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1 a in the C-terminal activation domain of the CLOCK protein.
2 by a transcriptional complex containing the CLOCK protein.
3 define important functional domains of this clock protein.
4 ipping and deletion of 51 amino acids in the CLOCK protein.
5 y to fulfill the biological function of this clock protein.
6 mporal, intracellular behaviors of mammalian clock proteins.
7 ong-term perturbation in the cycles of these clock proteins.
8 been identified that selectively target core clock proteins.
9 enges requires assessing levels of circadian clock proteins.
10 cterize antibodies against several circadian clock proteins.
11 n precise adjustment of expression levels of clock proteins.
12 ty and subcellular localization of essential clock proteins.
13 he nuclear translocation and/or stability of clock proteins.
14 ses regulating the function and stability of clock proteins.
15 Y 1 and CRY 2, are known to function as core clock proteins.
16 odicity from posttranslational regulation of clock proteins.
17 coexpressed in each PER-positive neuron, and clock protein and mRNA oscillations are all suppressed i
19 have also revealed novel interactions among clock proteins and new partners that couple the clock to
21 other hand, a similarity between eukaryotic clock proteins and the cyanobacterial KaiC protein is th
22 CYC, determined the interactions of the four clock proteins, and calculated their absolute levels as
23 al modifications (such as ubiquitination) of clock proteins are critical in maintaining the precision
26 t because few simple models exist, and known clock proteins are not conserved across phylogenetic kin
27 system against specific pathogens, the core-clock proteins as well as cells in which they are expres
28 he second example of a PAS domain-containing clock protein (besides Drosophila PERIOD), which suggest
29 nd CRY2G351D; the former shows deficiency in clock protein binding and is required for repression by
32 h the molecular clock, most notably the core clock proteins BMAL1, CLOCK, and REV-ERBalpha, control f
33 ional mechanisms, such as phosphorylation of clock proteins by casein kinase 1 (CK1) and glycogen syn
34 expressing a mutant form of the Arabidopsis clock protein CCA1 that cannot be phosphorylated by CK2,
36 log of the Caenorhabditis elegans biological clock protein CLK-2 (HCLK2), associated with and was hyd
39 cillator in which LdpA is a component of the clock protein complex that senses the redox state of a c
41 meters based on experimental data concerning clock protein concentrations within a cell, we find accu
42 first time that skin cells express circadian clock proteins constitutively although regulation of the
43 mechanism, in which cycling of the essential clock proteins CRY1 and CRY2 is thought to be necessary.
44 ss protein interacts with both the circadian clock protein cryptochrome 2 and with the cell cycle che
45 n in mouse slows the degradation of the core clock protein Cryptochrome, lengthening the period of th
47 of a repressive complex, defined by the core clock proteins cryptochrome 1 (CRY1):CLOCK:BMAL1, plays
49 e in vivo characterization of the Drosophila CLOCK protein (dCLOCK), a transcription factor that is r
50 otein are limited, the mechanisms regulating clock protein degradation are only beginning to be eluci
52 al role in regulating the expression of core clock proteins driving rhythms in activity and metabolis
53 hythm of KaiC abundance persists; therefore, clock protein expression has a preferred status under a
54 ice and hamsters at peak and trough times of clock protein expression in the suprachiasmatic nucleus
58 ing homology but do not show similarity with clock proteins found so far from either cyanobacteria or
59 ated degradation of the Neurospora circadian clock protein FREQUENCY (FRQ) is critical for clock func
62 Phosphorylation of the Neurospora circadian clock protein FREQUENCY (FRQ) regulates its degradation
63 Phosphorylation of the Neurospora circadian clock protein FREQUENCY by several kinases promotes its
66 necessary for rhythms in accumulation of the clock protein FRQ, indicating that clock control of eEF-
69 yzed sequence identities and similarities of clock protein homologues and immunostained brains of 10
70 bodies; (ii) wild-type virus stabilizes the CLOCK protein; (iii) overexpression of CLOCK partially c
75 e in modulating the stabilities of circadian clock proteins in a manner specific to the time of day.
77 d by the intrinsic properties of the central clock proteins in Arabidopsis, but rather by other genes
81 ation of transcription by the core circadian clock proteins including cryptochrome and by regulation
82 post-translational modification of molecular clock proteins influence the temporal expression of SCN
87 delay between the synthesis and function of clock proteins is due to phosphorylation-regulated nucle
89 such that, although PER2(Edo) complexes with clock proteins, its vulnerability to degradation mediate
91 are generated by the purified cyanobacterial clock proteins, KaiA, KaiB, and KaiC, through rhythmic i
94 ch we ectopically express the cyanobacterial clock protein KaiC in cells from which the clock genes k
96 nct functions for two domains of the central clock protein KaiC: the C-terminal autokinase domain int
100 s effect, posttranslational modifications of clock proteins modulate circadian rhythms and are though
101 nsists of a feedback loop in which canonical clock proteins negatively regulate transcription of thei
103 and epsilon (CK1epsilon) phosphorylate core clock proteins of the mammalian circadian oscillator.
104 s that directly modulate the activity of key clock proteins offer the potential to directly modulate
105 25a is required for temperature-synchronized clock protein oscillations in subsets of central clock n
106 ndependent superimposed oscillations and the clock protein oscillations in the dorsal neuron 1 and 2
107 xpression in LNvs severely dampened Timeless clock protein oscillations, we conclude that the master
108 xpressing immunoreactivity for the circadian clock protein PER is located in the same region as PTTH-
111 es that implicate heme interactions with the clock proteins PER2 and nPAS2 in biological function.
112 neuropeptide arginine vasopressin (AVP) and clock proteins (PER2 and BMAL1), supporting that paterna
113 ed by marked reductions in the levels of the clock protein Period (PER) as well as more modest effect
114 ity, and altered expression of the circadian clock protein period (Per) in a subset of pacemaker neur
115 ation of excitatory receptors influences the clock protein PERIOD 2 (PER2) in a contractile organ, th
120 odulate the stability of closely linked core clock proteins period (PER) and cryptochrome (CRY), resp
121 localized within clock neurons and that the clock proteins Period (Per) and Timeless (Tim) accumulat
123 e, these flies express low levels of the two clock proteins, PERIOD (PER) and TIMELESS (TIM), due to
125 We demonstrate that cryptochrome regulates clock protein phosphorylation by modulating the effect o
128 mong nuclear receptors but common among core clock proteins, protecting the organism from major pertu
130 ing that the lag in the accumulation of some clock proteins relative to their mRNAs does not arise fr
133 regulatory loops in which specific proteins (clock proteins) rhythmically repress expression of their
134 tion of qsm in the clock circuit restores LL clock protein rhythms in qsm-negative neurons, indicatin
135 biquitin-specific proteases can regulate the clock protein stability and circadian pathways remains l
137 In Drosophila melanogaster four circadian clock proteins termed PERIOD (PER), TIMELESS (TIM), dCLO
138 yanobacteria, KaiC is an essential hexameric clock protein that forms the core of a circadian protein
140 tify the first phosphorylation sites on core clock proteins that are acutely regulated by photic cues
141 CYC is by far the most abundant of the four clock proteins that have been examined, PER and TIM appe
142 to be generated by a feedback loop involving clock proteins that inhibit transcription of their own g
143 onally active heterodimer with the circadian CLOCK protein, the structurally related MOP4, and hypoxi
147 RY promotes the degradation of the circadian clock protein TIMELESS (TIM) and then is itself degraded
148 reviously been reported to interact with the clock protein TIMELESS (TIM) in a light-dependent manner
149 l role in light-dependent degradation of the clock protein Timeless (TIM), a key step in the entrainm
150 ecause of light-dependent degradation of the clock protein Timeless (Tim), constant illumination (LL)
155 elegans TIM-1, a paralogue of the Drosophila clock protein TIMELESS, in the regulation of chromosome
158 y promoting light-induced degradation of the clock proteins Timeless and Period, as well as its own p
160 lts define a biochemical action for the core clock protein TOC1 and refine our perspective on how pla
163 ities are rescued by expressing a functional CLOCK protein via viral-mediated gene transfer specifica
166 The clock manifests oscillations of key clock proteins, which are under dynamic control at multi
167 output and decreased expression of the core clock proteins, which regulate many aspects of cellular
168 ity primarily through interaction with other clock proteins, while mPER2 positively regulates rhythmi
169 nd precision of rhythms in PERIOD2 (PER2), a clock protein, within the SCN isolated from embryonic an
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