Evidence map›Paper›PMID 26457529›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

Stabilization of porcine pancreatic elastase crystals by glutaraldehyde cross-linking.

Stefan Hofbauer, José A Brito, Jalmira Mulchande, Przemyslaw Nogly, Miguel Pessanha, Rui Moreira, Margarida Archer

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 31% 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

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 1 country.

Stefan HofbauerInstituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Avenida da República, EAN, 2780-157 Oeiras, Portugal.
José A BritoInstituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Avenida da República, EAN, 2780-157 Oeiras, Portugal.
Jalmira MulchandeResearch Institute for Medicines (i-Med.ULisboa), Faculdade de Farmácia, Universidade de Lisboa, Avenida Professor Gama Pinto, 1649-003 Lisboa, Portugal.
Przemyslaw NoglyInstituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Avenida da República, EAN, 2780-157 Oeiras, Portugal.
Miguel PessanhaInstituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Avenida da República, EAN, 2780-157 Oeiras, Portugal.
Rui MoreiraResearch Institute for Medicines (i-Med.ULisboa), Faculdade de Farmácia, Universidade de Lisboa, Avenida Professor Gama Pinto, 1649-003 Lisboa, Portugal.
Margarida ArcherInstituto de Tecnologia Química e Biológica - António Xavier, Universidade Nova de Lisboa, Avenida da República, EAN, 2780-157 Oeiras, Portugal.
Instituto de Biologia Experimental e Tecnológica · PTUniversity of Lisbon · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elastase is a serine protease from the chymotrypsin family of enzymes with the ability to degrade elastin, an important component of connective tissues. Excessive elastin proteolysis leads to a number of pathological diseases. Porcine pancreatic elastase (PPE) is often used for drug development as a model for human leukocyte elastase (HLE), with which it shares high sequence identity. Crystals of PPE were grown overnight using sodium sulfate and sodium acetate at acidic pH. Cross-linking the crystals with glutaraldehyde was needed to resist the soaking procedure with a diethyl N-(methyl)pyridinyl-substituted oxo-β-lactam inhibitor. Crystals of PPE bound to the inhibitor belonged to the orthorhombic space group P2₁2₁2₁, with unit-cell parameters a = 51.0, b = 58.3, c = 74.9 Å, and diffracted to 1.8 Å resolution using an in-house X-ray source.

Indexed as

Animalsbeta-Lactamase InhibitorsCross-Linking ReagentsCrystallizationCrystallography, X-RayEnzyme StabilityGlutaralPancreasPancreatic ElastaseSus scrofabeta-Lactamase InhibitorsCross-Linking ReagentsGlutaralPancreatic Elastaseglutaraldehyde cross-linkingporcine pancreatic elastasesensitive protein crystalsserine proteasesoaking of hydrophobic ligandstreak-seeding

Identifiers

PMID26457529
PMCPMC4601602
OpenAlexW2294178516

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.