Evidence map›Paper›PMID 26445442›Full record

ArticleBiophysical journal2015

Rapid Bioinformatic Identification of Thermostabilizing Mutations.

David B Sauer, Nathan K Karpowich, Jin Mei Song, Da-Neng Wang

Abstract read
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

David B SauerDepartment of Cell Biology, The Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, New York. Electronic address: david.sauer@med.nyu.edu.
Nathan K KarpowichDepartment of Cell Biology, The Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, New York.
Jin Mei SongDepartment of Cell Biology, The Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, New York.
Da-Neng WangDepartment of Cell Biology, The Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, New York. Electronic address: da-neng.wang@med.nyu.edu.

Funding

STRUCTURAL STUDIES OF SUGAR TRANSPORTERSR01DK053973 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 1998 to 2014
$3.6M
Dopamine Transporters: Mechanisms of Ligand InteractionR01DA019676 · NIDA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI REITH, MAARTEN E · 2006 to 2016
$2.9M
Structural and Mechanistic Characterization of Neurotransmitter Reuptake InhibitiR01MH083840 · NIMH · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2008 to 2012
$2.2M
Structural and mechanistic studies of INDY proteinsR01DK099023 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2013 to 2016
$1.5M
Structural Basis of Tetracycline Resistance by Efflux Pump TetL.R01GM093825 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2010 to 2014
$1.4M
Intra-renal Bold MRI: Application to Diabetic NephropathyR01DK073973 · NIDDK · NORTHSHORE UNIVERSITY HEALTHSYSTEM · PI PRASAD, POTTUMARTHI V · 2007 to 2009
$677k
Crystallization of neurotransmitter transporter homologsR21GM075936 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2005 to 2007
$594k
Overexpression/crystallization of amino acid transporterR21DK060841 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DA-NENG · 2001 to 2002
$337k
NIDA NIH HHS R01 DA019676NIDDK NIH HHS R01 DK053973NIDDK NIH HHS R01 DK073973NIDDK NIH HHS R01-DK073973NIDDK NIH HHS R01 DK099023NIDDK NIH HHS R01-DK099023NIGMS NIH HHS R01 GM093825NIGMS NIH HHS R01-GM093825NIGMS NIH HHS R21 GM075936NIMH NIH HHS R01 MH083840NIMH NIH HHS R01-MH083840
6 · The paper itself

Abstract

Ex vivo stability is a valuable protein characteristic but is laborious to improve experimentally. In addition to biopharmaceutical and industrial applications, stable protein is important for biochemical and structural studies. Taking advantage of the large number of available genomic sequences and growth temperature data, we present two bioinformatic methods to identify a limited set of amino acids or positions that likely underlie thermostability. Because these methods allow thousands of homologs to be examined in silico, they have the advantage of providing both speed and statistical power. Using these methods, we introduced, via mutation, amino acids from thermoadapted homologs into an exemplar mesophilic membrane protein, and demonstrated significantly increased thermostability while preserving protein activity.

Indexed as

MutationProtein StabilityTemperatureAmino AcidsAnti-Bacterial AgentsAntiportersBacillus subtilisBacterial ProteinsComputational BiologyEscherichia coliGreen Fluorescent ProteinsTetracyclineTransfectionAmino AcidsAnti-Bacterial AgentsAntiportersBacterial ProteinsGreen Fluorescent ProteinsTetL protein, Bacillus subtilisTetracycline

Identifiers

PMID26445442
PMCPMC4601007

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.