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Noël Lamandé

Researcher at Collège de France

Publications -  32
Citations -  1723

Noël Lamandé is an academic researcher from Collège de France. The author has contributed to research in topics: Enolase & Angiogenesis. The author has an hindex of 20, co-authored 32 publications receiving 1608 citations. Previous affiliations of Noël Lamandé include PSL Research University & Institut national agronomique Paris Grignon.

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Bone Morphogenetic Protein-9 Is a Circulating Vascular Quiescence Factor

TL;DR: BMP9, circulating under a biologically active form, is a potent antiangiogenic factor that is likely to play a physiological role in the control of adult blood vessel quiescence.
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Angiopoietin-Like 4 Is a Proangiogenic Factor Produced during Ischemia and in Conventional Renal Cell Carcinoma

TL;DR: ANGPTL4, originally identified as a peroxisome proliferator-activated receptor alpha and gamma target gene, has potential for use as a new diagnostic tool and a potential therapeutic target, modulating angiogenesis both in tumors and in ischemic tissues.
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Angiogenic activity of human chorionic gonadotropin through LH receptor activation on endothelial and epithelial cells of the endometrium

TL;DR: It is demonstrated that peritrophoblastic angiostimulation may result from a paracrine dialogue between trophoblast, epithelial, and endothelial cells through hCG and VEGF and that hCG‐mediated angiogenesis involves adenylyl‐cyclase–protein kinase A activation.
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Angiotensinogen and Its Cleaved Derivatives Inhibit Angiogenesis

TL;DR: The data demonstrated that these compounds exerted a clear and equipotent antiangiogenic effect, thus attributing a novel function to angiotens inogen and des(angiotensin I)angiotENSinogen, for which no function was previously known.
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Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins.

TL;DR: It is shown for the first time that pure betabeta-enolase binds with high affinity the adjacent enzymes in the glycolytic pathway (pyruvate kinase and phosphoglycerate mutase), favouring the hypothesis that these three enzymes form a functional glycoleytic segment.