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Tayebeh Pourmotabbed

Researcher at University of Tennessee Health Science Center

Publications -  82
Citations -  2510

Tayebeh Pourmotabbed is an academic researcher from University of Tennessee Health Science Center. The author has contributed to research in topics: Population & Neopterin. The author has an hindex of 27, co-authored 82 publications receiving 2268 citations. Previous affiliations of Tayebeh Pourmotabbed include University of Tennessee & Kermanshah University of Medical Sciences.

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Human neutrophil collagenase : a distinct gene product with homology to other matrix metalloproteinases

TL;DR: In this article, a cDNA encoding human neutrophil collagenase from a lambda gt11 cDNA library constructed from mRNA extracted from the peripheral leukocytes of a patient with chronic granulocytic leukemia was identified and sequenced.
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Structure-function relationship of human neutrophil collagenase: identification of regions responsible for substrate specificity and general proteinase activity.

TL;DR: The data suggest that substrate specificity for interstitial collagen is determined by a 16-aa sequence in the COOH-terminal domain of neutrophil collagenase and is influenced by the integrity of a disulfide-defined loop at theCOOH terminus for maximal activity.
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Correlation of N-cadherin expression in high grade gliomas with tissue invasion

TL;DR: In this article, the effects of N-cadherin expression on invasion and metastasis in vitro and in vivo, were studied in a rat C6 glioma cell line.

Correlation of N-cadherin expression in high grade gliomas with tissue invasion - Springer

TL;DR: N-cadherin levels are important in the malignant behavior of gliomas, and may serve as a prognostic indicator for patients with high-gradegliomas.
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Optimization of efficiency in the glyoxalase pathway.

TL;DR: The model exhibits the following properties under conditions where substrate concentrations are small in comparison to the Km values for the glyoxalase enzymes: the overall rate of conversion of methylglyoxal to D-lactate is primarily limited by the rate of formation of the diastereotopic thiohemiacetals.