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Grzegorz Młynarczyk

Researcher at Medical University of Białystok

Publications -  10
Citations -  34

Grzegorz Młynarczyk is an academic researcher from Medical University of Białystok. The author has contributed to research in topics: Cancer & Medicine. The author has an hindex of 1, co-authored 5 publications receiving 7 citations.

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Journal ArticleDOI

Dominative role of MMP-14 over MMP-15 in human urinary bladder carcinoma on the basis of its enhanced specific activity.

TL;DR: Comparison of investigated enzymes’ activity and the inhibitor content suggests it opposite effects, higher suppression of MMP-14 than M MP-15 activity in low-grade bladder cancer and reverse TIMP-1 action in high-grade cancer.
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Comparative Assessment of the WNT/β-Catenin Pathway, CacyBP/SIP, and the Immunoproteasome Subunit LMP7 in Various Histological Types of Renal Cell Carcinoma.

TL;DR: Study results suggest an important role of WNT/β-catenin pathway, CacyBP/SIP and LMP7 in RCC carcinogenesis, and may indicate new aspects of pathomechanisms leading to differences in the biology of clear cell, papillary and chromophobe RCC.
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Grade‐dependent changes in sphingolipid metabolism in clear cell renal cell carcinoma

TL;DR: It is concluded that ccRCC is characterized by profound and multilevel alterations in sphingolipid metabolism, which to a large extent are grade‐dependent.
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Enhanced Expression but Decreased Specific Activity of Matrix Metalloproteinase 10 (MMP-10) in Comparison with Matrix Metalloproteinase 3 (MMP-3) in Human Urinary Bladder Carcinoma.

TL;DR: In this article, the expression and activity of matrix metalloproteinases (MMPs) in human urinary bladder cancer occurring at various stages of the disease were analyzed. And the results demonstrated that contrary participation of MMPs in ECM remodeling what may be crucial in the pathogenesis of human ureteral cancer.
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Suppressed Expression but Not Activity of Collagenases MMP-1 and MMP-13 in Human Renal Carcinoma.

TL;DR: The lower content and higher activity of the collagenases investigated in cancer tissue indicate that most of these enzymes are in active form in renal carcinoma, which can be explained at least in part by increased collagenase activity.