Evidence map›Paper›PMID 24506795›Full record

ReviewBiochemistry2014

Designing hydrolytic zinc metalloenzymes.

Melissa L Zastrow, Vincent L Pecoraro

Open access · bronzeAbstract readReview
In one paragraph

Review in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 1 pooled it
7.9field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 1 synthesis or guideline pooled it, 173 citations in OpenAlex.

  1. Evaluation of nutrients in bread: a systematic review.Journal of health, population, and nutrition · 2022
    Pooled it
  2. Review
  3. Dioxazolium desferrioxamine as a cell permeant chelator of intracellular labile iron.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  4. Catalytic pBiochemistry · 2026
    Article
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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

2 authors at 1 institution in 1 country.

Melissa L ZastrowDepartment of Chemistry, University of Michigan , Ann Arbor, Michigan 48109, United States.
Vincent L Pecoraro
University of Michigan–Ann Arbor · US

Funding

MICHIGAN CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008597 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MONTGOMERY, JOHN · 1996 to 2018
$5.0M
Toxic Metal Complexation By de Novo Designed PeptidesR01ES012236 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PECORARO, VINCENT L · 2003 to 2018
$4.4M
NIEHS NIH HHS ES012236NIEHS NIH HHS R01 ES012236NIGMS NIH HHS T32 GM008597
6 · The paper itself

Abstract

Zinc is an essential element required for the function of more than 300 enzymes spanning all classes. Despite years of dedicated study, questions regarding the connections between primary and secondary metal ligands and protein structure and function remain unanswered, despite numerous mechanistic, structural, biochemical, and synthetic model studies. Protein design is a powerful strategy for reproducing native metal sites that may be applied to answering some of these questions and subsequently generating novel zinc enzymes. From examination of the earliest design studies introducing simple Zn(II)-binding sites into de novo and natural protein scaffolds to current studies involving the preparation of efficient hydrolytic zinc sites, it is increasingly likely that protein design will achieve reaction rates previously thought possible only for native enzymes. This Current Topic will review the design and redesign of Zn(II)-binding sites in de novo-designed proteins and native protein scaffolds toward the preparation of catalytic hydrolytic sites. After discussing the preparation of Zn(II)-binding sites in various scaffolds, we will describe relevant examples for reengineering existing zinc sites to generate new or altered catalytic activities. Then, we will describe our work on the preparation of a de novo-designed hydrolytic zinc site in detail and present comparisons to related designed zinc sites. Collectively, these studies demonstrate the significant progress being made toward building zinc metalloenzymes from the bottom up.

Indexed as

Catalytic DomainBinding SitesCarbonic AnhydrasesCatalysisCrystallography, X-RayCysteineGlutamic AcidHistidineHydrolysisMetalloproteinsModels, MolecularProtein BindingProtein EngineeringProtein Structure, SecondaryZincZinc FingersCarbonic AnhydrasesCysteineGlutamic AcidHistidineMetalloproteinsZinc

Identifiers

PMID24506795
PMCPMC3985962
OpenAlexW2333550456

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.