"Zinc Fingers" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Motifs in DNA- and RNA-binding proteins whose amino acids are folded into a single structural unit around a zinc atom. In the classic zinc finger, one zinc atom is bound to two cysteines and two histidines. In between the cysteines and histidines are 12 residues which form a DNA binding fingertip. By variations in the composition of the sequences in the fingertip and the number and spacing of tandem repeats of the motif, zinc fingers can form a large number of different sequence specific binding sites.
Descriptor ID |
D016335
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MeSH Number(s) |
G02.111.570.820.709.275.500.985
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Concept/Terms |
Zinc Fingers- Zinc Fingers
- Finger, Zinc
- Fingers, Zinc
- Zinc Finger
- Zinc Finger Motifs
- Motif, Zinc Finger
- Motifs, Zinc Finger
- Zinc Finger Motif
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Below are MeSH descriptors whose meaning is more general than "Zinc Fingers".
Below are MeSH descriptors whose meaning is more specific than "Zinc Fingers".
This graph shows the total number of publications written about "Zinc Fingers" by people in this website by year, and whether "Zinc Fingers" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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1999 | 1 | 0 | 1 |
2000 | 1 | 0 | 1 |
2004 | 0 | 1 | 1 |
2016 | 0 | 1 | 1 |
2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Zinc Fingers" by people in Profiles.
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The zinc fingers and homeoboxes 2 protein ZHX2 and its interacting proteins regulate upstream pathways in podocyte diseases. Kidney Int. 2020 04; 97(4):753-764.
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Relation of genomic variants for Alzheimer disease dementia to common neuropathologies. Neurology. 2016 Aug 02; 87(5):489-96.
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Arsenic trioxide and thalidomide combination produces multi-lineage hematological responses in myelodysplastic syndromes patients, particularly in those with high pre-therapy EVI1 expression. Leuk Res. 2004 Aug; 28(8):791-803.
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The MDM2 RING-finger domain is required to promote p53 nuclear export. Nat Cell Biol. 2000 Sep; 2(9):569-73.
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Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2. J Biol Chem. 1999 Jun 04; 274(23):16531-5.