Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0155339 (Brown)
 12,436 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The insulin-regulatable glucose transporter (GLUT-4) is expressed in adipose tissue and in cardiac and skeletal muscle (D. E. James, R. Brown, J. Navarro, and P. F. Pilch. Nature Lond. 333: 183-185, 1988). We examined GLUT-4 development between postnatal days 1 and 41 (P1-P41) in male and female rats in these tissues by quantitative immunoblotting. GLUT-4 was detectable in each tissue at comparable levels at P1. However, the subsequent patterns of GLUT-4 development were distinctive. GLUT-4 increased in the diaphragm after P7, peaked at P20, and then declined. GLUT-4 expression in the heart increased rapidly after P7 to plateau on P41 at levels four times greater than the diaphragm. In sharp contrast, adipose tissue expression was highest between P3 and P5 but declined to a nadir at P20 before rebounding at P34. These patterns were observed for both sexes within each tissue, but female GLUT-4 expression was higher in diaphragm and heart and lower in adipose tissue. The expression of GLUT-4 appears to be regulated in a tissue-specific manner by a developmental program that may coordinate the expression of other proteins of metabolic importance.
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PMID:Developmental expression of insulin-regulatable glucose transporter GLUT-4. 163 86

The crystal structure of human cyclin H has been solved at 2.6 A resolution by the MIR method and refined to an R-factor of 23.1%. The core of the molecule consists of two helical repeats adopting the canonical cyclin fold already observed in the structures of cyclin A [Brown et al. (1995) Structure 3, 1235-1247; Jeffrey et al. (1995) Nature 376, 313-320; Russo et al. (1996) Nature 382, 325-331] and TFIIB [Nikoilov et al. (1995) Nature 377, 119-128]. The N-terminal and C-terminal residues form a new domain built on two long helices interacting essentially with the first repeat of the molecule.
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PMID:The crystal structure of human cyclin H. 894 15