Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
Articles by J Qin
Total Records ( 7 ) for J Qin
  G Tang , J Qin and G. G Dolnikowski

Background: Genetically engineered "Golden Rice" contains up to 35 µg β-carotene per gram of rice. It is important to determine the vitamin A equivalency of Golden Rice β-carotene to project the potential effect of this biofortified grain in rice-consuming populations that commonly exhibit low vitamin A status.

Objective: The objective was to determine the vitamin A value of intrinsically labeled dietary Golden Rice in humans.

Design: Golden Rice plants were grown hydroponically with heavy water (deuterium oxide) to generate deuterium-labeled [2H]β-carotene in the rice grains. Golden Rice servings of 65–98 g (130–200 g cooked rice) containing 0.99–1.53 mg β-carotene were fed to 5 healthy adult volunteers (3 women and 2 men) with 10 g butter. A reference dose of [13C10]retinyl acetate (0.4–1.0 mg) in oil was given to each volunteer 1 wk before ingestion of the Golden Rice dose. Blood samples were collected over 36 d.

Results: Our results showed that the mean (±SD) area under the curve for the total serum response to [2H]retinol was 39.9 ± 20.7 µg·d after the Golden Rice dose. Compared with that of the [13C10]retinyl acetate reference dose (84.7 ± 34.6 µg·d), Golden Rice β-carotene provided 0.24–0.94 mg retinol. Thus, the conversion factor of Golden Rice β-carotene to retinol is 3.8 ± 1.7 to 1 with a range of 1.9–6.4 to 1 by weight, or 2.0 ± 0.9 to 1 with a range of 1.0–3.4 to 1 by moles.

Conclusion: β-Carotene derived from Golden Rice is effectively converted to vitamin A in humans. This trial was registered at as NCT00680355.

  S Bangalore , J Qin , S Sloan , S. A Murphy , C. P Cannon and for the PROVE IT TIMI 22 Trial Investigators

Aggressive blood pressure (BP) control has been advocated in patients with acute coronary syndrome, but few data exist in this population relative to cardiovascular outcomes.

Methods and Results—

We evaluated 4162 patients enrolled in the PRavastatin Or atorVastatin Evaluation and Infection Therapy–Thrombolysis In Myocardial Infarction (PROVE IT-TIMI) 22 trial (acute coronary syndrome patients randomized to pravastatin 40 mg versus atorvastatin 80 mg). The average follow-up BP (systolic and diastolic) was categorized into 10-mm Hg increments. The primary outcome was a composite of death due to any cause, myocardial infarction, unstable angina requiring rehospitalization, revascularization after 30 days, and stroke. The secondary outcome was a composite of death due to coronary heart disease, nonfatal myocardial infarction, or revascularization. The relationship between BP (systolic or diastolic) followed a J- or U-shaped curve association with primary, secondary, and individual outcomes, with increased events rates at both low and high BP values, both unadjusted and after adjustment for baseline variables, baseline C-reactive protein, and on-treatment average levels of low-density lipoprotein cholesterol. A nonlinear Cox proportional hazards model showed a nadir of 136/85 mm Hg (range 130 to 140 mm Hg systolic and 80 to 90 mm Hg diastolic) at which the incidence of primary outcome was lowest. The curve was relatively flat for systolic pressures of 110 to 130 mm Hg and diastolic pressures of 70 to 90 mm Hg.


After acute coronary syndrome, a J- or U-shaped curve association existed between BP and the risk of future cardiovascular events, with lowest event rates in the BP range of approximately 130 to 140 mm Hg systolic and 80 to 90 mm Hg diastolic and a relatively flat curve for systolic pressures of 110 to 130 mm Hg and diastolic pressures of 70 to 90 mm Hg, which suggests that too low of a pressure (especially <110/70 mm Hg) may be dangerous.

Clinical Trial Registration—

URL: Unique identifier: NCT00382460.

  M Ito , K Miyado , K Nakagawa , M Muraki , M Imai , N Yamakawa , J Qin , Y Hosoi , H Saito and Y. Takahashi

p38 MAPK (p38) plays pivotal roles in aging and reproductive physiology. Nevertheless, involvement of p38 in female reproductive aging is uncertain. To improve knowledge of the role of p38 in age-associated reproductive failure, the expression and subcellular localization of phosphorylated p38 was investigated in human granulosa cells. p38 was 7-fold more activated in cells from older subjects than in those from younger subjects. Similar results were obtained in human granulosa-like KGN cells treated with hydrogen peroxide (H2O2). Interestingly, phosphorylated p38 was detected in the nucleus less frequently in older cells than in younger cells (Younger: 58.6%; Older: 29.8%, P< 0.01). Similarly cytoplasmic localization of phosphorylated p38 in KGN cells was observed after treatment with H2O2. The activation and cytoplasmic localization of p38 in H2O2-treated KGN cells were blocked by N-acetylcysteine and SB203580. Although the p38 activators, FSH and tumor necrosis factor-, induced a similar localization of phosphorylated p38 in KGN cells, the expression and localization patterns of p38 were distinct from those in older granulosa cells and H2O2-treated KGN cells. These results indicate that the characteristic localization of p38 in older granulosa cells is induced by oxidative stress.

  N. J McKenna , A. J Cooney , F. J DeMayo , M Downes , C. K Glass , R. B Lanz , M. A Lazar , D. J Mangelsdorf , D. D Moore , J Qin , D. L Steffen , M. J Tsai , S. Y Tsai , R Yu , R. N Margolis , R. M Evans and B. W. O`Malley

Nuclear receptors and coregulators are multifaceted players in normal metabolic and homeostatic processes in addition to a variety of disease states including cancer, inflammation, diabetes, obesity, and atherosclerosis. Over the past 7 yr, the Nuclear Receptor Signaling Atlas (NURSA) research consortium has worked toward establishing a discovery-driven platform designed to address key questions concerning the expression, organization, and function of these molecules in a variety of experimental model systems. By applying powerful technologies such as quantitative PCR, high-throughput mass spectrometry, and embryonic stem cell manipulation, we are pursuing these questions in a series of transcriptomics-, proteomics-, and metabolomics-based research projects and resources. The consortium’s web site ( integrates NURSA datasets and existing public datasets with the ultimate goal of furnishing the bench scientist with a comprehensive framework for hypothesis generation, modeling, and testing. We place a strong emphasis on community input into the development of this resource and to this end have published datasets from academic and industrial laboratories, established strategic alliances with Endocrine Society journals, and are developing tools to allow web site users to act as data curators. With the ongoing support of the nuclear receptor and coregulator signaling communities, we believe that NURSA can make a lasting contribution to research in this dynamic field.

  R. B Lanz , Y Bulynko , A Malovannaya , P Labhart , L Wang , W Li , J Qin , M Harper and B. W. O'Malley

The nuclear receptor and bona fide oncogene, steroid receptor coactivator-3 (SRC-3, AIB1), acts as a master transcriptional regulator of breast cancer by transducing growth signals via the estrogen receptor (ER). In this resource paper, we present the genome-wide localization analysis of SRC-3 chromatin affinity sites in MCF-7 human breast cancer chromatin and compare the cis binding sites to global cartographies for ER and FoxA1. By correlating their gene proximal binding sites to integrated gene expression signatures, and in combination with gene ontology analyses, we provide a functional classification of estradiol-induced gene regulation that further highlights an intricate transcriptional control of interdependent cellular pathways by SRC-3. Furthermore, by presenting proteomics analyses of in vivo SRC-3- and ER-associated proteins, we give strong evidence to support the idea that the interpretative power of SRC-3 in estrogen signaling is mediated through the formation of distinct, cell state-dependent protein complexes. Altogether, we present the first approach in complementary comparative analyses that converges results obtained by three discovery-driven methods (cistromics, transcriptomics, and proteomics) into testable hypotheses, thus providing a valuable resource for follow-up studies that further our understanding of estrogen signaling in human diseases in general and breast cancer in particular.

  V Stanisic , A Malovannaya , J Qin , D. M Lonard and B. W. O`Malley

Estrogen receptor (ER) is an essential component in human physiology and is a key factor involved in the development of breast and endometrial cancers. ER protein levels and transcriptional activity are tightly controlled by the ubiquitin proteasome system. Deubiquitinating enzymes, a class of proteases capable of removing ubiquitin from proteins, are increasingly being seen as key modulators of the ubiquitin proteasome system, regulating protein stability and other functions by countering the actions of ubiquitin ligases. Using mass spectrometry analysis of an ER protein complex, we identified OTU domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) as a novel ER-interacting protein capable of deubiquitinating ER in cells and in vitro. We show that OTUB1 negatively regulates transcription mediated by ER in transient reporter gene assays and transcription mediated by endogenous ER in Ishikawa endometrial cancer cells. We also show that OTUB1 regulates the availability and functional activity of ER in Ishikawa cells by affecting the transcription of the ER gene and by stabilizing the ER protein in the chromatin.

  Y Liu , M Porta , J Qin , J Ramos , A Nani , T. R Shannon and M. Fill

The cardiac type 2 ryanodine receptor (RYR2) is activated by Ca2+-induced Ca2+ release (CICR). The inherent positive feedback of CICR is well controlled in cells, but the nature of this control is debated. Here, we explore how the Ca2+ flux (lumen-to-cytosol) carried by an open RYR2 channel influences its own cytosolic Ca2+ regulatory sites as well as those on a neighboring channel. Both flux-dependent activation and inhibition of single channels were detected when there were super-physiological Ca2+ fluxes (>3 pA). Single-channel results indicate a pore inhibition site distance of 1.2 ± 0.16 nm and that the activation site on an open channel is shielded/protected from its own flux. Our results indicate that the Ca2+ flux mediated by an open RYR2 channel in cells (~0.5 pA) is too small to substantially regulate (activate or inhibit) the channel carrying it, even though it is sufficient to activate a neighboring RYR2 channel.

Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility