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Calmodulin regulates MGRN1-GP78 interaction mediated ubiquitin proteasomal degradation system.
demonstrate that RGS14 is a novel CaM effector and CaMKII phosphorylation substrate thereby providing new insight into mechanisms by which RGS14 controls plasticity in CA2 neurons.
Both FMRP deficiency in Fmr1(I304N) mice and Fmr1 knockdown impeded the axonal delivery of miR-181d, Map1b, and Calm1 and reduced the protein levels of MAP1B and calmodulin in axons.
The association of calcium-bound calmodulin (CaM) with DREAM is mediated by a short amphipathic amino acid sequence located between residues 29 and 44 on DREAM.
Calcium plays a role in regulating the expression and function of beta-adducin to sustain normal organization of the spectrin-based cytoskeleton and the differentiation properties in keratinocytes through the calmodulin/EGFR/cadherin signaling pathway.
Data suggest that Cys3602 in RyR2 (ryanodine receptor 2) plays important role in activation/termination of Ca2+ release, but it is not essential for calmodulin regulation of RyR2.
CaM plays an active role in shaping both the spatial and temporal aspects of calcineurin-mediated calcium signaling.
Calm1 signaling pathway is essential for the migration of mouse precerebellar neurons.
Ca(2+) binding to calmodulin induces major conformational changes in both IQ motifs and the post-IQ domain and increases flexibility of the myosin-1c tail.
Using mass spectrometry this study identified calmodulin as a calcium-dependent GluN2A binding partner.
new insights into the role of BTK, an important target for autoimmune diseases, in B cell activation
The relationships between the interaction of alphaCaMKII with CaM and the conformational change of alphaCaMKII, were investigated.
LFA-1-mediated firm adhesion under conditions of shear flow requires downstream integrin signaling, which is dependent on calcium/calmodulin and the actin cytoskeleton.
Calmodulin protects Aurora B on the midbody to regulate the fidelity of cytokinesis.
70-kDa heat shock cognate protein hsc70 mediates calmodulin-dependent nuclear import of the sex-determining factor SRY.
Fibronectin stimulates migration through lipid raft dependent NHE-1 activation in mouse embryonic stem cells: involvement of RhoA, Calcium/ calmodulin and ERK.
HCO3- permeability of ANO1 can be dynamically modulated by Ca2+/calmodulin.
Excessive resting[Ca2+ ]i level and lower CaM, CaMPKII expression in hippocampal neurons might participate in the pathogenesis of vascular dementia.
Cx32 is differentially phosphorylated and exists in a complex with SAP97 and CaM.
Calmodulin bound to the first IQ motif is responsible for calcium-dependent regulation of myosin 5a.
the conformational changes of calmodulin upon Ca(2+) and mastoparan binding
MLCK and calmodulin (CaM) co-purify with unphosphorylated SMM from chicken gizzard, suggesting that they are tightly bound.
The relationship between the CALM1 rs3179089 polymorphism and ischemic stroke was studied in the Chinese Han population. CALM1 mRNA expression was higher in patients than controls. The genomic frequency distribution was higher in female patients. GG genotype significantly increased the risk of IS compared with the CC+GC genotype in females.Rs3179089 polymorphism was associated positively with plasma D-dimer in patients.
This review discusses proteins, that in addition to their catalytic, transport, structure, localization or adaptor functions, also have segments resembling the helix-loop-helix EF-hand motifs found in Ca(2+)-binding proteins, such as calmodulin (CaM). [review]
Our analysis shows that Orai1binds to both C-terminal and N-terminal domains of CaM, indicating 1:2 stoichiometry. The Orai1 binding to N-terminal domain of CaM is less stable than that to the C-terminal domain. The binding residues are primarily hydrophobic. These observations are in qualitative agreement to the experiments
The rs12885713 and rs2300496 polymorphisms of the CALM1 gene may both increase the risk of osteoarthritis. (Meta-analysis)
Recent discoveries highlight that a small but rapidly growing set of actin nucleators and related proteins, i.e. factors that have the power to promote the formation of new actin filaments in cells, are tightly controlled by the Ca2+ sensor protein CaM. (Review)
Mutations of lysine residues in calmodulin binding site 2, strongly reduced calmodulin binding and TRPM3 activity indicating the importance of this domain for TRPM3-mediated calcium signaling.
High calmodulin expression is associated with triple negative breast cancer.
G143R substitution enhanced the Cx46-CaM interaction and attenuated its abolishment by Ca(2+) depletion.
Data suggest that TRPM4 exhibits binding sites for calmodulin (CaM) and S100 calcium-binding protein A1 (S100A1) located in very distal part of TRPM4 N-terminus. (TRPM4 = transient receptor potential cation channel subfamily M member 4)
The ataxia related G1107D mutation of the PMCA 3 impairs its calcium pumping function. The mutation affects the interplay of calmodulin with its binding domain on the pump, decreasing its stimulation.
The effect of Ca(2+), domain-specificity, and CaMKII on CaM binding to NaV1.1 has been reported.
Our FRET-based HTS detects RyR binding of accessory proteins calmodulin (CaM) or FKBP12.6...One compound increased FRET and inhibited RyR1, which was only significant at nM [Ca(2+)], and accentuated without CaM present.
Systematic review and meta-analysis of 5 case-control studies involving 2183 osteoarthritis patients 2654 healthy control subjects did not find association between the disease and the rs12885713 polymorphism of CALM1.
We demonstrate that under these conditions the TRPV5 C-terminus is exclusively bound to the CaM C-lobe only, while it confers conformational freedom to the CaM N-lobe. We also show that at elevated calcium levels, additional interactions between the TRPV5 C-terminus and CaM N-lobe occur, resulting in formation of a tight 1:1 complex, effectively making the N-lobe the calcium sensor.
we present a model for TRPV6 CaM-dependent inactivation, which involves a novel so-called "two-tail" mechanism whereby CaM bridges two TRPV6 monomers resulting in closure of the channel pore.
The conservation of homologous residues in helix B of other Kv7 subtypes confer similar competition of Ca(2+)-calmodulin (CaM) with PIP2 binding to their proximal C-termini and suggest that PIP2-CaM interactions converge to Kv7 helix B to modulates channel activity in a Kv7 subtype-dependent manner.
This review provides an overview over our present knowledge concerning the structural and functional aspects of the role of CaM as an adaptor protein and as a regulator of known adaptor/scaffold proteins
Our up-to-date review discusses CaM's role in PI3K signaling at the membrane in KRAS-driven cancers. This is significant since it may help development of K-Ras-specific pharmacology.
Calmodulin is up-regulated and can serve as the potential serum biomarker for predicting the recurrence of nasopharyngeal carcinoma.
cSH2 domain of p85alpha engages its two CaM-binding motifs in the interaction with the N- and C-lobes of CaM as well as the flexible central linker, and our nuclear magnetic resonance experiments provide structural details.
analysis of CaM docked to a functioning KCNQ K(+) channel (KCNQ2 and KCNQ3) [KCNQ2, KCNQ3]
Asp-CaM complex has a critical role in centrosome-pole cohesion and centrosome inheritance in neural stem cells
Basal body formation in the male testes and the production of functional sperm does not rely on the PLP-CaM interaction, whereas production of functional mechanosensory neurons does.
characterized the interdomain motions in the calcium-bound state of calmodulin (Ca(2+)-CaM) using NMR chemical shifts as replica-averaged structural restraints in molecular dynamics simulations
Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin V.
null behavioral phenotype originates in the nervous system and involves a calmodulin function that requires calcium binding to all four sites of the protein
the direct interaction of melatonin with intact calcium-saturated CaM is calcium-dependent; Molecular dynamics simulations follow the dynamics of melatonin in the binding pocket of CaM
potential functional role for calmodulin in regulation of the glycolytic pathway
A mutation to the gene encoding calmodulin deregulates muscle contraction.
Drosophila CaM is able to fully activate inducible nitric oxide synthase (iNOS); moreover, iNOS activation by CaM, like neuronal NOS, is not dependent on Ca2+ being bound to all four Ca2+-binding sites, but has specific and distinct requirements.
Calmodulin/CAMTA/Fbxl4 may mediate a long-term feedback regulation of the activity of Ca(2+)-stimulating G protein-coupled receptor, which could prevent cell damage due to extra Ca(2+) influx.
Thus, Calmodulin and Abelson tyrosine kinase are key signaling molecules working synergistically to transduce both midline attractive and repulsive cues.
This gene encodes a member of the EF-hand calcium-binding protein family. It is one of three genes which encode an identical calcium binding protein which is one of the four subunits of phosphorylase kinase. Two pseudogenes have been identified on chromosome 7 and X. Multiple transcript variants encoding different isoforms have been found for this gene.
, Calmodulin 1 (phosphorylase kinase, delta)
, calmodulin 1 (phosphorylase kinase, delta)
, phosphorylase kinase subunit delta
, phosphorylase kinase, delta subunit
, prepro-calmodulin 1
, Calmodulin-2 A
, Calmodulin-2 B
, CG8472 gene product from transcript CG8472-RC