ReviewProgress in nuclear magnetic resonance spectroscopy
Zinc finger structure determination by NMR: Why zinc fingers can be a handful.
Review in Progress in nuclear magnetic resonance spectroscopy. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed.
- Genome-wide identification and expression analysis of RBR-type ubiquitin ligase family genes reveal the role of ZmIBR10 in maize disease resistance.BMC plant biology · 2026Article
- RNA Binding Mechanism of the FUS Zinc Finger in Concert with Its Flanking Intrinsically Disordered Region.Journal of chemical information and modeling · 2025Article
- Is dolichol pathway dysfunction a significant factor in Alzheimer's disease?Inflammopharmacology · 2025Review
- Zinc-Induced Folding and Solution Structure of the Eponymous Novel Zinc Finger from the ZC4H2 Protein.Biomolecules · 2025Article
- "Disguise strategy" to bacteria: A multifunctional hydrogel with bacteria-targeting and photothermal conversion properties for the repair of infectious bone defects.Bioactive materials · 2025Article
- Zinc inhibits the voltage-gated proton channel HCNL1.Biophysical journal · 2024Article
- Structural insights into the DNA-binding mechanism of BCL11A: The integral role of ZnF6.Structure (London, England : 1993) · 2024Article
- Structural basis for regulation of a CBASS-CRISPR-Cas defense island by a transmembrane anti-σ factor and its ECF σ partner.Science advances · 2024Article
- Putative retina metal/metalloid-binding proteins: molecular functions, biological processes and retina disease associations.Metallomics : integrated biometal science · 2024Article
- Structure and RNA-binding of the helically extended Roquin CCCH-type zinc finger.Nucleic acids research · 2024Article
- Formerly degenerate seventh zinc finger domain from transcription factor ZNF711 rehabilitated by experimental NMR structure.Protein science : a publication of the Protein Society · 2024Article
- Updated understanding of the protein-DNA recognition code used by C2H2 zinc finger proteins.Current opinion in structural biology · 2024Review
- A molecular switch controls assembly of bacterial focal adhesions.Science advances · 2024Article
- Zinc Deficiency as a General Feature of Cancer: a Review of the Literature.Biological trace element research · 2024Review
- Mode of SUV420H2 heterochromatin localization through multiple HP1 binding motifs in the heterochromatic targeting module.Genes to cells : devoted to molecular & cellular mechanisms · 2024Article
- Formerly degenerate seventh zinc finger domain from transcription factor ZNF711 rehabilitated by experimental NMR structure.bioRxiv : the preprint server for biology · 2024Article
- NMR structure verifies the eponymous zinc finger domain of transcription factor ZNF750.Journal of structural biology: X · 2023Article
- Zinc Uptake by HIV-1 Viral Particles: An Isotopic Study.International journal of molecular sciences · 2023Article
- Predicted Membrane-Associated Domains in Proteins Encoded by Novel Monopartite Plant RNA Viruses Related to Members of the FamilyInternational journal of molecular sciences · 2023Article
- Zinc in Prostate Health and Disease: A Mini Review.Biomedicines · 2022Review
Corrections and comments
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Authors and funding
1 author.
Funding
Abstract
Zinc fingers can be loosely defined as protein domains containing one or more tetrahedrally-co-ordinated zinc ions whose role is to stabilise the structure rather than to be involved in enzymatic chemistry; such zinc ions are often referred to as "structural zincs". Although structural zincs can occur in proteins of any size, they assume particular significance for very small protein domains, where they are often essential for maintaining a folded state. Such small structures, that sometimes have only marginal stability, can present particular difficulties in terms of sample preparation, handling and structure determination, and early on they gained a reputation for being resistant to crystallisation. As a result, NMR has played a more prominent role in structural studies of zinc finger proteins than it has for many other types of proteins. This review will present an overview of the particular issues that arise for structure determination of zinc fingers by NMR, and ways in which these may be addressed.
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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.