Evidence map›Paper›PMID 31213125›Full record

ArticleRNA biology2019

A two-step probing method to compare lysine accessibility across macromolecular complex conformations.

Andrew J MacRae, Patricia Coltri, Eva Hrabeta-Robinson, Robert J Chalkley, A L Burlingame, Melissa S Jurica

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 95% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 3 institutions in 2 countries.

Andrew J MacRaeDepartment of Molecular, Cell and Developmental Biology, University California , Santa Cruz , USA.ORCID 0000-0002-5676-4312
Patricia ColtriDepartment of Molecular, Cell and Developmental Biology, University California , Santa Cruz , USA.ORCID 0000-0001-8447-7516
Eva Hrabeta-RobinsonDepartment of Molecular, Cell and Developmental Biology, University California , Santa Cruz , USA.
Robert J ChalkleyDepartment of Pharmaceutical Chemistry, University of California San Francisco , San Francisco , CA , USA.
A L BurlingameDepartment of Pharmaceutical Chemistry, University of California San Francisco , San Francisco , CA , USA.
Melissa S JuricaDepartment of Molecular, Cell and Developmental Biology, University California , Santa Cruz , USA.ORCID 0000-0002-4488-1386
University of California, Santa Cruz · USUniversity of California, San Francisco · USUniversidade de São Paulo · BR

Funding

YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JULIUS, DAVID · 1985 to 2011
$24.1M
Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Training Program/Molecular/Cell/Developmental BiologyT32GM008646 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI STROME, SUSAN · 1999 to 2018
$3.7M
Interpreting the Structure of the SpliceosomeR01GM072649 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI JURICA, MELISSA S · 2006 to 2016
$2.7M
Mechanisms of the spliceosome protein SF3B1 and inhibitorsR01GM122279 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI JURICA, MELISSA S · 2017 to 2020
$1.8M
PURCHASE OF LTQ FT-ICR HYBRID MASS SPECTROMETER: (HEI) PROTEOMICSS10RR019934 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BURLINGAME, ALMA L · 2004 to 2004
$1.0M
PURCHASE OF MICRO LC/NANO ESIQQTOF MASS SPECTROMETERS10RR015804 · NCRR · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BURLINGAME, ALMA L · 2001 to 2001
$500k
NCRR NIH HHS P41 RR001614NCRR NIH HHS S10 RR015804NCRR NIH HHS S10 RR019934NIGMS NIH HHS P41 GM103481NIGMS NIH HHS R01 GM072649NIGMS NIH HHS R01 GM122279NIGMS NIH HHS T32 GM008646
6 · The paper itself

Abstract

Structural models of large and dynamic molecular complexes are appearing in increasing numbers, in large part because of recent technical advances in cryo-electron microscopy. However, the inherent complexity of such biological assemblies comprising dozens of moving parts often limits the resolution of structural models and leaves the puzzle as to how each functional configuration transitions to the next. Orthogonal biochemical information is crucial to understanding the molecular interactions that drive those rearrangements. We present a two-step method for chemical probing detected by tandem mass-spectrometry to globally assess the reactivity of lysine residues within purified macromolecular complexes. Because lysine side chains often balance the negative charge of RNA in ribonucleoprotein complexes, the method is especially useful for detecting changes in protein-RNA interactions. By probing the

Indexed as

Models, MolecularMolecular ConformationAcetylationCrystallography, X-RayHumansLysineMacromolecular SubstancesPeptidesRibosome Subunits, Small, BacterialRNASpliceosomesTandem Mass SpectrometryLysineMacromolecular SubstancesPeptidesRNAChemical probinglysinemass spectrometryRNA protein complex

Identifiers

PMID31213125
PMCPMC6779377
OpenAlexW2949502218

What OpenQuestion holds

Textmetadata
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.