DNA Recognition by Cys2His2 Zinc Finger Proteins
SA Wolfe, L Nekludova, CO Pabo - Annual review of biophysics …, 2000 - annualreviews.org
▪ Abstract Cys2His2 zinc fingers are one of the most common DNA-binding motifs found in
eukaryotic transcription factors. These proteins typically contain several fingers that make …
eukaryotic transcription factors. These proteins typically contain several fingers that make …
[HTML][HTML] Metal binding properties, stability and reactivity of zinc fingers
K Kluska, J Adamczyk, A Krężel - Coordination Chemistry Reviews, 2018 - Elsevier
Zinc fingers (ZFs) are among the most structurally diverse protein domains. They interact
with nucleic acids, other proteins and lipids to facilitate a multitude of biological processes …
with nucleic acids, other proteins and lipids to facilitate a multitude of biological processes …
Directed evolution of novel binding proteins
RC Ladner, SK Guterman, BL Roberts… - US Patent …, 1993 - Google Patents
In order to obtain a novel binding protein against a chosen target, DNA molecules, each
encoding a protein comprising one of a family of similar potential binding domains and a …
encoding a protein comprising one of a family of similar potential binding domains and a …
Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å
NP Pavletich, CO Pabo - Science, 1991 - science.org
The zinc finger DNA-binding motif occurs in many proteins that regulate eukaryotic gene
expression. The crystal structure of a complex containing the three zinc fingers from Zif268 …
expression. The crystal structure of a complex containing the three zinc fingers from Zif268 …
The galvanization of biology: a growing appreciation for the roles of zinc
Zinc ions are key structural components of a large number of proteins. The binding of zinc
stabilizes the folded conformations of domains so that they may facilitate interactions …
stabilizes the folded conformations of domains so that they may facilitate interactions …
Intrinsic disorder and protein function
The dominant view of protein structure-function is that an amino acid sequence specifies a
three-dimensional (3-D) structure that is a prerequisite for protein function. In contrast, many …
three-dimensional (3-D) structure that is a prerequisite for protein function. In contrast, many …
Viruses expressing chimeric binding proteins
RC Ladner, SK Guterman, BL Roberts… - US Patent …, 1995 - Google Patents
First worldwide family litigation filed litigation Critical https://patents. darts-ip. com/? family=
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Cotranslational protein folding inside the ribosome exit tunnel
OB Nilsson, R Hedman, J Marino, S Wickles, L Bischoff… - Cell reports, 2015 - cell.com
At what point during translation do proteins fold? It is well established that proteins can fold
cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit …
cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit …
Directed evolution of novel binding proteins
RC Ladner, SK Guterman, BL Roberts… - US Patent …, 1996 - Google Patents
In order to obtain a novel binding protein against a chosen target, DNA molecules, each
encoding a protein comprising one of a family of similar potential binding domains and a …
encoding a protein comprising one of a family of similar potential binding domains and a …
Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins
PJ Mitchell, R Tjian - Science, 1989 - science.org
The cloning of genes encoding mammalian DNA binding transcription factors for RNA
polymerase II has provided the opportunity to analyze the structure and function of these …
polymerase II has provided the opportunity to analyze the structure and function of these …