Evidence map›Paper›PMID 26717925›Full record

ArticleThe protein journal2016

Structural Studies of Component of Lysoamidase Bacteriolytic Complex from Lysobacter sp. XL1.

Svetlana Tishchenko, Azat Gabdulkhakov, Bogdan Melnik, Irina Kudryakova, Oleg Latypov, Natalya Vasilyeva, Alexey Leontievsky

Abstract read
PubMed Publisher
In one paragraph

Article in The protein journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. The First Homologous Expression System for the β-Lytic Protease ofInternational journal of molecular sciences · 2022
    Article
  4. Article
  5. β-Lytic Protease ofAntibiotics (Basel, Switzerland) · 2020
    Article
  6. Stability of Therapeutic Enzymes: Challenges and Recent Advances.Advances in experimental medicine and biology · 2019
    Review
  7. 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.

Svetlana TishchenkoInstitute of Protein Research, Russian Academy of Sciences, Institutskaya str. 4, Pushchino, 142290, Moscow Region, Russian Federation. sveta@vega.protres.ru.
Azat GabdulkhakovInstitute of Protein Research, Russian Academy of Sciences, Institutskaya str. 4, Pushchino, 142290, Moscow Region, Russian Federation.
Bogdan MelnikInstitute of Protein Research, Russian Academy of Sciences, Institutskaya str. 4, Pushchino, 142290, Moscow Region, Russian Federation.
Irina KudryakovaG.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Prospect Nauki 5, Pushchino, 142290, Moscow Region, Russian Federation.
Oleg LatypovG.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Prospect Nauki 5, Pushchino, 142290, Moscow Region, Russian Federation.
Natalya VasilyevaG.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Prospect Nauki 5, Pushchino, 142290, Moscow Region, Russian Federation.
Alexey LeontievskyG.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Prospect Nauki 5, Pushchino, 142290, Moscow Region, Russian Federation.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lysoamidase bacteriolytic complex (LBC) comprising five enzymes (L1-L5) is secreted into the culture liquid by gram-negative bacterium Lysobacter sp. XL1. The medicinal agent lysoamidase has a broad-antimicrobial spectrum. Bacteriolytic protease L1 belongs to the LBC. Recombinant L1 protease of Lysobacter sp. XL1 was expressed, purified to homogeneity and crystallized. The X-ray structure of L1 at 1.35 Å resolution has been determined using the synchrotron data and the molecular replacement method. L1 protease is a thermostable whose thermal unfolding proceeds in one step without forming stable intermediates. Structural information concerning L1 will contribute to the development of new-generation antimicrobial drugs, whose application will not be accompanied by the selection of resistant microorganisms.

Indexed as

Amino Acid SequenceCircular DichroismLysobacterModels, MolecularMolecular Sequence DataPeptide HydrolasesProtein UnfoldinglysoamidasePeptide HydrolasesBacteriolytic protease L1Circular dichroismCrystalsLysobacter sp. XL1StructureThermal unfolding

Identifiers

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.