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Rajeev S. Samant

Researcher at University of Alabama at Birmingham

Publications -  109
Citations -  5459

Rajeev S. Samant is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Metastasis & Cancer. The author has an hindex of 43, co-authored 99 publications receiving 4865 citations. Previous affiliations of Rajeev S. Samant include University of Alabama & Veterans Health Administration.

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The gene expression profiles of primary and metastatic melanoma yields a transition point of tumor progression and metastasis

TL;DR: The gene expression profiling of primary, non-metastatic cutaneous tumors and metastatic melanoma has resulted in the identification of several genes that may be centrally involved in the progression and metastasis potential of melanoma.
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Multi-targeted therapy of cancer by niclosamide: A new application for an old drug.

TL;DR: The inhibitory effects of niclosamide on cancer stem cells provide further evidence for its consideration as a promising drug for cancer therapy.
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Functional evidence for a novel human breast carcinoma metastasis suppressor, BRMS1, encoded at chromosome 11q13.

TL;DR: The isolation and functional characterization of a full-length cDNA for one of the novel genes, designated breast-cancer metastasis suppressor 1 (BRMS1), which maps to human chromosome 11q13.1-q 13.2 provides compelling functional evidence that breast- cancer metastasis suppression 1 is a novel mediator of metastasis suppressed in human breast carcinoma.
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Role of osteopontin in the pathophysiology of cancer.

TL;DR: A broad perspective is provided on the importance of OPN in the pathophysiology of cancer to be a crucial mediator of cellular cross talk and an influential factor in the tumor microenvironment.
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Breast cancer metastasis suppressor 1 (BRMS1) forms complexes with retinoblastoma-binding protein 1 (RBP1) and the mSin3 histone deacetylase complex and represses transcription.

TL;DR: Deletion analyses show that the carboxyl-terminal 42 amino acids of BRMS1 are not critical for interaction with much of the mSin3 complex and that BR MS1 appears to have more than one binding point to the complex, and suggest a novel mechanism by whichBRMS1 might suppress cancer metastasis.