ArticleThe EMBO journal1995
The crystal structure of p13suc1, a p34cdc2-interacting cell cycle control protein.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 72 citations in OpenAlex.
- The Prozone Effect Accounts for the Paradoxical Function of the Cdk-Binding Protein Suc1/Cks.Cell reports · 2016Article
- The structure of a monomeric mutant Cks protein reveals multiple functions for a conserved hinge-region proline.Journal of molecular biology · 2011Article
- Preliminary crystallographic analysis of the Cks protein p13(suc1P90AP92A) from Schizosacharromyces pombe.European biophysics journal : EBJ · 2005Article
- Validity of Gō models: comparison with a solvent-shielded empirical energy decomposition.Biophysical journal · 2002Article
- Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe.Journal of biomolecular NMR · 2002Article
- 3D domain swapping: as domains continue to swap.Protein science : a publication of the Protein Society · 2002Review
- Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Inhibitory effect of zinc on human prostatic carcinoma cell growth.The Prostate · 1999Article
- Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 1998Review
- Cyclin-stimulated binding of Cks proteins to cyclin-dependent kinases.Molecular and cellular biology · 1998Article
- Leishmania mexicana p12cks1, a homologue of fission yeast p13suc1, associates with a stage-regulated histone H1 kinase.The Biochemical journal · 1996Article
- Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p13suc1 binds to p34cdc2 kinase and is essential for cell cycle progression in eukaryotic cells. The crystal structure of S.pombe p13suc1 has been solved to 2.7 A resolution using data collected at the ESRF source, Grenoble, from both native crystals and crystals of a seleno-methionine derivative. The starting point for structure solution was the determination of the six selenium sites by direct methods. The structure is dominated by a four-stranded beta-sheet, with four further alpha-helical regions. p13suc1 crystallizes as a dimer in the asymmetric unit stabilized by the binding of two zinc ions. A third zinc site stabilizes the higher-order crystal packing. The sites are consistent with a requirement for zinc during crystal growth. A likely site for p13suc1-protein interaction is immediately evident on one face of the p13suc1 surface. This region comprises a group of conserved, exposed aromatic and hydrophobic residues below a flexible negatively charged loop. A conserved positively charged area would also present a notable surface feature in the monomer, but is buried at the dimer interface. p13suc1 is larger than its recently solved human homologue p9CKS2, with the extra polypeptide forming a helical N-terminal extension and a surface loop between alpha-helices 3 and 4. Notably, p13suc1 does not show the unusual beta-strand exchange that creates an intimate p9CKS2 dimer. p13suc1 cannot oligomerize to form a stable hexamer as has been proposed for p9CKS2.
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.