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Volumn 8, Issue 5, 1998, Pages 635-641

PASting together the mammalian clock

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; VISUAL PIGMENT;

EID: 0032192001     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(98)80092-5     Document Type: Article
Times cited : (25)

References (45)
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    • of outstanding interest. This paper, together with one by Rutila et al. [17], demonstrates the power of the genetic approach for determining how the various clock components may fit together. The authors cloned the Drosophila homolog of Clock (dClock) as the result of a mutation that truncates the Clock activation domain and leads to arrhythmicity and reduced levels of per and tim expression.
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    • of outstanding interest. The perfect timing of the appearance of this paper and that of Allada et al. [13] reinforced the importance of the role of CLOCK:BMAL1 as partners in the clock mechanism. Cycle, the Drosophila homolog of bmal1, was identified in a genetic screen. Flies homozygous for a mutation in cycle are arrhythmic and have significantly reduced expression of per and tim.
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    • of outstanding interest. In this paper, the authors used Drosophila genetics to identify a new clock component, double-time. double-time mutants show accumulation of high levels of underphosphorylated period protein. The authors propose the double-time product phosphorylates period and thereby destabilizes it, contributing to the characteristic natural delay in period accumulation.
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    • of outstanding interest. The authors demonstrate that double-time is in fact a homolog of mammalian casein kinase 1ε. They confirm that period and double time interact physically.
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    • of outstanding interest. This pioneering work exploited the development of period promoter-luciferase reporter transgenics to analyse period expression in living Drosophila. In this way, the authors demonstrated rhythmic expression in many tissues that persisted in vitro and, most importantly, was also entrainable by light.
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    • Vitamin B2-based blue-light photoreceptors in the retinohypothalamic tract as the photoactive pigments for setting the circadian clock in mammals
    • 2-based blue-light photoreceptor proteins (cryptochromes) as light input molecules for the clock. Cryptochrome expression in the SCN (which oscillates), as well as in the ganglion cell and inner nuclear layers of the mouse retina, suggests that they may play a role in photoreception in these pacemaker structures.
    • 2-based blue-light photoreceptor proteins (cryptochromes) as light input molecules for the clock. Cryptochrome expression in the SCN (which oscillates), as well as in the ganglion cell and inner nuclear layers of the mouse retina, suggests that they may play a role in photoreception in these pacemaker structures.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6097-6102
    • Miyamoto, Y.1    Sancar, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.