ArticleProceedings of the National Academy of Sciences of the United States of America1991
Conversion of the E1A Cys4 zinc finger to a nonfunctional His2,Cys2 zinc finger by a single point mutation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed.
- Vertebrate-conserved Schnurri zinc fingers restrain Drosophila vein patterning.microPublication biology · 2024Article
- A viral suppressor of RNA silencing inhibits ARGONAUTE 1 function by precluding target RNA binding to pre-assembled RISC.Nucleic acids research · 2017Article
- Comparative Functional Genomic Analysis of TwoFrontiers in microbiology · 2016Article
- Cadmium down-regulates expression of XIAP at the post-transcriptional level in prostate cancer cells through an NF-kappaB-independent, proteasome-mediated mechanism.Molecular cancer · 2010Article
- Intrinsic structural disorder in adenovirus E1A: a viral molecular hub linking multiple diverse processes.Journal of virology · 2008Review
- Roles for APIS and the 20S proteasome in adenovirus E1A-dependent transcription.The EMBO journal · 2006Article
- C-terminal nsP1a protein of human astrovirus colocalizes with the endoplasmic reticulum and viral RNA.Journal of virology · 2004Article
- Adeno-associated virus Rep78 protein interacts with protein kinase A and its homolog PRKX and inhibits CREB-dependent transcriptional activation.Journal of virology · 1998Article
- Studies of cation binding in ZnCl2-regenerated bacteriorhodopsin by x-ray absorption fine structures: effects of removing water molecules and adding Cl- ions.Biophysical journal · 1997Article
- Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5.Molecular and cellular biology · 1996Article
- Subregions of the adenovirus E1A transactivation domain target multiple components of the TFIID complex.Molecular and cellular biology · 1995Article
- Mutational analysis of adeno-associated virus Rep protein-mediated inhibition of heterologous and homologous promoters.Journal of virology · 1995Article
- The LIM/double zinc-finger motif functions as a protein dimerization domain.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Requirement for a zinc motif for template recognition by the bacteriophage T7 primase.The EMBO journal · 1994Article
- The zinc finger region of the adenovirus E1A transactivating domain complexes with the TATA box binding protein.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Cysteine-dependent zinc binding by membrane proteins of Giardia lamblia.Infection and immunity · 1993Article
- The Drosophila doublesex proteins share a novel zinc finger related DNA binding domain.The EMBO journal · 1993Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Trans-activation by the adenovirus E1A 289R protein requires a zinc finger defined by Cys-154, Cys-157, Cys-171, and Cys-174. Whereas individually replacing the four cysteine residues with serines resulted in a loss of transactivation, only three of the Cys----Ser mutants (C157S, C171S, and C174S) lost the ability to bind Zn(II). X-ray absorption fine structure analysis revealed that, in the wild-type protein, Zn(II) is coordinated by four cysteine residues whereas in the C154S mutant, Zn(II) is coordinated by two histidines and two cysteines. The mutant protein probably retains, as ligands, two cysteines on the right side of the zinc finger (Cys-171 and Cys-174) and recruits two of the four histidines on the left side (His-149, His-152, His-158, and His-160), despite the presence of Cys-157. This finding may shed light on the general structural requirements of zinc fingers.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.