Nicole Schupp

Dr. Nicole Schupp

Heinrich Heine Universitat, Medical Faculty Institute of Toxicology, Düsseldorf, Germany
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Research Focus & Metrics

Academic Career Length

23Years (2004-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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1 May 2006 in Stem Cells
Verified
Journal Article
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RERegina Ebert
Regina Ebert
MUMatthias Ulmer
Matthias Ulmer
SZSabine Zeck
Sabine Zeck
JMJutta Meissner‐Weigl
Jutta Meissner‐Weigl
DSDoris Schneider
Doris Schneider
FJFranz Jakob
Franz Jakob
STEM CELLS, a peer reviewed journal published monthly, provides a forum for prompt publication of original investigative papers and concise reviews. STEM CELLS is read and written by clinical and basic scientists whose expertise encompasses the rapidly expanding fields of stem and progenitor cell biology. STEM CELLS welcomes original articles and concise reviews describing basic laboratory investigations of stem cells and the translation of their clinical aspects of characterization and manipulation from the bench to patient care. The journal covers all aspects of stem cells embryonic stem cells/induced pluripotent stem cells; tissue-specific stem cells; stem cell technology: epigenetics, genomics, proteomics, and metabonomics; cancer stem cells; translational and clinical research; and regenerative medicine.

10 July 2017 in Basic & Clinical Pharmacology & Toxicology
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Journal Article
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BABadreldin H. Ali
Badreldin H. Ali
SASuhail Al-Salam
Suhail Al-Salam
YSYousuf Al Suleimani
Yousuf Al Suleimani
JKJamila Al Kalbani
Jamila Al Kalbani
SBShadia Al Bahlani
Shadia Al Bahlani
Nicole SchuppNicole Schupp
Nicole Schupp

1 February 2013 in PLOS ONE
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Journal Article
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BABadreldin H Ali
Badreldin H Ali
IAIsehaq Al-Huseini
Isehaq Al-Huseini
SBSumyia Beegam
Sumyia Beegam
AAAhmed Al-Shukaili
Ahmed Al-Shukaili
Abderrahim NemmarAbderrahim Nemmar
Abderrahim Nemmar
Nicole SchuppNicole Schupp
Nicole Schupp
Inflammation and oxidative stress are known to be involved in the pathogenesis of chronic kidney disease in humans, and in chronic renal failure (CRF) in rats. The aim of this work was to study the role of inflammation and oxidative stress in adenine-induced CRF and the effect thereon of the purported nephroprotective agent gum arabic (GA). Rats were divided into four groups and treated for 4 weeks as follows: control, adenine in feed (0.75%, w/w), GA in drinking water (15%, w/v) and adenine+GA, as before. Urine, blood and kidneys were collected from the rats at the end of the treatment for analysis of conventional renal function tests (plasma creatinine and urea concentration). In addition, the concentrations of the pro-inflammatory cytokine TNF-α and the oxidative stress markers glutathione and superoxide dismutase, renal apoptosis, superoxide formation and DNA double strand break frequency, detected by immunohistochemistry for γ-H2AX, were measured. Adenine significantly increased the concentrations of urea and creatinine in plasma, significantly decreased the creatinine clearance and induced significant increases in the concentration of the measured inflammatory mediators. Further, it caused oxidative stress and DNA damage. Treatment with GA significantly ameliorated these actions. The mechanism of the reported salutary effect of GA in adenine-induced CRF is associated with mitigation of the adenine-induced inflammation and generation of free radicals.

1 August 2008 in Atherosclerosis
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Journal Article
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Nicole SchuppNicole Schupp
Nicole Schupp
USUrsula Schmid
Ursula Schmid
AHAugust Heidland
August Heidland
HSHelga Stopper
Helga Stopper

2 April 2008 in Diabetes/Metabolism Research and Reviews
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Journal Article
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USUrsula Schmid
Ursula Schmid
HSHelga Stopper
Helga Stopper
AHAugust Heidland
August Heidland
Nicole SchuppNicole Schupp
Nicole Schupp

15 October 2004 in Plant and Cell Physiology
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Journal Article
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Nicole SchuppNicole Schupp
Nicole Schupp
PZPaul Ziegler
Paul Ziegler
Tissues of wheat (Triticum aestivum L., var. Star) exhibit three starch phosphorylase activity forms resolved by non-denaturing polyacrylamide gel affinity electrophoresis (P1, P2 and P3). Compartmentation analysis of young leaf tissues showed that P3 is plastidic, whereas P1 and P2 are cytosolic. P1 exhibits a strong binding affinity to immobilized glycogen upon electrophoresis, whereas P2 and the chloroplastic P3 do not. Cytosolic leaf phosphorylase was purified to homogeneity by affinity chromatography. The single polypeptide product constituted both the P1 and P2 activity forms. Probes for the detection of phosphorylase transcripts were derived from cDNA sequences of cytosolic and plastidic phosphorylases, and these—together with activity assays and a cytosolic phosphorylase-specific antiserum—were used to monitor phosphorylase expression in leaves and seeds. Mature leaves contained only plastidic phosphorylase, which was also strongly evident in the endosperm of developing seeds at the onset of reserve starch accumulation. Germinating seeds contained only cytosolic phosphorylase, which was restricted to the embryo. Plastidic phosphorylase thus appears to be associated with transitory leaf starch metabolism and with the initiation of seed endosperm reserve starch accumulation, but it plays no role in the degradation of the reserve starch. Cytosolic phosphorylase may be involved in the processing of incoming carbohydrate during rapid tissue growth.