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CRY1 encodes a flavin adenine dinucleotide-binding protein that is a key component of the circadian core oscillator complex, which regulates the circadian clock. Additionally we are shipping CRY1 Antibodies (75) and CRY1 Kits (34) and many more products for this protein.
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Human CRY1 Protein expressed in Wheat germ - ABIN1350417
Santagata, Maire, Idbaih, Geffers, Correll, Holton, Quackenbush, Ligon: CRX is a diagnostic marker of retinal and pineal lineage tumors. in PLoS ONE 2009
CRYs' C termini are essential for nuclear localization but not necessary for the suppression of CLOCK/BMAL1 (show ARNTL Proteins) activation
we investigated the structure/function relationships of Xenopus laevis CRY1 (xCRY1) and xCRY2 (show CRY2 Proteins) in cultured cells
Cry1 is expressed in the olfactory bulb of newborn and juvenile rabbits.
Altered CRY1 and CRY2 (show CRY2 Proteins) expression patterns and the interplay with the genetic landscape in colon cancer cells may underlie phenotypic divergence.
possible circadian rhythm in full-term placental expression
Given the distinct characteristics of the C-terminal tails of the CRY1 and CRY2 (show CRY2 Proteins) proteins, our study addresses a long-standing hypothesis that the ratio of these two CRY (show CRY2 Proteins) molecules affects the clock period.
Overexpression of CRY1 protects against the development of atherosclerosis via the TLR/NFkappaB pathway
Collectively, these data show that KPNB1 (show KPNB1 Proteins) is required for timely nuclear import of PER/CRY (show CRY2 Proteins) in the negative feedback regulation of the circadian clock.
these observations suggest a biologically plausible season-dependent association between SNPs at CRY1, CRY2 and MTNR1B and glucose homeostasis.
CRY1 and CRY2 (show CRY2 Proteins) variants showed nominal association with the metabolic syndrome components, hypertension and triglyceride levels.
In men undergoing acute total sleep deprivation, there was increased methylation in the promoter of CRY1 in adipose tissue compared with controls. Also decreased gene expression in skeletal muscle.
SNPs in CRY1 were significantly associated with overall survival in Chinese hepatocellular carcinoma patients.
Study reveals an interaction between a CRY1 variant and carbohydrate intake for glucose metabolism.
polyamines control the circadian period in cultured cells and animals by regulating the interaction between the core clock repressors PER2 (show PER2 Proteins) and CRY1
Data show that cryptochrome Cry1 and Cry2 (show CRY2 Proteins) expression must be circadian and appropriately phased to support rhythms, and arginine vasopressin (AVP (show AVP Proteins)) receptor signaling is required to impose circuit-level circadian function.
uncovered a novel biological role for CUL4A (show CUL4A Proteins)-DDB1 (show DDB1 Proteins)-CDT2 E3 ligase that regulates molecular circadian behaviors via promoting ubiquitination-dependent degradation of CRY1
Data suggest that cryptochromes (Cry1 and Cry2 (show CRY2 Proteins)) mediate periodic binding of Ck2b (show CSNK2B Proteins) (casein kinase 2beta) to Bmal1 (aryl hydrocarbon receptor nuclear translocator-like (show ARNTL Proteins) protein) and thus inhibit Bmal1 (show ARNTL Proteins)-Ser90 phosphorylation by Ck2a (show CSNK2A1 Proteins) (casein kinase 2alpha).
demonstrate that genotoxic stress stimulates Cry1 phosphorylation and its deubiquitination by Herpes virus associated ubiquitin-specific protease (Hausp (show USP7 Proteins), a.k.a Usp7 (show USP7 Proteins)), stabilizing Cry1 and shifting circadian clock time
Cry1/Cry2-deficient mice had significantly lower N6- methyladenosine methylation of RNA and lost the circadian rhythm of N6-methyladenosine levels in RNA.
these results suggested that the overexpression of CRY1 inhibited sleep deprivation-induced vascular inflammation that might be associated with NF-kappaB (show NFKB1 Proteins) and cAMP/PKA pathways.
These results suggest that CRY1 fulfills its role as an essential circadian repressor by sequestering the C-terminal transactivation domain of BMAL1 (show ARNTL Proteins) from coactivators.
Report compression of daily activity time in Cry1 mutant mice.
These data illustrate that in vivo modulation by metabolites in the cellular environment may play an important role in cryptochrome signaling.
For growth under a canopy, where blue light is diminished, CRY1 and CRY2 perceive this change and respond by directly contacting two bHLH transcription factors, PIF4 and PIF5.
CRY1 represses auxin biosynthesis in response to elevated temperature through PIF4.
CRY1 inhibits hypocotyl elongation in blue light through CNT1-mediated repression of the auxin/BR/GAresponsive gene expression.
Reactive oxygen species formation results from cry1 activation and induces cell death in insect cell cultures.
The study shows that ATP binding and aspartate protonation enhance photoinduced electron transfer in plant CRY1.
photoreduction-deficient Trp (show TBPL1 Proteins)-triad mutations of CRY1 remained physiologically and biochemically active in Arabidopsis plants.
Based on the loss of degradation of cry2 (show CRY2 Proteins) after prolonged darkness and loss of reversibility of photoactivated cry1 by a pulse of green light, we estimate the in vivo half-lives of the signaling states of cry1 and cry2 (show CRY2 Proteins) to be in the range of 5 and 16 min.
Data indicate that the green light (GL) opposition of red light (RL) responses persists in phyA, phyB, cry1cry2 and phot2 mutants, and the response requires phot1 and NPH3.
Perception of light by phyA, cry1 or phyB activates ROC1; this in turn reduces the intensity of brassinosteroid signalling and fine-tunes seedling de-etiolation.
This gene encodes a flavin adenine dinucleotide-binding protein that is a key component of the circadian core oscillator complex, which regulates the circadian clock. The encoded protein is widely conserved across plants and animals. Loss of the related gene in mouse results in a shortened circadian cycle in complete darkness.
cryptochrome 1 (photolyase-like)
, cryptochrome 2 (photolyase-like)
, cryptochrome 1