Evidence map›Paper›PMID 7629052›Full record

ReviewJournal of bioenergetics and biomembranes1995

Effects of phosphorylation of P-glycoprotein on multidrug resistance.

U A Germann, T C Chambers, S V Ambudkar, I Pastan, M M Gottesman

Abstract readComparative StudyReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

11 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Inhibition of the multidrug resistance P-glycoprotein: time for a change of strategy?Drug metabolism and disposition: the biological fate of chemicals · 2014
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Regulation of organic anion transport in the liver.The Yale journal of biology and medicine
    Review
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

5 authors at 5 institutions in 1 country.

U A GermannVertex Pharmaceuticals Incorporated, Cambridge, Massachusetts 02139, USA.
T C Chambers
S V Ambudkar
I Pastan
M M Gottesman
Johns Hopkins Medicine · USNational Cancer Institute · USNational Institutes of Health · USUniversity of Arkansas for Medical Sciences · USVertex Pharmaceuticals (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells expressing elevated levels of the membrane phosphoprotein P-glycoprotein exhibit a multidrug resistance phenotype. Studies involving protein kinase activators and inhibitors have implied that covalent modification of P-glycoprotein by phosphorylation may modulate its biological activity as a multidrug transporter. Most of these reagents, however, have additional mechanisms of action and may alter drug accumulation within multidrug resistant cells independent of, or in addition to, their effects on the state of phosphorylation of P-glycoprotein. The protein kinase(s) responsible for P-glycoprotein phosphorylation has(ve) not been unambiguously identified, although several possible candidates have been suggested. Recent biochemical analyses demonstrate that the major sites of phosphorylation are clustered within the linker region that connects the two homologous halves of P-glycoprotein. Mutational analyses have been initiated to confirm this finding. Preliminary data obtained from phosphorylation- and dephosphorylation-defective mutants suggest that phosphorylation of P-glycoprotein is not essential to confer multidrug resistance.

Indexed as

Drug Resistance, MultipleAmino Acid SequenceAnimalsATP Binding Cassette Transporter, Subfamily B, Member 1Cell MembraneDNA Mutational AnalysisHumansModels, StructuralMolecular Sequence DataPhosphorylationProtein KinasesProtein Structure, SecondaryRecombinant ProteinsSequence Homology, Amino AcidATP Binding Cassette Transporter, Subfamily B, Member 1Protein KinasesRecombinant Proteins

Identifiers

PMID7629052
OpenAlexW2040855441

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.