A5088629060- RNA and protein synthesis mechanisms
- DNA and Nucleic Acid Chemistry
- Chemical Synthesis and Analysis
- Metabolism and Genetic Disorders
- Metal complexes synthesis and properties
- Health and Medical Research Impacts
- Metalloenzymes and iron-sulfur proteins
- Amino Acid Enzymes and Metabolism
- Mass Spectrometry Techniques and Applications
- RNA Research and Splicing
- Enzyme Catalysis and Immobilization
- Genomics and Chromatin Dynamics
- Enzyme Structure and Function
- Microbial Metabolic Engineering and Bioproduction
- Magnetism in coordination complexes
- Protein Structure and Dynamics
- Advanced biosensing and bioanalysis techniques
- Biotin and Related Studies
- Polyoxometalates: Synthesis and Applications
- RNA modifications and cancer
- scientometrics and bibliometrics research
- Mitochondrial Function and Pathology
- Glycosylation and Glycoproteins Research
- CRISPR and Genetic Engineering
- Diet and metabolism studies
University of Pittsburgh
2014-2025
Beth Israel Deaconess Medical Center
2025
Harvard University
1984-2025
Magee-Womens Hospital
2021-2024
Johns Hopkins Medicine
1996-2022
Johns Hopkins University
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University of Pittsburgh Medical Center
2015-2021
NYU Langone Health
2021
Council of Science Editors
2016-2019
University of Saskatchewan
2019
Zinc ions are key structural components of a large number proteins. The binding zinc stabilizes the folded conformations domains so that they may facilitate interactions between proteins and other macromolecules such as DNA. modular nature some these zinc-containing has allowed rational design site-specific DNA ability to be bound specifically within range tetrahedral sites appears responsible for evolution wide zinc-stabilized now known exist. lack redox activity ion its exchange kinetics...
An Overview of Bioinorganic Chemistry Principles Coordination Related to Research Properties Biological Molecules Physical Methods in Choice and Assembly Metal Ions Biology Control Utilization Ion Concentrations Cells Folding Crosslinking Biomolecules Binding Biomolecule Active Centres Electron Transfer Proteins Substrate Activation Atom Group Protein Turning Achieve Specific Functions Frontiers Chemistry.
A systematic search for sequences that potentially could form metal-binding domains in proteins has been performed. Five classes of involved nucleic acid binding or gene regulation were found to contain such sequences. These observations suggest numerous experiments aimed at determining whether are present these and, if present, what roles play the processes and regulation.
Several proteins, including the gene regulatory protein transcription factor IIIA, have been shown to contain tandem repeats of sequences approximately equal 30 amino acids that are believed form structural domains around bound zinc ions ("zinc fingers"). The consensus sequence for these is (Phe, Tyr)-Xaa-Cys-(Xaa)2 or 4-Cys-(Xaa)3-Phe-(Xaa)5-Leu-(Xaa)2-His-(Xaa)3-His- (Xaa)5, where Xaa any acid. Comparisons with metalloproteins known structures allowed development a detailed...
The time is right for biologists to post their research findings onto preprint servers
A 30-amino acid peptide, which corresponds to the second "zinc finger" domain of transcription factor IIIA, has been synthesized and purified. This peptide folds in presence zinc: adding Zn2+ significantly changes circular dichroism spectrum, protects from tryptic digestion. The also binds Co2+, absorption spectrum Co2+ complex suggests that a tetrahedral binding site is formed by two cysteines histidines. Experiments at higher temperatures (60-75 degrees C) suggest these folded...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTA consensus zinc finger peptide: design, high-affinity metal binding, a pH-dependent structure, and His to Cys sequence variantBeth Allyn Krizek, Barbara T. Amann, Valda J. Kilfoil, Denise L. Merkle, Jeremy M. BergCite this: Am. Chem. Soc. 1991, 113, 12, 4518–4523Publication Date (Print):June 1, 1991Publication History Published online1 May 2002Published inissue 1 June 1991https://doi.org/10.1021/ja00012a021RIGHTS & PERMISSIONSArticle...
We have designed three zinc-finger proteins with different DNA binding specificities. The design strategy combines a consensus framework sequence previously characterized recognition regions such that the specificity of each protein is predictable. first consists identical zinc fingers, which was expected to recognize subsite GCG. This binds specifically 5'-GCG-GCG-GCG-3' dissociation constant approximately 11 microM. second has fingers predicted preferred subsites. site 5'-GGG-GCG-GCT-3' 2...
Zinc finger proteins of the Cys2-His2 type consist tandem arrays domains, where each domain appears to contact three adjacent base pairs DNA through key residues. We have designed and prepared a series variants central zinc within binding Sp1 by using information from an analysis large data protein sequences. Through systematic variations at two positions (underlined), relatively specific recognition sequences form 5'-GGGGN(G or T)GGG-3' has been achieved. These results provide basis for...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTLigand variation and metal ion binding specificity in zinc finger peptidesBeth Allyn Krizek, Denise L. Merkle, Jeremy M. BergCite this: Inorg. Chem. 1993, 32, 6, 937–940Publication Date (Print):March 1, 1993Publication History Published online1 May 2002Published inissue 1 March 1993https://pubs.acs.org/doi/10.1021/ic00058a030https://doi.org/10.1021/ic00058a030research-articleACS PublicationsRequest reuse permissionsArticle...
Because the mammalian bladder must store urine of composition which differs markedly from that plasma for prolonged periods, permeability barrier maintain extremely low permeabilities to substances normally cross membranes relatively rapidly, such as water, protons, and small nonelectrolytes like urea ammonia. In present studies, apical membrane dissected rabbit epithelium urea, ammonia, protons were measured in Ussing chambers averaged (in cm/s) 5.15 +/- 0.43 x 10(-5); 4.51 0.67 10(-6);...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTModel for the active site of oxo-transfer molybdoenzymes: synthesis, structure, and propertiesJeremy M. Berg R. H. HolmCite this: J. Am. Chem. Soc. 1985, 107, 4, 917–925Publication Date (Print):February 1, 1985Publication History Published online1 May 2002Published inissue 1 February 1985https://pubs.acs.org/doi/10.1021/ja00290a029https://doi.org/10.1021/ja00290a029research-articleACS PublicationsRequest reuse permissionsArticle...
The Cancer Genome Atlas Project (TCGA) is a National Institute effort to profile at least 500 cases of 20 different tumor types using genomic platforms and make these data, both raw processed, available all researchers. TCGA data are currently over 1.2 Petabyte in size include whole genome sequence (WGS), exome sequence, methylation, RNA expression, proteomic, clinical datasets. Publicly accessible released through public portals, but many challenges exist navigating obtained from sites. We...
A minimalist Cys2His2 zinc finger peptide, Lys-Tyr-Ala-Cys-Ala-Ala-Cys-Ala-Ala-Ala-Phe-Ala-Ala-Lys-Ala-Ala-Leu-Ala- Ala-His-Ala-Ala-Ala-His-Ala-Lys, has been synthesized. Metal binding studies using Co2+ as a probe indicated that this peptide forms 1:1 peptide/metal complex with dissociation constant comparable to observed for other peptides. At high concentrations, 2:1 also forms, four cysteinates coordinated Co2+. Additional sequence variants in which the canonical hydrophobic residues...