Evidence map›Paper›PMID 22120745›Full record

ArticleActa crystallographica. Section D, Biological crystallography2011

Deprotonated imidodiphosphate in AMPPNP-containing protein structures.

Miroslawa Dauter, Zbigniew Dauter

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Biological crystallography, 2011. 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
0.1field-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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Review
  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

2 authors at 1 institution in 1 country.

Miroslawa DauterBasic Research Program, SAIC-Frederick Inc., Argonne National Laboratory, Argonne, IL 60439, USA. dauter@anl.gov
Zbigniew Dauter
Argonne National Laboratory · US

Funding

Macromolecular Crystallography Research with Synchrotron RadiationZIABC010378 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DAUTER, ZBIGNIEW · 2009 to 2020
$18.8M
CCR NIH HHS HHSN261200800001CIntramural NIH HHSNCI NIH HHS HHSN261200800001EPHS HHS HHSN261200800001
6 · The paper itself

Abstract

Many different proteins utilize the chemical energy provided by the cofactor adenosine triphosphate (ATP) for their proper function. A number of structures in the Protein Data Bank (PDB) contain adenosine 5'-(β,γ-imido)triphosphate (AMPPNP), a nonhydrolysable analog of ATP in which the bridging O atom between the two terminal phosphate groups is substituted by the imido function. Under mild conditions imides do not have acidic properties and thus the imide nitrogen should be protonated. However, an analysis of protein structures containing AMPPNP reveals that the imide group is deprotonated in certain complexes if the negative charges of the phosphate moieties in AMPPNP are in part neutralized by coordinating divalent metals or a guanidinium group of an arginine.

Indexed as

ProtonsAdenylyl ImidodiphosphateDiphosphonatesModels, MolecularProteinsProtein Structure, TertiaryAdenylyl ImidodiphosphateDiphosphonatesimidodiphosphonic acidProteinsProtons

Identifiers

PMID22120745
PMCPMC3225179
OpenAlexW2072015441

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.