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Your search keyword '"Kahvejian, Avak"' showing total 18 results
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18 results on '"Kahvejian, Avak"'

3. Global genome analysis reveals a vast and dynamic anellovirus landscape within the human virome

Author

Arze, Cesar A., primary, Springer, Simeon, additional, Dudas, Gytis, additional, Patel, Sneha, additional, Bhattacharyya, Agamoni, additional, Swaminathan, Harish, additional, Brugnara, Carlo, additional, Delagrave, Simon, additional, Ong, Tuyen, additional, Kahvejian, Avak, additional, Echelard, Yann, additional, Weinstein, Erica G., additional, Hajjar, Roger J., additional, Andersen, Kristian G., additional, and Yozwiak, Nathan L., additional

Published
2021
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4. UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant

Author

Tsung-Cheng Chang, Yamashita, Akio, Chyi-Ying A. Chen, Yamashita, Yukiko, and Wenmiao Zhu; Durdan, Simon; Kahvejian, Avak; Sonenberg, Nahum; Shyu, Ann-Bin

Subjects
Messenger RNA -- Research, Mammals -- Genetic aspects, Cytoplasm -- Research, Biological sciences
Abstract

The different classes of mammalian poly(A) nucleases are tested. A new insight into a mechanism is provided by which interplay between mRNA turnover and translation determines the lifespan of a mCRD-containing mRNA in the cytoplasm.

Published
2004

7. Single-molecule sequencing advances

Author

Kahvejian, Avak

Subjects
Nucleotide sequencing -- Innovations, Nucleotide sequencing -- Methods, Human genome -- Observations, Biotechnology industry -- Product information, Biotechnology industry, Business
Abstract

The Helicos Genetic Analysis System, developed by Helicos Biosciences Corp., uses True Single Molecule Sequencing (tSMS) that allows researchers to acquire data from individual DNA molecules and does not require amplification. Other details of the tSMS process are discussed.

Published
2008

8. Single-step capture and sequencing of natural DNA for detection of BRCA1 mutations

Author

Thompson, John F., primary, Reifenberger, Jeffrey G., additional, Giladi, Eldar, additional, Kerouac, Kristen, additional, Gill, Jaime, additional, Hansen, Erik, additional, Kahvejian, Avak, additional, Kapranov, Philipp, additional, Knope, Travis, additional, Lipson, Doron, additional, Steinmann, Kathleen E., additional, and Milos, Patrice M., additional

Published
2011
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14. Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase

Author

Kozlov, Guennadi, primary, De Crescenzo, Gregory, additional, Lim, Nadia S, additional, Siddiqui, Nadeem, additional, Fantus, Daniel, additional, Kahvejian, Avak, additional, Trempe, Jean-François, additional, Elias, Demetra, additional, Ekiel, Irena, additional, Sonenberg, Nahum, additional, O'Connor-McCourt, Maureen, additional, and Gehring, Kalle, additional

Published
2003
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17. Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase.

Author

Kozlov, Guennadi, De Crescenzo, Gregory, Lim, Nadia S., Siddiqui, Nadeem, Fantus, Daniel, Kahvejian, Avak, Trempe, Jean-François, Elias, Demetra, Ekiel, Irena, Sonenberg, Nahum, O'Connor-McCourt, Maureen, and Gehring, Kalle

Subjects
LIGANDS (Biochemistry), UBIQUITIN, LIGASES, ENZYMES, PROTEINS, BIOCHEMISTRY
Abstract

The C-terminal domain of poly(A)-binding protein (PABC) is a peptide-binding domain found in poly(A)-binding proteins (PABPs) and a HECT (homologous to E6-AP Cterminus) family E3 ubiquitin ligase. In protein synthesis, the PABC domain of PABP functions to recruit several translation factors possessing the PABP-interacting motif 2 (PAM2) to the mRNA poly(A) tail. We have determined the solution structure of the human PABC domain in complex with two peptides from PABP-interacting protein-1 (Paip1) and Paip2. The structures show a novel mode of peptide recognition, in which the peptide binds as a pair of β-turns with extensive hydrophobic, electrostatic and aromatic stacking interactions. Mutagenesis of PABC and peptide residues was used to identify key protein-peptide interactions and quantified by isothermal calorimetry, surface plasmon resonance and GST pulldown assays. The results provide insight into the specificity of PABC in mediating PABP-protein interactions. [ABSTRACT FROM AUTHOR]

Published
2004
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18. Single-step capture and sequencing of natural DNA for detection of BRCA1 mutations.

Author

Thompson, John F., Reifenberger, Jeffrey G., Giladi, Eldar, Kerouac, Kristen, Gill, Jaime, Hansen, Erik, Kahvejian, Avak, Kapranov, Philipp, Knope, Travis, Lipson, Doron, and Milos, Kathleen E. Steinmann and Patrice M.

Subjects
*GENETICS, *DISEASE risk factors, *MEDICAL care, *DNA, *GENOMICS, *NUCLEOTIDE sequence
Abstract

Genetic testing for disease risk is an increasingly important component of medical care. However, testing can be expensive, which can lead to patients and physicians having limited access to the genetic information needed for medical decisions. To simplify DNA sample preparation and lower costs, we have developed a system in which any gene can be captured and sequenced directly from human genomic DNA without amplification, using no proteins or enzymes prior to sequencing. Extracted whole-genome DNA is acoustically sheared and loaded in a flow cell channel for single-molecule sequencing. Gene isolation, amplification, or ligation is not necessary. Accurate and low-cost detection of DNA sequence variants is demonstrated for the BRCA1 gene. Disease-causing mutations as well as common variants from well-characterized samples are identified. Single-molecule sequencing generates very reproducible coverage patterns, and these can be used to detect any size insertion or deletion directly, unlike PCR-based methods, which require additional assays. Because no gene isolation or amplification is required for sequencing, the exceptionally low costs of sample preparation and analysis could make genetic tests more accessible to those who wish to know their own disease susceptibility. Additionally, this approach has applications for sequencing integration sites for gene therapy vectors, transposons, retroviruses, and other mobile DNA elements in a more facile manner than possible with other methods. [ABSTRACT FROM AUTHOR]

Published
2012
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