Yamashita, E, Tsuchiya, T, Miyakawa   +3 more
openaire   +2 more sources

Extracellular calmodulin-binding proteins in plants: purification of a 21-kDa calmodulin-binding protein

Planta, 1996
A 21-kDa calmodulin (CaM)-binding protein and a 19-kDa calmodulin-binding protein were detected in 0.1 M CaCl2 extracts of Angelica dahurica L. suspension-cultured cells and carrot (Daucus carota L.) suspension-cultured cells, respectively, using a biotinylated cauliflower CaM gel-overlay technique in the presence of 1 mM Ca2+.
Tang, Jun, Wu, Shupin, Bai, Juan, Sun, Daye   +3 more
openaire   +2 more sources