نتایج جستجو برای: zinc finger nuclease

تعداد نتایج: 105645  

Journal: :Current opinion in structural biology 2001
J H Laity B M Lee P E Wright

Zinc finger proteins are among the most abundant proteins in eukaryotic genomes. Their functions are extraordinarily diverse and include DNA recognition, RNA packaging, transcriptional activation, regulation of apoptosis, protein folding and assembly, and lipid binding. Zinc finger structures are as diverse as their functions. Structures have recently been reported for many new zinc finger doma...

2011
Shanping He Kuowei Huang Xu Zhang Xiangchun Yu Ping Huang Chengcai An

BACKGROUND Genetic studies of the Arabidopsis mutant lsd1 highlight the important role of LSD1 in the negative regulation of plant programmed cell death (PCD). Arabidopsis thaliana LSD1 (AtLSD1) contains three LSD1-type zinc finger motifs, which are involved in the protein-protein interaction. METHODOLOGY/PRINCIPAL FINDINGS To further understand the function of LSD1, we have analyzed cellular...

Journal: :Journal of Nanobiotechnology 2005
Markus von Nickisch-Rosenegk Eva Ehrentreich-Forster Rothin Strehlow Alexander Christmann Frank F Bier

Our experiments describe an alternative method of dsDNA recognition using zinc finger (ZF) molecules which bind DNA specifically and with high affinity. Our aim was to develop zinc finger probes which are able to bind to dsDNA molecules at predetermined sites. In our basic approach we used pairs of complementary oligonucleotides to form dsDNAs, containing one of the three SP1-transcription fact...

2000
Dagmar Steffen Dusan Ihracky Lothar Gierl

Zinc finger domains are protein structures first identified in the Xenopus transcription factor TFIIIA. A zinc finger is composed of 20 to 30 amino-acid residues. There are two residues at both extremities of the domain which are involved in the tetrahedral coordination of a zinc atom. It has been proposed that such a domain interacts with the DNA. Many classes of zinc fingers are characterized...

Journal: :The Biochemical journal 2007
Jong Seok Kang

Rapid progress in the ability to develop and utilize zinc-finger proteins with customized sequence specificity have led to their increasing use as tools for modulation of target gene transcription in the post-genomic era. In the present paper, a series of in vitro binding assays and in vivo reporter analyses were used to demonstrate that a zinc-finger protein can effectively specify a base at e...

Journal: :Chembiochem : a European journal of chemical biology 2003
Carla Isernia Enrico Bucci Marilisa Leone Laura Zaccaro Paola Di Lello Giuseppe Digilio Sabrina Esposito Michele Saviano Benedetto Di Blasio Carlo Pedone Paolo V Pedone Roberto Fattorusso

Zinc finger domains of the classical type represent the most abundant DNA binding domains in eukaryotic transcription factors. Plant proteins contain from one to four zinc finger domains, which are characterized by high conservation of the sequence QALGGH, shown to be critical for DNA-binding activity. The Arabidopsis thaliana SUPERMAN protein, which contains a single QALGGH zinc finger, is nec...

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