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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
18 simodo mutants elicit rhythmic expression of clock proteins and behavior in LL.
19  have also revealed novel interactions among clock proteins and new partners that couple the clock to
20       Here, we have purified all of the core clock proteins and performed in vitro and in vivo bioche
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
24                           The genes encoding clock proteins are expressed throughout the brain, thoug
25                                    Circadian clock proteins are modified in many different ways.
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
30                                          The clock protein BMAL1 (brain and muscle Arnt-like protein
31 ins to interact with the canonical basic HLH clock proteins BMAL1 and CLOCK.
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,
35                        Arabidopsis circadian clock protein CIRCADIAN CLOCK ASSOCIATED1 (CCA1) binds t
36 log of the Caenorhabditis elegans biological clock protein CLK-2 (HCLK2), associated with and was hyd
37                                  The central clock protein CLOCK has HAT properties.
38 at this may be via interaction with the bHLH clock proteins CLOCK and BMAL1.
39 cillator in which LdpA is a component of the clock protein complex that senses the redox state of a c
40 nobacteria that forms the core of the KaiABC clock protein complex.
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
46      Finally, the results show that the core clock proteins cryptochrome (CRY) 1 and 2 repressed infl
47 of a repressive complex, defined by the core clock proteins cryptochrome 1 (CRY1):CLOCK:BMAL1, plays
48                                The mammalian clock protein, cryptochrome 1 (CRY1), is degraded via th
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
51 ess is known about phosphatases that control clock protein dephosphorylation.
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
55                                     Peak PER clock protein expression is elevated in the mutant, indi
56 the SCN shell and triggers downregulation of clock protein expression.
57 hat suggests a defect in the rising phase of clock protein expression.
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
60                               In Neurospora, clock protein FREQUENCY (FRQ) is progressively phosphory
61                 In Neurospora, the circadian clock protein FREQUENCY (FRQ) is progressively phosphory
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
64 graphic structure of the cyanobacterial KaiB clock protein from Synechocystis sp. PCC6803.
65                                Levels of the clock protein FRQ were measured in Neurospora at various
66 necessary for rhythms in accumulation of the clock protein FRQ, indicating that clock control of eEF-
67               The cycling of the PER and CRY clock proteins has been thought to be necessary to keep
68 s post-translational processes that regulate clock protein homeostasis.
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
71               KaiA is a two-domain circadian clock protein in cyanobacteria, acting as the positive e
72 us PCC 7942 (KaiC) is an essential circadian clock protein in cyanobacteria.
73  encode the N-terminus of the TIMELESS (TIM) clock protein in Drosophila simulans and D. yakuba.
74                             We show that the clock protein in the donor tubules cycled out of phase w
75 e in modulating the stabilities of circadian clock proteins in a manner specific to the time of day.
76  cellular location, and interacts with other clock proteins in a time-dependent manner.
77 d by the intrinsic properties of the central clock proteins in Arabidopsis, but rather by other genes
78                                  Analysis of clock proteins in mCRY-deficient mice shows that the mCR
79 ave examined posttranslational regulation of clock proteins in mouse liver in vivo.
80 LOCK that are useful for assessing circadian clock proteins in the SCN by immunocytochemistry.
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
83         This suggests that expression of the CLOCK protein is not necessary for normal interval timin
84     Progressive phosphorylation of circadian clock proteins is a hallmark of time-keeping.
85              Posttranslational regulation of clock proteins is an essential part of mammalian circadi
86        The posttranslational modification of clock proteins is critical for the function of circadian
87  delay between the synthesis and function of clock proteins is due to phosphorylation-regulated nucle
88                               Versatility of clock proteins is seen in terms of their function in the
89 such that, although PER2(Edo) complexes with clock proteins, its vulnerability to degradation mediate
90                          The other essential clock proteins KaiA and KaiB modulate the status of KaiC
91 are generated by the purified cyanobacterial clock proteins, KaiA, KaiB, and KaiC, through rhythmic i
92 ter kaiABC encodes three essential circadian clock proteins: KaiA, KaiB and KaiC.
93 e the BRET technique to demonstrate that the clock protein KaiB interacts to form homodimers.
94 ch we ectopically express the cyanobacterial clock protein KaiC in cells from which the clock genes k
95 llations in the phosphorylation state of the clock protein KaiC.
96 nct functions for two domains of the central clock protein KaiC: the C-terminal autokinase domain int
97 anisms that control the cycling of circadian clock protein levels are not known.
98 res precisely calibrated degradation of core clock proteins, like PERIOD.
99      The rhythmic expression of RORgamma1 by clock proteins may lead to the rhythmic expression of RO
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
102                                          The clock proteins of Drosophila and mammals exhibit strikin
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-
109 ic cells coexpress ghrelin and the circadian clock proteins PER1 and PER2.
110 in a diurnal manner and are dependent on the clock proteins PER1/2.
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
116                          Oscillations of the clock protein PERIOD are intact in na mutants, indicatin
117                          Oscillations of the clock protein PERIOD are normal in pacemaker neurons lac
118 d by phase-advanced oscillations of the core clock protein PERIOD.
119  system stems from robust degradation of the clock protein PERIOD.
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
122               Antisera against the circadian clock proteins Period (PER) and Timeless (TIM) were used
123 e, these flies express low levels of the two clock proteins, PERIOD (PER) and TIMELESS (TIM), due to
124        Bioluminescent recording of circadian clock protein (PERIOD2) output from ex vivo SCN revealed
125   We demonstrate that cryptochrome regulates clock protein phosphorylation by modulating the effect o
126                    Within the core molecular clock, protein phosphorylation and degradation play a vi
127                           Phosphorylation of clock proteins plays a critical role in generating prope
128 mong nuclear receptors but common among core clock proteins, protecting the organism from major pertu
129 lings, whereas the levels of closely related clock proteins, PRR3 and PRR7, are unchanged.
130 ing that the lag in the accumulation of some clock proteins relative to their mRNAs does not arise fr
131                 Phosphorylation of circadian clock proteins represents a major regulatory step that c
132                           Phosphorylation of clock proteins represents an important mechanism regulat
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
136                                  A series of clock protein structures demonstrate that the PAS (Per/A
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
139                 Cryptochrome (CRY) is a core clock protein that plays an essential role in the repres
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
144  contribution to timekeeping than any of the clock proteins they phosphorylate.
145         In addition, the recently identified clock protein TIM (for timeless) interacted with PER in
146           Like CRY, this pathway targets the clock protein TIM.
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)
151 s mediated by proteasomal degradation of the clock protein TIMELESS (TIM).
152 nvolves the light-induced degradation of the clock protein timeless (TIM).
153 s interactions with targets that include the clock protein Timeless (TIM).
154 clock via light-dependent degradation of the clock protein TIMELESS (TIM).
155 elegans TIM-1, a paralogue of the Drosophila clock protein TIMELESS, in the regulation of chromosome
156 ing of nuclear accumulation of the circadian clock protein TIMELESS.
157 , as well as altered cycling kinetics of the clock proteins timeless (TIM) and period (PER).
158 y promoting light-induced degradation of the clock proteins Timeless and Period, as well as its own p
159 roteasome-dependent degradation of a central clock protein, TIMING OF CAB EXPRESSION 1 (TOC1).
160 lts define a biochemical action for the core clock protein TOC1 and refine our perspective on how pla
161  PIL1, previously shown to interact with the clock protein TOC1.
162 ) that plays an important role in regulating clock protein turnover.
163 ities are rescued by expressing a functional CLOCK protein via viral-mediated gene transfer specifica
164                         Here, the Drosophila CLOCK protein was shown to induce transcription of the c
165                         Clock gene mRNAs and clock proteins were found differentially expressed in th
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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