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Michael Z. Gilman

Researcher at Cold Spring Harbor Laboratory

Publications -  68
Citations -  10745

Michael Z. Gilman is an academic researcher from Cold Spring Harbor Laboratory. The author has contributed to research in topics: Transcription factor & Transcription (biology). The author has an hindex of 43, co-authored 68 publications receiving 10510 citations. Previous affiliations of Michael Z. Gilman include ARIAD Pharmaceuticals, Inc. & Howard Hughes Medical Institute.

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Cloning the soil metagenome: a strategy for accessing the genetic and functional diversity of uncultured microorganisms.

TL;DR: Phylogenetic analysis of 16S rRNA gene sequences recovered from one of the libraries indicates that the BAC libraries contain DNA from a wide diversity of microbial phyla, including sequences from diverse taxa such as the low-G+C, gram-positive Acidobacterium,Cytophagales, and Proteobacteria.
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A common nuclear signal transduction pathway activated by growth factor and cytokine receptors.

TL;DR: Two unrelated receptors may activate a common nuclear signal transduction pathway that, through differential use of latent cytoplasmic proteins, permits these receptors to regulate both common and unique sets of genes.
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A humanized system for pharmacologic control of gene expression

TL;DR: The properties of a suitable system for pharmacologic control of therapeutic gene expression are reported and its use to control circulating levels of human growth hormone in mice implanted with engineered human cells is demonstrated.
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Redesigning an FKBP–ligand interface to generate chemical dimerizers with novel specificity

TL;DR: Ligands that bind specifically to a mutated FKBP over the wild-type protein are designed by remodeling an FK BP-ligand interface to introduce a specificity binding pocket and showed that recognition is surprisingly relaxed, with the modified ligand only partially filling the engineered cavity.
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Polypeptide signalling to the nucleus through tyrosine phosphorylation of Jak and Stat proteins

TL;DR: The tyrosine phosphorylation events on Stat and Jak proteins after treatment of cells with IFNs α and γ and with epidermal growth factor (EGF) are investigated and Jakl is found to be the enzyme that phosphorylates Tyr701inStat91.