Evidence map›Paper›PMID 26527144›Full record

ArticleActa crystallographica. Section D, Biological crystallography2015

The structure of the GemC1 coiled coil and its interaction with the Geminin family of coiled-coil proteins.

Christophe Caillat, Alexander Fish, Dafni Eleftheria Pefani, Stavros Taraviras, Zoi Lygerou, Anastassis Perrakis

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

16 citing papers in PubMed, 26 citations in OpenAlex.

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  8. Cell cycle (Georgetown, Tex.) · 2019
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Christophe CaillatDepartment of Biochemistry, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands.
Alexander FishDepartment of Biochemistry, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands.
Dafni Eleftheria PefaniLaboratory of Biology, School of Medicine, University of Patras, 26505 Rio, Patras, Greece.
Stavros TaravirasLaboratory of Physiology, School of Medicine, University of Patras, 26505 Rio, Patras, Greece.
Zoi LygerouLaboratory of Biology, School of Medicine, University of Patras, 26505 Rio, Patras, Greece.
Anastassis PerrakisDepartment of Biochemistry, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands.
The Netherlands Cancer Institute · NLUniversity of Patras · GR

Funding

European Research Council 281851
6 · The paper itself

Abstract

GemC1, together with Idas and Geminin, an important regulator of DNA-replication licensing and differentiation decisions, constitute a superfamily sharing a homologous central coiled-coil domain. To better understand this family of proteins, the crystal structure of a GemC1 coiled-coil domain variant engineered for better solubility was determined to 2.2 Å resolution. GemC1 shows a less typical coiled coil compared with the Geminin homodimer and the Geminin-Idas heterodimer structures. It is also shown that both in vitro and in cells GemC1 interacts with Geminin through its coiled-coil domain, forming a heterodimer that is more stable that the GemC1 homodimer. Comparative analysis of the thermal stability of all of the possible superfamily complexes, using circular dichroism to follow the unfolding of the entire helix of the coiled coil, or intrinsic tryptophan fluorescence of a unique conserved N-terminal tryptophan, shows that the unfolding of the coiled coil is likely to take place from the C-terminus towards the N-terminus. It is also shown that homodimers show a single-state unfolding, while heterodimers show a two-state unfolding, suggesting that the dimer first falls apart and the helices then unfold according to the stability of each protein. The findings argue that Geminin-family members form homodimers and heterodimers between them, and this ability is likely to be important for modulating their function in cycling and differentiating cells.

Indexed as

Amino Acid SequenceCarrier ProteinsCell Cycle ProteinsCrystallography, X-RayGemininHumansModels, MolecularMolecular Sequence DataProtein ConformationProtein Interaction MapsProtein MultimerizationProtein StabilityTemperatureCarrier ProteinsCell Cycle ProteinsGemininGMNC protein, humancoiled coilDNA-replication licenseGemC1GemininIdasMcIdasmulticilinprotein stability

Identifiers

PMID26527144
PMCPMC4631479
OpenAlexW2123483058

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.