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Zinc fingers were first identified in a study of transcription in the African clawed frog, Xenopus laevis in the laboratory of Aaron Klug.A study of the transcription of a particular RNA sequence revealed that the binding strength of a small transcription factor (transcription factor IIIA; TFIIIA) was due to the presence of zinc-coordinating finger-like structures. [6]
Zinc fingers and homeoboxes protein 1 is a protein that in humans is encoded by the ZHX1 gene. [5] [6]The members of the zinc fingers and homeoboxes gene family are nuclear homodimeric transcriptional repressors that interact with the A subunit of nuclear factor-Y (NF-YA) and contain two C2H2-type zinc fingers and five homeobox DNA-binding domains.
Vaccines are recommended for most people starting before their 15th birthday in two doses, but children can get it starting at age 9. Research suggests a first dose around 9 years old provides ...
In molecular biology, GATA zinc fingers are zinc-containing domains found in a number of transcription factors (including erythroid-specific transcription factor and nitrogen regulatory proteins). Some members of this class of zinc fingers specifically bind the DNA sequence (A/T)GATA(A/G) in the regulatory regions of genes ., [ 1 ] giving rise ...
The Ikaros Zinc Finger (IkZF) family of transcription factors are known regulators of hematopoietic cell development and many immune cells including that of CD4 + T cells. The IkZF family consists of five members: Ikaros (encoded by the gene Ikzf1), Helios , Aiolos , Eos , and Pegasus . These factors contain N-terminal zinc finger (ZF) domains ...
Vaccines are not injected intravenously into the bloodstream. Most injections deposit a small dose into a muscle, but some are given superficially just under the skin surface or deeper beneath the skin. [1] Fluenz Tetra, a live flu vaccine for children, is administered nasally with 0.1ml of liquid sprayed into each nostril.
In molecular biology the ZZ-type zinc finger domain is a type of protein domain that was named because of its ability to bind two zinc ions. [1] These domains contain 4-6 Cys residues that participate in zinc binding (plus additional Ser/His residues), including a Cys-X2-Cys motif found in other zinc finger domains.
In molecular biology the B-box-type zinc finger domain is a short protein domain of around 40 amino acid residues in length. B-box zinc fingers can be divided into two groups, where types 1 and 2 B-box domains differ in their consensus sequence and in the spacing of the 7-8 zinc-binding residues.