Articolele autorului Vlad Cojocaru
Link la profilul stiintific al lui Vlad Cojocaru

Reprogramming to pluripotency is an ancient trait of vertebrate Oct4 and Pou2 proteins.

The evolutionary origins of the gene network underlying cellular pluripotency, a central theme in developmental biology, have yet to be elucidated. In mammals, Oct4 is a factor crucial in the reprogramming of differentiated cells into induced pluripotent stem cells. The Oct4 and Pou2 genes evolved from a POU class V gene ancestor, but it is unknown whether pluripotency induced by Oct4 gene activity is a feature specific to mammals or was already

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Interviu cu Vlad Cojocaru pe portalul de stiri „ziare.com”

http://www.ziare.com/victor-ponta/plagiat/plagiatul-la-nivel-inalt-cazul-ponta-vs-cazul-guttenberg-interviu-ziare-com-1175149

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Comunicat Ad Astra privind infiintarea „Global Research Council”

Catre Ministerul Educatiei, Cercetarii, Tineretului si Sportului, Asociatia Ad Astra constatavcu regret ca in timp ce la Bucuresti se numeau si eliberau din functie ministrii pentru educatie si cercetare cu probleme grave in curriculum vitae si se schimba conducerea Autoritatii Nationale pentru Cercetarea Stiintifica pe cu totul alte considerente decat cercetarea stiintifica, la Washington DC in SUA, pe 16 mai 2012 s-au pus bazele “Global Research

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Liviu Giosan, co-fondator Ad Astra: Studiu asupra civilizatiei Indusului (PNAS)

Fall of Indus civilization tied to vagaries of monsoons A study suggests that monsoon-related riverine dynamics might have played a role in the collapse of the Indus civilization, one of the earliest urban civilizations that thrived during the Bronze Age. Urban settlements in the Indus or Harappan civilization flourished in the western parts of the Indo-Gangetic Plain—an area spanning parts of India, Pakistan, Nepal and Bangladesh—for nearly 600

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Comunicat Ad Astra privind posibila secretizare a deciziilor de acordare a titlurilor universitare

Comunicatul AdAstra se poate descarca aici: http://docs.ad-astra.ro/Comunicat_AdAstra_Titluri_Universitare_29072011.pdf

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Structure and dynamics of the membrane-bound cytochrome P450 2C9

The microsomal, membrane-bound, human cytochrome P450 (CYP) 2C9 is a liver-specific monooxygenase essential for drug metabolism. CYPs require electron transfer from the membrane-bound CYP reductase (CPR) for catalysis. The structural details and functional relevance of the CYP-membrane interaction are not understood. From multiple coarse grained molecular simulations started with arbitrary configurations of protein-membrane complexes, we found two

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Multiple, ligand-dependent routes from the active site of cytochrome P450 2C9

The active site of liver-specific, drug-metabolizing cytochrome P450 (CYP) monooxygenases is deeply buried in the protein and is connected to the protein surface through multiple tunnels, many of which were found open in different CYP crystal structures. It has been shown that different tunnels could serve as ligand passage routes in different CYPs. However, it is not understood whether one CYP uses multiple routes for substrate access and product

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Control of Dead end localization and activity–implications for the function of the protein in antagonizing miRNA function.

Dead end (dnd) is a vertebrate-specific component of the germ plasm and germ-cell granules that is crucial for germ-cell development in zebrafish and mouse. Dnd counteracts the inhibitory function of miRNAs, thereby facilitating the expression of proteins such as Nanos and Tdrd7 in the germ cells. Here, we show that cis-acting elements within dnd mRNA and the RNA recognition motive (RRM) of the protein are essential for targeting protein expression

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Pozitie de doctorand la Insitutul Max Planck din Muenster, Germania

http://www.mpi-muenster.mpg.de/career/openings/08-2011_phD_Cojocaru.pdf

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The Ins and Outs of Cytochrome P450s

The active site of cytochromes P450 is situated deep inside the protein next to the heme cofactor. Consequently, enzyme specificity and kinetics can be influenced by how substrates pass through the protein to access the active site and how products egress from the active site. We previously analysed the channels between the active site and the protein surface in P450 crystal structures available in October 2003 [R.C. Wade, P.J. Winn, I. Schlichting,

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