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Covalent Inhibitors of S100A4 Block the Formation of a Pro-Metastasis Non-Muscle Myosin 2A Complex.
J Med Chem
November 2024
Centre for Medicines Discovery, Nuffield Department of Medicine, NDM Research building, Old Road Campus, Oxford OX3 7FZ, U.K.
The S100 protein family functions as protein-protein interaction adaptors regulated by Ca binding. Formation of various S100 complexes plays a central role in cell functions, from calcium homeostasis to cell signaling, and is implicated in cell growth, migration, and tumorigenesis. We established a suite of biochemical and cellular assays for small molecule screening based on known S100 protein-protein interactions.
View Article and Find Full Text PDFThe Effect of Retinoic Acid on Arsenite-Transformed Malignant UROtsa Bladder Cancer Cells: In Vitro Model of Basal Muscle-Invasive Bladder Cancer.
Cancers (Basel)
March 2024
Department of Pathology, School of Medicine and Health Sciences, University of North Dakota, Grand Forks, ND 58202, USA.
Article Synopsis
- - Bladder cancer (BC) is the eighth leading cause of cancer-related deaths in the U.S., with two main types: non-muscle-invasive (NMIBC) and muscle-invasive bladder cancer (MIBC), which can be further classified into aggressive basal and less aggressive luminal subtypes.
- - This study investigates the effects of all-trans retinoic acid (tretinoin) on arsenite-transformed malignant urothelial cells to see if it can impact muscle-invasive bladder cancer characteristics.
- - Results showed that tretinoin reduced cell proliferation and encouraged luminal differentiation while lowering basal marker expression, suggesting that targeting the retinoic acid pathway could reduce the aggressiveness of basal MIBC and improve patient survival chances
Barriers to single-dose intravesical chemotherapy in non-muscle invasive bladder cancer: what's the problem?
Urol Pract
March 2021
Regenstreif Institute, Inc, Veterans Health Administration, Center for Health Information and Communication, U.S.
Introduction: The intravesical instillation of mitomycin C immediately following surgery for non-muscle invasive bladder cancer has been shown to be efficacious in reducing cancer recurrence. As a result, the American Urological Association adopted guidelines for non-muscle invasive bladder cancer care to support its use in low to intermediate risk patients. Despite this, urologists' use of this drug following transurethral resection of a bladder tumor (TURBT) has been reported as low as 5% or less.
View Article and Find Full Text PDFLinking Biochemical and Structural States of SERCA: Achievements, Challenges, and New Opportunities.
Int J Mol Sci
June 2020
Center for Arrhythmia Research, Department of Internal Medicine, Division of Cardiovascular Medicine, University of Michigan, Ann Arbor, MI 48109, USA.
Sarcoendoplasmic reticulum calcium ATPase (SERCA), a member of the P-type ATPase family of ion and lipid pumps, is responsible for the active transport of Ca from the cytoplasm into the sarcoplasmic reticulum lumen of muscle cells, into the endoplasmic reticulum (ER) of non-muscle cells. X-ray crystallography has proven to be an invaluable tool in understanding the structural changes of SERCA, and more than 70 SERCA crystal structures representing major biochemical states (defined by bound ligand) have been deposited in the Protein Data Bank. Consequently, SERCA is one of the best characterized components of the calcium transport machinery in the cell.
View Article and Find Full Text PDFThe structure of the actin-smooth muscle myosin motor domain complex in the rigor state.
J Struct Biol
December 2017
Institute of Molecular Biophysics, Kasha Laboratory, Florida State University, Tallahassee, FL 32306-4380, United States. Electronic address:
Myosin-based motility utilizes catalysis of ATP to drive the relative sliding of F-actin and myosin. The earliest detailed model based on cryo-electron microscopy (cryoEM) and X-ray crystallography postulated that higher actin affinity and lever arm movement were coupled to closure of a feature of the myosin head dubbed the actin-binding cleft. Several studies since then using crystallography of myosin-V and cryoEM structures of F-actin bound myosin-I, -II and -V have provided details of this model.
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