Evidence map›Paper›PMID 29159215›Full record

ArticleData in brief2017

Nfs1 cysteine desulfurase protein complexes and phosphorylation sites as assessed by mass spectrometry.

Agostinho G Rocha, Simon A B Knight, Alok Pandey, Heeyong Yoon, Jayashree Pain, Debkumar Pain, Andrew Dancis

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Data in brief, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
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.

Agostinho G RochaDepartment of Medicine, Division of Hematology-Oncology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.
Simon A B KnightDepartment of Medicine, Division of Hematology-Oncology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.
Alok PandeyDepartment of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ, United States.
Heeyong YoonDepartment of Medicine, Division of Hematology-Oncology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.
Jayashree PainDepartment of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ, United States.
Debkumar PainDepartment of Pharmacology, Physiology and Neuroscience, New Jersey Medical School, Rutgers University, Newark, NJ, United States.
Andrew DancisDepartment of Medicine, Division of Hematology-Oncology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, United States.
University of Pennsylvania · USRutgers, The State University of New Jersey · US

Funding

Mitochondria-cytoplasm interactions for cytosolic Fe-S cluster assemblyR01GM107542 · NIGMS · RUTGERS BIOMEDICAL AND HEALTH SCIENCES · PI DANCIS, ANDREW B., PAIN, DEBKUMAR · 2014 to 2023
$4.5M
Biochemistry and genetics of iron transport in mitochondria and related processesR37DK053953 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI DANCIS, ANDREW B. · 2008 to 2015
$2.9M
IRON TRAFFICKING IN SACCHAROMYCES CEREVISIAER01DK053953 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI DANCIS, ANDREW B. · 1998 to 2007
$2.4M
NIDDK NIH HHS R01 DK053953NIDDK NIH HHS R37 DK053953NIGMS NIH HHS R01 GM107542
6 · The paper itself

Abstract

Fe-S clusters are cofactors that participate in diverse and essential biological processes. Mitochondria contain a complete machinery for Fe-S cluster assembly. Cysteine desulfurase (Nfs1) is required generation of a form of activated sulfur and is essential for the initial Fe-S cluster assembly step. Using mass-spectometry we identified proteins that were copurified with Nfs1 using a pull-down strategy, including a novel protein kinase. Furthermore, we were able to identify phosphorylation sites on the Nfs1 protein. These data and analyses support the research article "Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria" by Rocha et al. (in press) [1].

Identifiers

PMID29159215
PMCPMC5675994
OpenAlexW2764223791

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.