Evidence map›Paper›PMID 42160704›Full record

ArticleACS synthetic biology2026

Using Domain Insertion to Create Sulfite Reductases That Present Chemical-Dependent Activities.

Elizabeth Windham, Dru Myerscough, Samuel K Schwartz, Matthew D Carpenter, Caroline M Ajo-Franklin, Jonathan J Silberg

Abstract read
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In one paragraph

Article in ACS synthetic 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

6 authors.

Elizabeth WindhamDepartment of Biosciences, Rice University, 6100 Main Street, Houston, Texas 77005, United States.
Dru MyerscoughDepartment of Biosciences, Rice University, 6100 Main Street, Houston, Texas 77005, United States.
Samuel K SchwartzSystems, Synthetic, and Physical Biology Graduate Program, Rice University, 6100 Main Street, Houston, Texas 77005, United States.ORCID 0000-0003-1297-9909
Matthew D CarpenterSystems, Synthetic, and Physical Biology Graduate Program, Rice University, 6100 Main Street, Houston, Texas 77005, United States.ORCID 0000-0003-0310-2881
Caroline M Ajo-FranklinDepartment of Biosciences, Rice University, 6100 Main Street, Houston, Texas 77005, United States.ORCID 0000-0001-8909-6712
Jonathan J SilbergDepartment of Biosciences, Rice University, 6100 Main Street, Houston, Texas 77005, United States.ORCID 0000-0001-5612-0667

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Domain insertion can be used to create oxidoreductases whose activities are dependent upon analyte binding. To date, most domain insertion studies have targeted relatively small oxidoreductases of known structure, so it remains unclear how to apply this protein engineering approach to large hetero-oligomeric proteins that require dynamic conformational changes for catalysis. To address this question, we studied the effects of peptide and domain insertions on the activity of NADPH-dependent sulfite reductase (SiR) from

Indexed as

Protein EngineeringSulfite Reductase (NADPH)Escherichia coliProtein DomainsSulfite Reductase (NADPH)bioelectronicsdomain insertionextracellular electron transferoxidoreductaseprotein engineeringsensorsulfite reductasesynthetic biology

Identifiers

PMID42160704
PMCPMC13288892

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.