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Iafa Keydar

Researcher at Tel Aviv University

Publications -  54
Citations -  4106

Iafa Keydar is an academic researcher from Tel Aviv University. The author has contributed to research in topics: Antigen & Breast cancer. The author has an hindex of 31, co-authored 54 publications receiving 4011 citations.

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Establishment and characterization of a cell line of human breast carcinoma origin.

TL;DR: A cell line established from the pleural effusion of a patient with breast carcinoma exhibits epithelial morphology and form monolayers in culture, supported by immunohistologic detection of intracellular casein and the presence of steroid receptors characteristic of mammary tissue.
Journal Article

The CC chemokine RANTES in breast carcinoma progression: regulation of expression and potential mechanisms of promalignant activity.

TL;DR: This study suggests that the expression of RantES by breast tumor cells results not only in monocyte migration to the tumor site but also in protumorigenic activities of RANTES and of proinflammatory cytokines that may facilitate metastasis formation and contribute to disease progression.
Journal Article

Elevated expression of the CC chemokine regulated on activation, normal T cell expressed and secreted (RANTES) in advanced breast carcinoma.

TL;DR: The results indicate that the expression of RantES is directly correlated with a more advanced stage of disease, suggesting that RANTES may be involved in breast cancer progression.
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The met proto-oncogene receptor and lumen formation.

TL;DR: It was shown that Met is expressed in cells bordering lumen-like structures that resemble ducts in the human mammary cell line T47D, and reduced expression of Met could be related to the extent of tumor cell differentiation.
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Human epithelial tumor antigen cDNA sequences. Differential splicing may generate multiple protein forms.

TL;DR: The cDNAs and deduced amino acid sequences, presented here, define the complete amino acids sequences of the epithelial tumor antigen and demonstrate the existence of multiple protein forms that probably localize to different cellular and extracellular compartments.