Evidence map›Paper›PMID 15388867›Full record

ArticleProtein science : a publication of the Protein Society2004

Arm-domain interactions can provide high binding cooperativity.

Robert Schleif, Cynthia Wolberger

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

2 authors at 2 institutions in 1 country.

Robert SchleifBiology Department, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA. schleif@jhu.edu
Cynthia Wolberger
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

REGULATORY MECHANISMS OF THE E COLI ARABINOSE OPERONR37GM018277 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHLEIF, ROBERT F. · 1994 to 2004
$2.3M
REGULATORY MECHANISMS OF THE E COLI ARABINOSE OPERONR01GM018277 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHLEIF, ROBERT F. · 1985 to 2009
$2.2M
BIOPHYSICS OF THE NUCLEOPROTEIN ACCESSORY PROTEIN NHP6AF32GM018277 · NIGMS · FOX CHASE CANCER CENTER · PI KATZ, DARIN S · 1996 to 1997
–
NIGMS NIH HHS F32 GM018277NIGMS NIH HHS GM18277NIGMS NIH HHS R01 GM018277NIGMS NIH HHS R37 GM018277
6 · The paper itself

Abstract

Peptidyl arms extending from one protein domain to another protein domain mediate many important interactions in biology. A well-studied example of this type of protein-protein interaction occurs between the yeast homeodomain proteins, MAT alpha2 and MAT a1, which form a high-affinity heterodimer on DNA. The carboxyl-terminal arm extending from MAT alpha2 to MAT a1 has been proposed to produce an allosteric conformational change in the a1 protein that generates a very large increase in the DNA binding affinity of a1. Although early studies lent some support to this model, a more recent crystal structure determination of the free a1 protein argues against any allosteric change. This note presents a thermodynamic argument that accounts for the proteins' binding behavior, so that allosteric conformational changes are not required to explain the large affinity increase. The analysis presented here should be useful in analyzing binding behavior in other systems involving arm interactions.

Indexed as

Computational BiologyDimerizationDNADNA-Binding ProteinsHomeodomain ProteinsProtein Structure, TertiaryRepressor ProteinsSaccharomyces cerevisiae ProteinsThermodynamicsDNADNA-Binding ProteinsHomeodomain ProteinsMATA1 protein, S cerevisiaeMATA2 protein, S cerevisiaeRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID15388867
PMCPMC2286541
OpenAlexW1993822100

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.