Evidence map›Paper›PMID 30585724›Full record

ArticleBiochemistry2019

A Robust Method for the Purification and Characterization of Recombinant Human Histone H1 Variants.

Adewola Osunsade, Nicholas A Prescott, Jakob M Hebert, Devin M Ray, Yazen Jmeian, Ivo C Lorenz, Yael David

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. A nucleosome switch primes Hepatitis B Virus infection.bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
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  7. Review
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  14. Article
  15. (De)Toxifying the Epigenetic Code.Chemical research in toxicology · 2019
    Review
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

7 authors at 2 institutions in 1 country.

Adewola OsunsadeChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10065 , United States.ORCID 0000-0001-6340-8765
Nicholas A PrescottChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10065 , United States.
Jakob M HebertChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10065 , United States.
Devin M RayChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10065 , United States.
Yazen JmeianTri-Institutional Therapeutics Discovery Institute , New York 10021 , United States.
Ivo C LorenzTri-Institutional Therapeutics Discovery Institute , New York 10021 , United States.
Yael DavidChemical Biology Program , Memorial Sloan Kettering Cancer Center , New York 10065 , United States.
Memorial Sloan Kettering Cancer Center · USTri-Institutional Therapeutics Discovery Institute · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SELWYN M VICKERS · 1985 to 2026
$347.4M
Weill Cornell/Rockefeller/Sloan-Kettering MST ProgramT32GM007739 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI HSU, KATHARINE C · 1985 to 2023
$51.1M
Tri-Institutional PhD Program in Chemical BiologyT32GM115327 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI TAN, DEREK S · 2015 to 2019
$741k
NCI NIH HHS P30 CA008748NIGMS NIH HHS T32 GM007739NIGMS NIH HHS T32 GM115327
6 · The paper itself

Abstract

Higher order compaction of the eukaryotic genome is key to the regulation of all DNA-templated processes, including transcription. This tightly controlled process involves the formation of mononucleosomes, the fundamental unit of chromatin, packaged into higher order architectures in an H1 linker histone-dependent process. While much work has been done to delineate the precise mechanism of this event in vitro and in vivo, major gaps still exist, primarily due to a lack of molecular tools. Specifically, there has never been a successful purification and biochemical characterization of all human H1 variants. Here we present a robust method to purify H1 and illustrate its utility in the purification of all somatic variants and one germline variant. In addition, we performed a first ever side-by-side biochemical comparison, which revealed a gradient of nucleosome binding affinities and compaction capabilities. These data provide new insight into H1 redundancy and lay the groundwork for the mechanistic investigation of disease-driving mutations.

Indexed as

Circular DichroismElectrophoresis, Polyacrylamide GelEscherichia coliHistonesHumansMicrococcal NucleaseNucleosomesPeptide LibraryProtein EngineeringRecombinant ProteinsSUMO-1 ProteinHistonesMicrococcal NucleaseNucleosomesPeptide LibraryRecombinant ProteinsSUMO-1 Protein

Identifiers

PMID30585724
PMCPMC6541009
OpenAlexW2905635030

What OpenQuestion holds

Textmetadata
LicenceTDM
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.