Evidence map›Paper›PMID 26851284›Full record

ArticleThe Journal of biological chemistry2016

Introduction to the Thematic Minireview Series on Intrinsically Disordered Proteins.

Ruma Banerjee

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. 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
–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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Intrinsic protein disorder in oncogenic KRAS signaling.Cellular and molecular life sciences : CMLS · 2017
    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

1 author.

Ruma BanerjeeFrom the Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109-0600 rbanerje@umich.edu.

Funding

REACTION MECHANISMS OF MAMMALIAN B12-DEPENDENT ENZYMESR01DK045776 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI RUMA V BANERJEE · 1998 to 2026
$9.7M
Transsulfuration and HyperhomocysteinemiaR01HL058984 · NHLBI · UNIVERSITY OF NEBRASKA LINCOLN · PI BANERJEE, RUMA V · 1997 to 2020
$6.0M
Enzymology of Sulfide OxidationR01GM112455 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BANERJEE, RUMA V · 2014 to 2017
$1.2M
REACTION MECHANISMS OF COBALAMIN-DEPENDENT ENZYMESR29DK045776 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI BANERJEE, RUMA V · 1993 to 1997
–
NHLBI NIH HHS HL58984NHLBI NIH HHS R01 HL058984NIDDK NIH HHS DK45776NIDDK NIH HHS R01 DK045776NIGMS NIH HHS GM112455NIGMS NIH HHS R01 GM112455
6 · The paper itself

Abstract

In this thematic minireview series, the JBC presents six exciting articles on low complexity or intrinsically disordered proteins (IDPs). The dynamical and fluctuating structures of IDPs or of disordered regions within proteins result in virtually all of their primary sequence being exposed, at least at some time, to potential interacting partners. Their structural versatility underlies their often wide functional repertoires, which is further expanded by post-translational modifications. Given these characteristics, it is not surprising that IDPs serve as important hubs in signaling networks, scaffolding multivalent interactions. They are also important for organizing membrane-less protein organelles. This collection of reviews discusses biophysical approaches for studying IDPs and illuminates their importance to critical functions such as cell cycle control, transcription, and translation, as well as their regulation via cellular input signals.

Indexed as

Protein Processing, Post-TranslationalBiophysicsCell CycleHumansIntrinsically Disordered ProteinsProtein BiosynthesisProtein ConformationProtein FoldingSignal TransductionTranscription, GeneticIntrinsically Disordered Proteinsconformational changeintrinsically disordered proteinpost-translational modification (PTM)protein foldingsignaling

Identifiers

PMID26851284
PMCPMC4807254

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.