Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function.
about
Protein design: toward functional metalloenzymesMetal binding mediated conformational change of XPA protein:a potential cytotoxic mechanism of nickel in the nucleotide excision repairCleavage and polyadenylation specificity factor 30: An RNA-binding zinc-finger protein with an unexpected 2Fe-2S cluster.Switching metal ion coordination and DNA Recognition in a Tandem CCHHC-type zinc finger peptideCu(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).A role for hydrogen bonding in DNA recognition by the non-classical CCHHC type zinc finger, NZF-1.Design of a synthetic luminescent probe from a biomolecule binding domain: selective detection of AU-rich mRNA sequences.Characterization of Polyelectrolyte Complex Formation Between Anionic and Cationic Poly(amino acids) and Their Potential Applications in pH-Dependent Drug Delivery.Reactivity of a Zn(Cys)2(His)2 Zinc Finger with Singlet Oxygen: Oxidation Directed toward Cysteines but not Histidines.Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy.Peptide-based FeS4 complexes: the zinc ribbon fold is unsurpassed to stabilize both the FeII and FeIII states.
P2860
Q26866201-57EE552B-3828-460B-93EE-A9E015E63BA4Q36053638-CD98F5D2-15F2-4693-9EAE-FB928B02BA6FQ36866046-63EDBFB2-84B0-4451-B710-ED6C038DC7D8Q36899695-54D9EEAC-7541-4581-A65A-901B66C9E49DQ38756757-CD7A7634-A184-4639-8280-D072FAFE45DDQ39952442-AACB2BB2-1848-4984-ADCA-283B185F44F4Q40987387-2F0A4BC3-CE99-4714-9EF5-E1E0BDC44E63Q41995698-E254AE1E-B82F-405A-B89A-685AEA6DCBE1Q46341933-8AED2212-890B-4E66-BEBE-E37BD058040BQ46684962-F4BA58DD-9671-4358-93D6-12FB10BB5371Q48130098-BB877525-74D6-41FD-BCBF-AFC17A0CDC3FQ53635440-069E6797-67EE-4B68-B1FC-B058E2295E7D
P2860
Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function.
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին 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
Cysteine and histidine shuffli ...... different folds and function.
@ast
Cysteine and histidine shuffli ...... different folds and function.
@en
type
label
Cysteine and histidine shuffli ...... different folds and function.
@ast
Cysteine and histidine shuffli ...... different folds and function.
@en
prefLabel
Cysteine and histidine shuffli ...... different folds and function.
@ast
Cysteine and histidine shuffli ...... different folds and function.
@en
P2093
P2860
P356
P1433
P1476
Cysteine and histidine shuffli ...... different folds and function.
@en
P2093
Angelique N Besold
Jamie L Michalek
Sarah L J Michel
P2860
P304
12619-12632
P356
10.1039/C1DT11071C
P407
P577
2011-09-26T00:00:00Z