Evidence map›Paper›PMID 8298459›Full record

ArticleProtein science : a publication of the Protein Society1993

MIF protein are theta-class glutathione S-transferase homologs.

F A Blocki, L B Ellis, L P Wackett

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Role of macrophage migration inhibitory factor in age-related lung disease.American journal of physiology. Lung cellular and molecular physiology · 2015
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Crystal structure at 2.6-A resolution of human macrophage migration inhibitory factor.Proceedings of the National Academy of Sciences of the United States of America · 1996
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. MIF proteins are not glutathione transferase homologs.Protein science : a publication of the Protein Society · 1994
    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

3 authors at 2 institutions in 1 country.

F A BlockiDepartment of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul 55108.
L B Ellis
L P Wackett
University of Minnesota · USEarthTech International (United States) · US

Funding

MECHANISM OF BACTERIAL DEHALOGENASESR29GM041235 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WACKETT, LAWRENCE P · 1989 to 1993
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CHEMICAL BASES OF CELL AND MOLECULAR BIOLOGYT32GM007323 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI GOLDSTEIN, IRIS · 1985 to 1995
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NIGMS NIH HHS 5T32GM07323NIGMS NIH HHS GM 41235
6 · The paper itself

Abstract

MIF proteins are mammalian polypeptides of approximately 13,000 molecular weight. This class includes human macrophage migration inhibitory factor (MIF), a rat liver protein that has glutathione S-transferase (GST) activity (TRANSMIF), and the mouse delayed early response gene 6 (DER6) protein. MIF proteins were previously linked to GSTs by demonstrating transferase activity and observing N-terminal sequence homology with a mu-class GST (Blocki, F.A., Schlievert, P.M., & Wackett, L.P., 1992, Nature 360, 269-270). In this study, MIF proteins are shown to be structurally related to the theta class of GSTs. This is established in three ways. First, unique primary sequence patterns are developed for each of the GST gene classes. The patterns identify the three MIF proteins as theta-like transferase homologs. Second, pattern analysis indicates that GST members of the theta class contain a serine residue in place of the N-terminal tyrosine that is implicated in glutathione deprotonation and activation in GSTs of known structure (Liu, S., et al., 1992, J. Biol. Chem. 267, 4296-4299). The MIF proteins contain a threonine at this position. Third, polyclonal antibodies raised against recombinant human MIF cross-react on Western blots with rat theta GST but not with alpha and mu GSTs. That MIF proteins have glutathione-binding ability may provide a common structural key toward understanding the varied functions of this widely distributed emerging gene family. Because theta is thought to be the most ancient evolutionary GST class, MIF proteins may have diverged early in evolution but retained a glutathione-binding domain.

Indexed as

Glutathione TransferaseMacrophage Migration-Inhibitory FactorsSequence Homology, Amino AcidAmino Acid SequenceBlotting, WesternCross ReactionsMathematical ComputingMolecular Sequence DataSequence AlignmentGlutathione TransferaseMacrophage Migration-Inhibitory Factors

Identifiers

PMID8298459
PMCPMC2142320
OpenAlexW1995855154

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.