Evidence map›Paper›PMID 28975383›Full record

ArticleEuropean biophysics journal : EBJ2018

Intrinsic thermodynamics of high affinity inhibitor binding to recombinant human carbonic anhydrase IV.

Aurelija Mickevičiūtė, David D Timm, Marius Gedgaudas, Vaida Linkuvienė, Zhiwei Chen, Abdul Waheed, Vilma Michailovienė, Asta Zubrienė, Alexey Smirnov, Edita Čapkauskaitė and 9 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in European biophysics journal : EBJ, 2018. 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
1.1field-weighted citation impact, top 22% 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, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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

19 authors at 2 institutions in 2 countries.

Aurelija MickevičiūtėDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
David D TimmDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Marius GedgaudasDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Vaida LinkuvienėDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Zhiwei ChenDepartment of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO, 63104, USA.
Abdul WaheedDepartment of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO, 63104, USA.
Vilma MichailovienėDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Asta ZubrienėDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Alexey SmirnovDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Edita ČapkauskaitėDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Lina BaranauskienėDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Jelena JachnoDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Jurgita RevuckienėDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Elena ManakovaDepartment of Protein-DNA Interactions, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Saulius GražulisDepartment of Protein-DNA Interactions, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Jurgita MatulienėDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania.
Enrico Di CeraDepartment of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO, 63104, USA.
William S SlyDepartment of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, MO, 63104, USA.
Daumantas MatulisDepartment of Biothermodynamics and Drug Design, Institute of Biotechnology, Life Sciences Center, Vilnius University, Saulėtekio 7, 10257, Vilnius, Lithuania. matulis@ibt.lt.ORCID http://orcid.org/0000-0002-6178-6276
Vilnius University · LTSaint Louis University · US

Funding

STUDIES ON THROMBIN ALLOSTERYR01HL049413 · NHLBI · WASHINGTON UNIVERSITY · PI Enrico Di Cera · 2000 to 2026
$9.6M
Studies on the anticoagulant properties of thrombinR01HL073813 · NHLBI · WASHINGTON UNIVERSITY · PI DI CERA, ENRICO · 2003 to 2015
$5.3M
BIOPHYSICAL STUDIES OF THROMBINR29HL049413 · NHLBI · WASHINGTON UNIVERSITY · PI DI CERA, ENRICO · 1995 to 1999
–
Lietuvos Mokslo Taryba SEN-04/2015NHLBI NIH HHS R01 HL049413NHLBI NIH HHS R01 HL073813NHLBI NIH HHS R29 HL049413
6 · The paper itself

Abstract

Membrane-associated carbonic anhydrase (CA) isoform IV participates in carbon metabolism and pH homeostasis and is implicated in the development of eye diseases such as retinitis pigmentosa and glaucoma. A series of substituted benzenesulfonamides were designed and their binding affinity to CA IV was determined by fluorescent thermal shift assay and isothermal titration calorimetry (ITC). Compound [(4-chloro-2-phenylsulfanyl-5-sulfamoyl-benzoyl)amino]propyl acetate (19) bound CA IV with the K

Indexed as

Carbonic Anhydrase InhibitorsCarbonic Anhydrase IVCatalytic DomainHumansLigandsModels, MolecularProtein BindingRecombinant ProteinsThermodynamicsCarbonic Anhydrase InhibitorsCarbonic Anhydrase IVLigandsRecombinant ProteinsCarbonic anhydraseDifferential scanning fluorimetryFluorescent thermal shift assayIntrinsic thermodynamics of protein–ligand bindingIsothermal titration calorimetryX-ray crystallography

Identifiers

PMID28975383
PMCPMC6276378
OpenAlexW2761464773

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.