Evidence map›Paper›PMID 24246881›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2013

Shortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.

Kazutoshi Yamamoto, Marc A Caporini, Sangchoul Im, Lucy Waskell, Ayyalusamy Ramamoorthy

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

  1. Sensing with photoluminescent semiconductor quantum dots.Methods and applications in fluorescence · 2019
    Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Kazutoshi YamamotoBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, United States.
Marc A CaporiniBruker BioSpin Corporation, 15 Fortune Drive, Billerica, MA 01821, United States.
Sangchoul ImDepartment of Anesthesiology, University of Michigan, VA Medical Center, Ann Arbor, MI, United States.
Lucy WaskellDepartment of Anesthesiology, University of Michigan, VA Medical Center, Ann Arbor, MI, United States.
Ayyalusamy RamamoorthyBiophysics and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, United States. Electronic address: ramamoor@umich.edu.
University of Michigan–Ann Arbor · USAnn Arbor VA Medical Center · USBruker (United States) · US

Funding

Supplement: Investigation of Membrane-Bound Cytochromes-P450-b5 InteractionsR01GM084018 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2018
$3.8M
Microsomal Cytochromes P450 and their Interactions with their Redox PartnersR01GM094209 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WASKELL, LUCY A · 2011 to 2014
$1.5M
Rapid and efficient production of functional Cytochrome P450 enzymatic complex foR01GM095640 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2010 to 2013
$1.3M
NIGMS NIH HHS GM084018NIGMS NIH HHS GM095640NIGMS NIH HHS R01 GM084018NIGMS NIH HHS R01 GM094209NIGMS NIH HHS R01 GM095640
6 · The paper itself

Abstract

Inherent low sensitivity of NMR spectroscopy has been a major disadvantage, especially to study biomolecules like membrane proteins. Recent studies have successfully demonstrated the advantages of performing solid-state NMR experiments at very low and ultralow temperatures to enhance the sensitivity. However, the long spin-lattice relaxation time, T1, at very low temperatures is a major limitation. To overcome this difficulty, we demonstrate the use of a copper-chelated lipid for magic angle spinning solid-state NMR measurements on cytochrome-b5 reconstituted in multilamellar vesicles. Our results on multilamellar vesicles containing as small as 0.5mol% of a copper-chelated lipid can significantly shorten T1 of protons, which can be used to considerably reduce the data collection time or to enhance the signal-to-noise ratio. We also monitored the effect of slow cooling on the resolution and sensitivity of (13)C and (15)N signals from the protein and (13)C signals from lipids.

Indexed as

AnimalsCarbon IsotopesChelating AgentsChromatography, High Pressure LiquidCopperCytochromes b5LipidsMembrane ProteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularRabbitsSignal-To-Noise RatioTemperatureCarbon IsotopesChelating AgentsCopperCytochromes b5LipidsMembrane ProteinsNitrogen IsotopesLow-temperatureMembrane proteinSensitivity

Identifiers

PMID24246881
PMCPMC3868731
OpenAlexW2091657997

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.