Evidence map›Paper›PMID 26465508›Full record

ArticlePhysical review. E, Statistical, nonlinear, and soft matter physics2015

Random-walk enzymes.

Chi H Mak, Phuong Pham, Samir A Afif, Myron F Goodman

Open access · greenAbstract readComparative Study
In one paragraph

Article in Physical review. E, Statistical, nonlinear, and soft matter physics, 2015. 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
0.8field-weighted citation impact, top 27% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. The role of HIRA-dependent H3.3 deposition and its modifications in the somatic hypermutation of immunoglobulin variable regions.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Review
  5. Better living with hyper-mutation.Environmental and molecular mutagenesis · 2016
    Review
  6. Article
  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

4 authors at 1 institution in 1 country.

Chi H MakDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, USA.
Phuong PhamDepartment of Biological Sciences, University of Southern California, Los Angeles, California 90089, USA.
Samir A AfifDepartment of Biological Sciences, University of Southern California, Los Angeles, California 90089, USA.
Myron F GoodmanDepartment of Chemistry, University of Southern California, Los Angeles, California 90089, USA.
University of Southern California · US

Funding

Biochemical Basis of Somatic HypermutationR01ES013192 · NIEHS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2004 to 2013
$3.7M
ERROR CORRECTION IN DNA SYNTHESIS--A BIOCHEMICAL STUDYR37GM021422 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2000 to 2009
$3.5M
ERROR CORRECTION IN DNA SYNTHESIS: A BIOCHEMICAL STUDYR01GM021422 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 1985 to 2014
$1.6M
Biochemical Basis of Somatic HypermutationR56ES013192 · NIEHS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2015 to 2015
$150k
NIEHS NIH HHS ES13192NIEHS NIH HHS R01 ES013192NIEHS NIH HHS R56 ES013192NIGMS NIH HHS GM21422NIGMS NIH HHS R01 GM021422NIGMS NIH HHS R37 GM021422
6 · The paper itself

Abstract

Enzymes that rely on random walk to search for substrate targets in a heterogeneously dispersed medium can leave behind complex spatial profiles of their catalyzed conversions. The catalytic signatures of these random-walk enzymes are the result of two coupled stochastic processes: scanning and catalysis. Here we develop analytical models to understand the conversion profiles produced by these enzymes, comparing an intrusive model, in which scanning and catalysis are tightly coupled, against a loosely coupled passive model. Diagrammatic theory and path-integral solutions of these models revealed clearly distinct predictions. Comparison to experimental data from catalyzed deaminations deposited on single-stranded DNA by the enzyme activation-induced deoxycytidine deaminase (AID) demonstrates that catalysis and diffusion are strongly intertwined, where the chemical conversions give rise to new stochastic trajectories that were absent if the substrate DNA was homogeneous. The C→U deamination profiles in both analytical predictions and experiments exhibit a strong contextual dependence, where the conversion rate of each target site is strongly contingent on the identities of other surrounding targets, with the intrusive model showing an excellent fit to the data. These methods can be applied to deduce sequence-dependent catalytic signatures of other DNA modification enzymes, with potential applications to cancer, gene regulation, and epigenetics.

Indexed as

EnzymesModels, MolecularCatalysisComputer SimulationDiffusionDNAKineticsMonte Carlo MethodMutationStochastic ProcessesDNAEnzymes

Identifiers

PMID26465508
PMCPMC4672870
OpenAlexW2413239430

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.