Evidence map›Paper›PMID 30802311›Full record

ArticleBiotechnology and bioengineering2019

Establishing synthesis pathway-host compatibility via enzyme solubility.

Sara A Amin, Venkatesh Endalur Gopinarayanan, Nikhil U Nair, Soha Hassoun

Open access · greenAbstract read
In one paragraph

Article in Biotechnology and bioengineering, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

3 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Strategic Approaches to Improvise Peptide Drugs as Next Generation Therapeutics.International journal of peptide research and therapeutics · 2023
    Review
  3. 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

4 authors at 1 institution in 1 country.

Sara A AminDepartment of Computer Science, Tufts University, Medford, Massachusetts.
Venkatesh Endalur GopinarayananDepartment of Chemical and Biological Engineering, Tufts University, Medford, Massachusetts.
Nikhil U NairDepartment of Chemical and Biological Engineering, Tufts University, Medford, Massachusetts.ORCID 0000-0001-7737-1385
Soha HassounDepartment of Computer Science, Tufts University, Medford, Massachusetts.ORCID 0000-0001-9477-2199
Tufts University · US

Funding

Metabolic engineering in humans: Altered gut microbes as a therapeutic platformDP2HD091798 · NICHD · TUFTS UNIVERSITY MEDFORD · PI NAIR, NIKHIL UNNI · 2016 to 2016
$2.3M
NICHD NIH HHS DP2 HD091798
6 · The paper itself

Abstract

Current pathway synthesis tools identify possible pathways that can be added to a host to produce the desired target molecule through the exploration of abstract metabolic and reaction network space. However, not many of these tools explore gene-level information required to physically realize the identified synthesis pathways, and none explore enzyme-host compatibility. Developing tools that address this disconnect between abstract reactions/metabolic design space and physical genetic sequence design space will enable expedited experimental efforts that avoid exploring unprofitable synthesis pathways. This work describes a workflow, termed Probabilistic Pathway Assembly with Solubility Confidence Scores (ProPASS), which links synthesis pathway construction with the exploration of the physical design space as imposed by the availability of enzymes with predicted characterized activities within the host. Predicted protein solubility propensity scores are used as a confidence level to quantify the compatibility of each pathway enzyme with the host Escherichia coli (E. coli). This study also presents a database, termed Protein Solubility Database (ProSol DB), which provides solubility confidence scores in E. coli for 240,016 characterized enzymes obtained from UniProtKB/Swiss-Prot. The utility of ProPASS is demonstrated by generating genetic implementations of heterologous synthesis pathways in E. coli that target several commercially useful biomolecules.

Indexed as

Biosynthetic PathwaysBiocatalysisEscherichia coliEscherichia coli ProteinsIndustrial MicrobiologyMetabolic EngineeringSolubilityWorkflowEscherichia coli Proteinsmetabolic engineeringpathway designpathway implementationsolubilitysynthesis pathwaysynthetic biology

Identifiers

PMID30802311
PMCPMC6494684
OpenAlexW2952678103

What OpenQuestion holds

Textmetadata
LicenceTDM
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.