Evidence map›Paper›PMID 41993913›Full record

ArticlemicroPublication biology2026

Effect of Amino Acid Substitutions at Site F397 on the Kinetic and Thermostability Properties of

Alyssa Yanes, Marianne Gutierrez Santos, Isabella Chiang, Jaime Mayoral

Abstract read
In one paragraph

Article in microPublication biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Alyssa YanesDepartment of Biological Sciences, Florida International University, Miami, FL, US.
Marianne Gutierrez SantosDepartment of Biological Sciences, Florida International University, Miami, FL, US.
Isabella ChiangDepartment of Biological Sciences, Florida International University, Miami, FL, US.
Jaime MayoralDepartment of Biological Sciences, Florida International University, Miami, FL, US.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-Glucosidase B (BglB) hydrolyzes β‑glycosidic bonds in complex carbohydrates, playing an important role in global carbon cycling, and diverse biofuel and biotechnological applications. This study systematically evaluated the functional and structural role of residue F397 by generating and characterizing all 19 possible amino acid substitutions. Hydrophobic and neutral substitutions expressed efficiently and retained catalytic efficiency and substrate affinity comparable to wild-type, whereas charged or polar substitutions reduced BglB expression and structural stability. Kinetic analyses showed minimal effects on K

Identifiers

PMID41993913
PMCPMC13080521

What OpenQuestion holds

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Registered trials

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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.