Evidence map›Paper›PMID 19693704›Full record

ArticleBiomolecular NMR assignments2009

(1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA.

Stephen Martin-Tumasz, Samuel E Butcher

Abstract read
In one paragraph

Article in Biomolecular NMR assignments, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
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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

2 authors.

Stephen Martin-TumaszDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Samuel E Butcher

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
900 MHz NMR Spectrometer Biomolecular InvestigationsP41GM066326 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN L · 2002 to 2006
$5.0M
Structure and Function of U6 Spliceosomal RNAR01GM065166 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BROW, DAVID A, BUTCHER, SAMUEL E · 2002 to 2016
$3.5M
WIDE-BORE 9.4 TESLA NMR SPECTROMETER FOR UW-MADISONS10RR002781 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1986 to 1986
–
CONSOLE UPGRADES FOR NMR FACILITYS10RR008438 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1993 to 1993
–
NCRR NIH HHS P41 RR002301NCRR NIH HHS P41RR02301NCRR NIH HHS S10 RR002781NCRR NIH HHS S10 RR008438NIGMS NIH HHS GM007215NIGMS NIH HHS GM065166NIGMS NIH HHS P41 GM066326NIGMS NIH HHS P41GM66326NIGMS NIH HHS R01 GM065166NIGMS NIH HHS T32 GM007215
6 · The paper itself

Abstract

Saccharomyces cerevisiae Prp24 is an essential RNA binding protein involved in pre-mRNA splicing. Nearly complete backbone and side chain resonance assignments have been obtained for the second RNA recognition motif (RRM) of Prp24 (RRM2, residues M114-E197) both in isolation and bound to a six nucleotide fragment of U6 RNA (AGAGAU). In addition, nearly complete backbone assignments have been made for a Prp24 construct spanning the second and third RRMs (RRM23, residues M114-K290), both free and bound to AGAGAU.

Indexed as

Amino Acid MotifsBase SequenceNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryRibonucleoproteins, Small NuclearRNASaccharomyces cerevisiae ProteinsPrp24 protein, S cerevisiaeRibonucleoproteins, Small NuclearRNASaccharomyces cerevisiae Proteins

Identifiers

PMID19693704
PMCPMC2972308

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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.