The In Silico Characterization of Monocotyledonous α-l-Arabinofuranosidases on the Example of Maize.

Alsu Nazipova, Olga Makshakova, Liudmila Kozlova

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Article in Life (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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.

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5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Alsu NazipovaThe Laboratory of Plant Cell Growth Mechanisms, Kazan Institute of Biochemistry and Biophysics FRC Kazan Scientific Center of RAS, Lobachevsky Str. 2/31, 420111 Kazan, Russia.

Olga MakshakovaThe Laboratory of Biophysical Chemistry of Nanosystems, Kazan Institute of Biochemistry and Biophysics FRC Kazan Scientific Center of RAS, Lobachevsky Str. 2/31, 420111 Kazan, Russia.ORCID 0000-0002-0615-3513

Liudmila KozlovaThe Laboratory of Plant Cell Growth Mechanisms, Kazan Institute of Biochemistry and Biophysics FRC Kazan Scientific Center of RAS, Lobachevsky Str. 2/31, 420111 Kazan, Russia.ORCID 0000-0002-6323-167X

Kazan Institute of Biochemistry and Biophysics · RU

Funding

Russian Science Foundation 18-14-00168The government assignment for the FRC Kazan Scientific Center of RAS

6 · The paper itself

Abstract

Plant α-l-arabinofuranosidases remove terminal arabinose from arabinose-containing substrates such as plant cell wall polysaccharides, including arabinoxylans, arabinogalactans, and arabinans. In plants, de-arabinosylation of cell wall polysaccharides accompanies different physiological processes such as fruit ripening and elongation growth. In this report, we address the diversity of plant α-l-arabinofuranosidases of the glycoside hydrolase (GH) family 51 through their phylogenetic analysis as well as their structural features. The CBM4-like domain at N-terminus was found to exist only in GH51 family proteins and was detected in almost 90% of plant sequences. This domain is similar to bacterial CBM4, but due to substitutions of key amino acid residues, it does not appear to be able to bind carbohydrates. Despite isoenzymes of GH51 being abundant, in particular in cereals, almost half of the GH51 proteins in

Indexed as

arabinoxylanhomology modelingmaizemolecular dockingα-l-arabinofuranosidase

Identifiers

PMID36836625

DOI10.3390/life13020266

PMCPMC9964162

OpenAlexW4317426601

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LicenceCC BY

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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.