Minimal functional sites allow a classification of zinc sites in proteins.
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Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1Zinc as Allosteric Ion Channel Modulator: Ionotropic Receptors as MetalloproteinsMinimal Functional Sites in Metalloproteins and Their Usage in Structural BioinformaticsMechanisms of glutamate transportDeubiquitinase function of arterivirus papain-like protease 2 suppresses the innate immune response in infected host cellsStructural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active sitePeroxiredoxin chaperone activity is critical for protein homeostasis in zinc-deficient yeast.Designing hydrolytic zinc metalloenzymesIdentifying proteins that can form tyrosine-cysteine crosslinks.Characterization of the Zn(II) binding properties of the human Wilms' tumor suppressor protein C-terminal zinc finger peptideFindGeo: a tool for determining metal coordination geometry.Structure and mechanism of Zn2+-transporting P-type ATPases.Cooperative functions of ZnT1, metallothionein and ZnT4 in the cytoplasm are required for full activation of TNAP in the early secretory pathwayEffects of Zn fertilization on hordein transcripts at early developmental stage of barley grain and correlation with increased Zn concentration in the mature grain.Characterization of two Lactococcus lactis zinc membrane proteins, Llmg_0524 and Llmg_0526, and role of Llmg_0524 in cell wall integrityHigh potency zinc modulation of human P2X2 receptors and low potency zinc modulation of rat P2X2 receptors share a common molecular mechanismZinc biochemistry: from a single zinc enzyme to a key element of life.Switching metal ion coordination and DNA Recognition in a Tandem CCHHC-type zinc finger peptideCurrent understanding of ZIP and ZnT zinc transporters in human health and diseases.Relationship between the architecture of zinc coordination and zinc binding affinity in proteins--insights into zinc regulation.The mechanical role of metal ions in biogenic protein-based materials.The Physiological, Biochemical, and Molecular Roles of Zinc Transporters in Zinc Homeostasis and Metabolism.A rationally designed metal-binding helical peptoid for selective recognition processesCu(I) Disrupts the Structure and Function of the Nonclassical Zinc Finger Protein Tristetraprolin (TTP).Revisiting and re-engineering the classical zinc finger peptide: consensus peptide-1 (CP-1).Reactive cysteine in the structural Zn(2+) site of the C1B domain from PKCα.A role for hydrogen bonding in DNA recognition by the non-classical CCHHC type zinc finger, NZF-1.mFASD: a structure-based algorithm for discriminating different types of metal-binding sites.MetalPDB: a database of metal sites in biological macromolecular structures.Hidden relationships between metalloproteins unveiled by structural comparison of their metal sites.On the design of zinc-finger models with cyclic peptides bearing a linear tail.MetalS(3), a database-mining tool for the identification of structurally similar metal sites.Coordination complexes of 4-methylimidazole with ZnII and CuII in gas phase and in water: a DFT study.Reactivity of a Zn(Cys)2(His)2 Zinc Finger with Singlet Oxygen: Oxidation Directed toward Cysteines but not Histidines.MetalPDB in 2018: a database of metal sites in biological macromolecular structures.To what extent do structural changes in catalytic metal sites affect enzyme function?Differential Effects of Iron, Zinc, and Copper on Dictyostelium discoideum Cell Growth and Resistance to Legionella pneumophila.Heteroleptic complexes via solubility control: examples of Cu(ii), Co(ii), Ni(ii) and Mn(ii) complexes based on the derivatives of terpyridine and hydroxyquinoline.Zinc Protects Oxidative Stress-Induced RPE Death by Reducing Mitochondrial Damage and Preventing Lysosome Rupture.Enrichment and Identification of the Most Abundant Zinc Binding Proteins in Developing Barley Grains by Zinc-IMAC Capture and Nano LC-MS/MS.
P2860
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P2860
Minimal functional sites allow a classification of zinc sites in proteins.
description
2011 nî lūn-bûn
@nan
2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Minimal functional sites allow a classification of zinc sites in proteins.
@ast
Minimal functional sites allow a classification of zinc sites in proteins.
@en
type
label
Minimal functional sites allow a classification of zinc sites in proteins.
@ast
Minimal functional sites allow a classification of zinc sites in proteins.
@en
prefLabel
Minimal functional sites allow a classification of zinc sites in proteins.
@ast
Minimal functional sites allow a classification of zinc sites in proteins.
@en
P2860
P1433
P1476
Minimal functional sites allow a classification of zinc sites in proteins.
@en
P2093
Gabriele Cavallaro
P2860
P304
P356
10.1371/JOURNAL.PONE.0026325
P407
P577
2011-10-17T00:00:00Z