Results 221 to 230 of about 2,710,839 (274)

Calcium and Ca<sup>2+</sup>-Binding Proteins Regulate Microtubule and Cytoskeletal Dynamics During Mammalian Corticogenesis. [PDF]

open access: yesBrain Sci
De la Merced-García DS   +4 more
europepmc   +1 more source

AMPK phosphorylation proceeds through hierarchical proteoform cascades revealed by integrated mass spectrometry. [PDF]

open access: yesSci Adv
Krichel B   +8 more
europepmc   +1 more source
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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

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.
Sreejit Parameswaran
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

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

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