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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Calcium ATPase at 60A

Top mentioned proteins: ATPase, CAN, V1a, Phospholamban, ACID
Papers on SERCA
Sarcoplasmic Reticulum Structure and Functional Properties that Promote Long-Lasting Calcium Sparks.
Bers et al., Davis, United States. In Biophys J, Feb 2016
We varied the number of functional RyRs in the single cluster, diffusion within the SR network, diffusion between network and junctional SR, cytosolic Ca diffusion, SERCA uptake activity, and RyR open probability.
ER functions of oncogenes and tumor suppressors: Modulators of intracellular Ca(2+) signaling.
Bultynck et al., Leuven, Belgium. In Biochim Biophys Acta, Feb 2016
An important aspect of this is the identification of several major oncogenes, including Bcl-2, Bcl-XL, Mcl-1, PKB/Akt, and Ras, and tumor suppressors, such as p53, PTEN, PML, BRCA1, and Beclin 1, as direct and critical regulators of Ca(2+)-transport systems located at the ER membranes, including IP3 receptors and SERCA Ca(2+) pumps.
Cylindrical Spirals in Skeletal Muscles Originate From the Longitudinal Sarcoplasmic Reticulum.
Yan et al., Jinan, China. In J Neuropathol Exp Neurol, Feb 2016
Immunohistochemical studies revealed subsarcolemmal immunoreactivity for sarco/endoplasmic reticulum Ca(2+)-ATPase 1 (SERCA 1) in the longitudinal SR, but no immunoreactivity for calsequestrin in the terminal cisternae or type 1 ryanodine receptor (RYR1) in the junctional SR.
Calcium regulation of HCN channels supports persistent activity in a multiscale model of neocortex.
Lytton et al., United States. In Neuroscience, Jan 2016
Metabotropic glutamate receptors (mGluR) produced inositol triphosphate (IP3) which caused the release of Ca(2+) from endoplasmic reticulum (ER) stores, with reuptake by sarco/ER Ca(2+)-ATP-ase pumps (SERCA), and influence on HCN channels.
Phospholamban and sarcolipin: Are they functionally redundant or distinct regulators of the Sarco(Endo)Plasmic Reticulum Calcium ATPase?
Periasamy et al., Orlando, United States. In J Mol Cell Cardiol, Jan 2016
UNASSIGNED: In muscle, the Sarco(Endo)plasmic Reticulum Calcium ATPase (SERCA) activity is regulated by two distinct proteins, PLB and SLN, which are highly conserved throughout vertebrate evolution.
Sarcolipin is a novel regulator of muscle metabolism and obesity.
Periasamy et al., Orlando, United States. In Pharmacol Res, Dec 2015
The purpose of this review is to highlight the role of sarcolipin (SLN), a regulator of SERCA pump, in muscle thermogenesis and metabolism.
The calcium-signaling toolkit: Updates needed.
Vanden Abeele et al., Villeneuve-d'Ascq, France. In Biochim Biophys Acta, Dec 2015
These concepts have emerged by the use of ER stressor agents that decrease the ER Ca(2+) pool by inhibiting SERCA pumps.
Vascular nitric oxide: Beyond eNOS.
Leung et al., Hong Kong, Hong Kong. In J Pharmacol Sci, Oct 2015
NO regulates the degree of contraction of vascular smooth muscle cells mainly by stimulating soluble guanylyl cyclase (sGC) to produce cyclic guanosine monophosphate (cGMP), although cGMP-independent signaling [S-nitrosylation of target proteins, activation of sarco/endoplasmic reticulum calcium ATPase (SERCA) or production of cyclic inosine monophosphate (cIMP)] also can be involved.
Phosphoenolpyruvate Is a Metabolic Checkpoint of Anti-tumor T Cell Responses.
Kaech et al., New Haven, United States. In Cell, Oct 2015
We discovered a new role for the glycolytic metabolite phosphoenolpyruvate (PEP) in sustaining T cell receptor-mediated Ca(2+)-NFAT signaling and effector functions by repressing sarco/ER Ca(2+)-ATPase (SERCA) activity.
A mathematical model of the calcium transient in urinary bladder smooth muscle cells.
Manchanda et al., In Conf Proc Ieee Eng Med Biol Soc, Aug 2015
The plasma membrane Ca(2+)ATPase (PMCA) pump and sarco/endoplasmic reticulum Ca(2+)ATPase (SERCA) pump are responsible for lowering [Ca(2+)]i which leads to relaxation of smooth muscle.
Reactive oxygen and nitrogen species disturb Ca(2+) oscillations in insulin-secreting MIN6 β-cells.
Pedersen et al., Padova, Italy. In Islets, Aug 2015
Application of the sarcoplasmic/endoplasmic reticulum Ca(2+) ATPase (SERCA) inhibitor thapsigargin modifies the Ca(2+) response to high concentrations of ROS/RNS.
A micropeptide encoded by a putative long noncoding RNA regulates muscle performance.
Olson et al., Dallas, United States. In Cell, Mar 2015
MLN shares structural and functional similarity with phospholamban (PLN) and sarcolipin (SLN), which inhibit SERCA, the membrane pump that controls muscle relaxation by regulating Ca(2+) uptake into the sarcoplasmic reticulum (SR).
Structure and mechanism of Zn2+-transporting P-type ATPases.
Gourdon et al., Århus, Denmark. In Nature, 2014
These findings suggest a mechanistic link between PIB-type Zn(2+)-ATPases and PIII-type H(+)-ATPases and at the same time show structural features of the extracellular release pathway that resemble PII-type ATPases such as the sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase (SERCA) and Na(+), K(+)-ATPase.
Seipin promotes adipose tissue fat storage through the ER Ca²⁺-ATPase SERCA.
Huang et al., Beijing, China. In Cell Metab, 2014
Here, we show that Seipin physically interacts with the sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA) in both Drosophila and man.
Ionic leakage underlies a gain-of-function effect of dominant disease mutations affecting diverse P-type ATPases.
Cook et al., Los Angeles, United States. In Nat Genet, 2014
Using a Drosophila melanogaster genetic screen, we identified a dominant mutation altering the PAII member sarcoendoplasmic reticulum Ca(2+) ATPase (SERCA).
Analysis of a zebrafish behavioral mutant reveals a dominant mutation in atp2a1/SERCA1.
Downes et al., In Genesis, 2010
study showed that accordian acc(dta5) mutants harbor a novel mutation in atp2a1; indicate the acc(dta5) mutation diminishes SERCA1 function to a greater degree than other acc alleles through haploinsufficient or dominant-negative molecular mechanisms
Conditional mutations in SERCA, the Sarco-endoplasmic reticulum Ca2+-ATPase, alter heart rate and rhythmicity in Drosophila.
Ramaswami et al., Tucson, United States. In J Comp Physiol B, 2006
Heart beat frequency is strikingly reduced in mutant animals following dSERCA inactivation
Analysis of conditional paralytic mutants in Drosophila sarco-endoplasmic reticulum calcium ATPase reveals novel mechanisms for regulating membrane excitability.
Ramaswami et al., Tucson, United States. In Genetics, 2005
Analysis of conditional paralytic mutants in SERCA reveals novel mechanisms for regulating membrane excitability.
A mutation in serca underlies motility dysfunction in accordion zebrafish.
Mandel et al., Stony Brook, United States. In Dev Biol, 2005
concluded that the motility dysfunction in embryonic and larval accordion zebrafish stems directly from defective calcium transport in skeletal muscle due to mutation in SERCA rather than defective CNS drive.
accordion, a zebrafish behavioral mutant, has a muscle relaxation defect due to a mutation in the ATPase Ca2+ pump SERCA1.
Kuwada et al., Ann Arbor, United States. In Development, 2004
encodes the sarco(endo)plasmic reticulum Ca2+-ATPase 1 (SERCA1), a Ca2+ pump found in the muscle sarcoplasmic reticulum (SR) that is responsible for pumping Ca2+ from the cytosol back to the SR
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