Evidence map›Paper›PMID 17468268›Full record

ArticleApplied and environmental microbiology2007

Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains.

D Guillén, M Santiago, L Linares, R Pérez, J Morlon, B Ruiz, S Sánchez, R Rodríguez-Sanoja

Open access · greenAbstract readComparative Study
In one paragraph

Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 49 citations in OpenAlex.

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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

8 authors at 4 institutions in 3 countries.

D GuillénDepartamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, UNAM, A.P. 70228, 04510 México D.F., Mexico.
M Santiago
L Linares
R Pérez
J Morlon
B Ruiz
S Sánchez
R Rodríguez-Sanoja
Universidad Nacional Autónoma de México · MXCenter of Molecular Immunology (Cuba) · CUInstitut de Recherche en Infectiologie de Montpellier · FRStation Biologique de Roscoff · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Lactobacillus amylovorus alpha-amylase starch binding domain (SBD) is a functional domain responsible for binding to insoluble starch. Structurally, this domain is dissimilar from other reported SBDs because it is composed of five identical tandem modules of 91 amino acids each. To understand adsorption phenomena specific to this SBD, the importance of their modular arrangement in relationship to binding ability was investigated. Peptides corresponding to one, two, three, four, or five modules were expressed as His-tagged proteins. Protein binding assays showed an increased capacity of adsorption as a function of the number of modules, suggesting that each unit of the SBD may act in an additive or synergic way to optimize binding to raw starch.

Indexed as

Adsorptionalpha-AmylasesDNA PrimersElectrophoresis, Polyacrylamide GelLactobacillus acidophilusPlasmidsProtein BindingProtein Structure, TertiaryStarchalpha-AmylasesDNA PrimersStarch

Identifiers

PMID17468268
PMCPMC1932744
OpenAlexW2135784586

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.