A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins.
Danish Khan, Dongju Lee, Gulcin Gulten, Anup Aggarwal, Joshua Wofford, Inna Krieger, Ashutosh Tripathi, John W Patrick, Debra M Eckert, Arthur Laganowsky and 3 more
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.0field-weighted citation impact, top 28% 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
4 citing papers in PubMed, 11 citations in OpenAlex.
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
13 authors at 4 institutions in 1 country.
Danish KhanDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, United States.ORCID 0000-0002-0650-3990
Dongju Lee *Department of Molecular and Cellular Medicine, Texas A&M Health Sciences Center, College Station, United States.
Gulcin Gulten *Department of Biochemistry and Biophysics, Texas A&M University, College Station, United States.
Anup AggarwalDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, United States.
Joshua WoffordDepartment of Chemistry, Texas A&M University, College Station, United States.
Inna KriegerDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, United States.
Ashutosh TripathiDepartment of Molecular and Cellular Medicine, Texas A&M Health Sciences Center, College Station, United States.
John W PatrickDepartment of Chemistry, Texas A&M University, College Station, United States.
Debra M EckertDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, United States.
Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, United States.
James SacchettiniDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, United States.ORCID 0000-0001-5767-2367
Paul LindahlDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, United States.
Vytas A BankaitisDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, United States.ORCID 0000-0002-1654-6759
Texas A&M University · USTexas A&M Health Science Center · USCharleston Southern University · USUniversity of Utah · US
Funding
X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
Virus TransmissionP50AI150464 · NIAID · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 2019 to 2021
$14.9M
The Biology and Biochemistry of Lipid Transfer Protein-Regulated Phosphoinositide SignalingR35GM131804 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI Vytas A Bankaitis · 2019 to 2026
$4.5M
Iron Trafficking and Regulation in Biological SystemsR35GM127021 · NIGMS · TEXAS A&M UNIVERSITY · PI PAUL A. LINDAHL · 2018 to 2026
$3.4M
Native ion mobility mass spectrometry studies of potassium inward rectifier channels: insight into gating and lipid bindingDP2GM123486 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI LAGANOWSKY, ARTHUR D · 2016 to 2016
Yeast Sfh5 is an unusual member of the Sec14-like phosphatidylinositol transfer protein (PITP) family. Whereas PITPs are defined by their abilities to transfer phosphatidylinositol between membranes in vitro, and to stimulate phosphoinositide signaling in vivo, Sfh5 does not exhibit these activities. Rather, Sfh5 is a redox-active penta-coordinate high spin Fe
Indexed as
Carrier ProteinsHeme-Binding ProteinsPhosphatidylinositolsPhospholipid Transfer ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionCarrier ProteinsHeme-Binding ProteinsPhosphatidylinositolsPhospholipid Transfer ProteinsSaccharomyces cerevisiae ProteinsSEC14 protein, S cerevisiaeSFH5 protein, S cerevisiaeCandidahemelipid signalingmolecular biophysicsphosphoinositidesPITPsS. cerevisiaeSfh5structural biology
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.
A Sec14-like phosphatidylinositol transfer protein paralog defines a novel class of heme-binding proteins. · full record | OpenQuestion