231 Citations
The protein architecture in Bacteria and Archaea identifies a set of promiscuous and ancient domains
- BiologyPloS one
- 2019
It is considered that the association between these two classes of protein domains (promiscuous and non- Promiscuous) provides bacterial and archaeal cells with the ability to respond to diverse environmental challenges.
The transcription factor FOXM1 (Forkhead box M1): proliferation-specific expression, transcription factor function, target genes, mouse models, and normal biological roles.
- BiologyAdvances in cancer research
- 2013
DNA Binding Specificity of Mu Transcription Factor C and Crystallization of C : DNA Complex
- Biology
- 2007
To understand the binding specificity of C and determine a possible consensus sequence for C binding, and to crystallize the C : DNA complex as a first step towards structure determination, this study tested additional candidate mutations within and flanking the C binding sequence.
Characterization of the S. cerevisiae Rap1 DNA binding domain and biochemical analysis of its interactions with telomeric and silencer DNA
- Biology, Chemistry
- 2000
In vivo studies of Rapl binding showed that Rapl binds with higher affinity to telomeric than to silencer sites, which suggested that HTH1 and HTH2 bind D N A in a cooperative manner: the affinity of one subdomain is enhanced when the second sub domain is bound to DNA.
Oncogenic mutations in the DNA-binding domain of FOXO1 disrupt folding: quantitative insights from experiments and molecular simulations
- BiologybioRxiv
- 2022
The results suggest that atomic detail provided from simulation is important for accurate prediction of mutational effects on folding stability, and a simple hydrophobic transfer model, combined with estimates of unfolded-state solvent accessible surface areas from molecular simulation, is able to more accurately predict changes in folding free energies due to mutations.
FOXA1: A Pioneer of Nuclear Receptor Action in Breast Cancer
- BiologyCancers
- 2021
This review discusses the current literature on how FOXA1 controls gene activity, cell biology, and the response of breast cancers to hormone therapies and offers areas of future study to identify roles ofFOXA1 in controlling breast cancers that is independent of its regulation of nuclear receptors.
In silico Drug Target Discovery Through Proteome Mining from M. tuberculosis: An Insight towards Antivirulent Therapy.
- Biology, MedicineCombinatorial chemistry & high throughput screening
- 2020
The study successfully assigned functions of 83 essential hypothetical proteins of Mycobacterium tuberculosis, among which 25 were identified as virulence factors, which has the potential to bring revolutionary treatment over conventional antibiotics to overcome the lethality of antibiotic-resistant strains.
Spatiotemporal Regulation of Vibrio Exotoxins by HlyU and Other Transcriptional Regulators
- BiologyToxins
- 2020
This review covers three major exotoxins in pathogenic Vibrio species and their transcriptional regulation systems and discusses anti-virulence strategies that target the coordinating master regulator HlyU.
References
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Co-crystal structure of the HNF-3/fork head DNA-recognition motif resembles histone H5
- ChemistryNature
- 1993
The three-dimensional structure of an HNF-3/fork head DNA-recognition motif complexed with DNA has been determined by X-ray crystallography at 2.5 Å resolution and the transcription factor fold is very similar to the structure of histone H5.
Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
- Chemistry, BiologyNature
- 1993
The structure of GH5, the globular domain of the linker histone H5, has been solved to 2.5 Å resolution by multiwavelength anomalous diffraction on crystals of the selenomethionyl protein, thereby providing a possible model for the binding ofGH5 to DNA.
Solution structure of the POU-specific DNA-binding domain of Oct-1
- ChemistryNature
- 1993
The observed selective exchange broadening in the (15N, 1H)-HMQC (heteronuclear multiple quantum coherence) spectrum of the POUs–DNA complex is concluded that DNA-binding is mediated by helix III.
The X-ray structure of an atypical homeodomain present in the rat liver transcription factor LFB1/HNF1 and implications for DNA binding.
- Biology, Chemistry
- 1993
Comparison with the engrailed homeodomain-DNA complex indicates that the mode of interaction with DNA is similar in both proteins, with a number of conserved contacts in the major groove.
The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage λ repressor DNA-binding domain
- BiologyCell
- 1993
The three‐dimensional NMR‐solution structure of the polypeptide fragment 195–286 of the LFB1/HNF1 transcription factor from rat liver comprises a nonclassical homeodomain.
- Biology, ChemistryThe EMBO journal
- 1993
The three‐dimensional backbone fold of a polypeptide fragment from the rat LFB1/HNF1 transcription factor was determined by nuclear magnetic resonance (NMR) spectroscopy in solution and confirms a recently advanced hypothesis based on sequence comparisons that this polyPEptide segment of LFB 1/H NF1 might represent a homeodomain‐like structural element.
Transcription factors: structural families and principles of DNA recognition.
- BiologyAnnual review of biochemistry
- 1992
Familiarity, ease of access, trust, and awareness of benefits and risks to minimize uncertainty, will all be important for the sustained support of existing and new generations of DNA-B isolaters.