Evidence map›Paper›PMID 10545346›Full record

ArticleBiophysical journal1999

A modular treatment of molecular traffic through the active site of cholinesterase.

S A Botti, C E Felder, S Lifson, J L Sussman, I Silman

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

11 citing papers in PubMed, 59 citations in OpenAlex.

  1. Forebrain Cholinergic Signaling: Wired and Phasic, Not Tonic, and Causing Behavior.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Review
  2. Resurrection and Reactivation of Acetylcholinesterase and Butyrylcholinesterase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019
    Review
  3. Guided Evolution of RecombinantInternational journal of molecular sciences · 2018
    Article
  4. Article
  5. Article
  6. Article
  7. Acetylcholinesterase: from 3D structure to function.Chemico-biological interactions · 2010
    Article
  8. Article
  9. Article
  10. Article
  11. Review
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

5 authors at 1 institution in 1 country.

S A BottiDepartment of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel. simone.botti@weizmann.ac.il
C E Felder
S Lifson
J L Sussman
I Silman
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present a model for the molecular traffic of ligands, substrates, and products through the active site of cholinesterases (ChEs). First, we describe a common treatment of the diffusion to a buried active site of cationic and neutral species. We then explain the specificity of ChEs for cationic ligands and substrates by introducing two additional components to this common treatment. The first module is a surface trap for cationic species at the entrance to the active-site gorge that operates through local, short-range electrostatic interactions and is independent of ionic strength. The second module is an ionic-strength-dependent steering mechanism generated by long-range electrostatic interactions arising from the overall distribution of charges in ChEs. Our calculations show that diffusion of charged ligands relative to neutral isosteric analogs is enhanced approximately 10-fold by the surface trap, while electrostatic steering contributes only a 1.5- to 2-fold rate enhancement at physiological salt concentration. We model clearance of cationic products from the active-site gorge as analogous to the escape of a particle from a one-dimensional well in the presence of a linear electrostatic potential. We evaluate the potential inside the gorge and provide evidence that while contributing to the steering of cationic species toward the active site, it does not appreciably retard their clearance. This optimal fine-tuning of global and local electrostatic interactions endows ChEs with maximum catalytic efficiency and specificity for a positively charged substrate, while at the same time not hindering clearance of the positively charged products.

Indexed as

Catalytic DomainModels, BiologicalAnimalsBiocatalysisBiological TransportCholinesterasesDiffusionHumansLigandsModels, MolecularStatic ElectricitySubstrate SpecificityThermodynamicsCholinesterasesLigands

Identifiers

PMID10545346
PMCPMC1300520
OpenAlexW1996152843

What OpenQuestion holds

Textmetadata
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.