Výsledky vyhledávání - "Asli Ertekin"

A Disorder-to-Order Transition Mediates RNA Binding of the Caenorhabditis elegans Protein MEX-5

Autor: Francesca Massi, Asli Ertekin, Sean P. Ryder, Hila Schaal, Davide Tavella

Publikováno v: Biophys J

CCCH-type tandem zinc finger (TZF) domains are found in many RNA-binding proteins (RBPs) that regulate the essential processes of post-transcriptional gene expression and splicing through direct protein-RNA interactions. In Caenorhabditis elegans, RB

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a02d4fb91da2a961ace2a2b5bcebc1b
https://europepmc.org/articles/PMC7175634/

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Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples

Autor: Thomas Acton, Rong Xiao, Gaetano T. Montelione, David Baker, Paolo Rossi, James M. Aramini, Nikolaos G. Sgourakis, H. Lee, Asli Ertekin, Oliver F. Lange, Yifan Song

Publikováno v: Proc. Natl. Acad. Sci. U.S.A. 109, 10873-10878 (2012)

We have developed an approach for determining NMR structures of proteins over 20 kDa that utilizes sparse distance restraints obtained using transverse relaxation optimized spectroscopy experiments on perdeuterated samples to guide RASREC Rosetta NMR

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::903ca46bd90b64251234835996f6b8ce
https://doi.org/10.1073/pnas.1203013109

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Human Cyclin-dependent Kinase 2-associated Protein 1 (CDK2AP1) Is Dimeric in Its Disulfide-reduced State, with Natively Disordered N-terminal Region

Autor: Gaetano T. Montelione, Rong Xiao, Melissa Maglaqui, Paul G. Leonard, Paolo Rossi, James H. Prestegard, James M. Aramini, Haleema Janjua, Asli Ertekin, H. Lee

Publikováno v: Journal of Biological Chemistry. 287:16541-16549

CDK2AP1 (cyclin-dependent kinase 2-associated protein 1), corresponding to the gene doc-1 (deleted in oral cancer 1), is a tumor suppressor protein. The doc-1 gene is absent or down-regulated in hamster oral cancer cells and in many other cancer cell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5caeb21360d91e9a900573ed08574785
https://doi.org/10.1074/jbc.m112.343863

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Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping

Autor: Greg Wylie, Xu Wang, Gaetano T. Montelione, Sonal Bansal, James H. Prestegard, Adam W. Barb, Megan A. Macnaughtan, H. Lee, Asli Ertekin

Publikováno v: Protein Science. 19:1673-1685

The traditional NMR-based method for determining oligomeric protein structure usually involves distinguishing and assigning intra- and intersubunit NOEs. This task becomes challenging when determining symmetric homo-dimer structures because NOE cross

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::54ad9f8edabb496c5b336bd64b9dadee
https://doi.org/10.1002/pro.447

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Structural Basis of O6-Alkylguanine Recognition by a Bacterial Alkyltransferase-like DNA Repair Protein

Autor: Ta Tsen Soong, Julie L. Tubbs, John K. Everett, Keith Hamilton, Melissa Maglaqui, Mei Jiang, Rong Xiao, Gaetano T. Montelione, Paolo Rossi, Burkhard Rost, James M. Aramini, Colleen Ciccosanti, Sreenivas Kanugula, Asli Ertekin, Anthony E. Pegg, John A. Tainer, Thomas Acton

Publikováno v: Journal of Biological Chemistry. 285:13736-13741

Alkyltransferase-like proteins (ATLs) are a novel class of DNA repair proteins related to O(6)-alkylguanine-DNA alkyltransferases (AGTs) that tightly bind alkylated DNA and shunt the damaged DNA into the nucleotide excision repair pathway. Here, we p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ab0e80fe20d8f3870097a22193cb046
https://doi.org/10.1074/jbc.m109.093591

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A microscale protein NMR sample screening pipeline

Autor: Keith Hamilton, Gaetano T. Montelione, G. V. T. Swapna, James M. Aramini, Clemens Anklin, Thomas Acton, Paolo Rossi, Yuanpeng J. Huang, Asli Ertekin, K. Conover, John K. Everett, Rong Xiao

Publikováno v: Journal of Biomolecular Nmr

As part of efforts to develop improved methods for NMR protein sample preparation and structure determination, the Northeast Structural Genomics Consortium (NESG) has implemented an NMR screening pipeline for protein target selection, construct optim

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e537082dc660a1267de9ff1223aa60ad
https://doi.org/10.1007/s10858-009-9386-z

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Construct optimization for protein NMR structure analysis using amide hydrogen/deuterium exchange mass spectrometry

Autor: Li Zhao, Haiyan Zheng, James M. Aramini, Gaetano T. Montelione, Roberto Tejero, Yuanpeng J. Huang, Thomas Acton, Yoshitomo Hamuro, Seema Sharma, Mei Jiang, Asli Ertekin, G. V. T. Swapna, Rong Xiao, Paolo Rossi, Li Chung Ma

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 76:882-894

Disordered or unstructured regions of proteins, while often very important biologically, can pose significant challenges for resonance assignment and three-dimensional structure determination of the ordered regions of proteins by NMR methods. In this

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73d1f454d89a444b48331b77658a9377
https://doi.org/10.1002/prot.22394

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Association of putative concave protein-binding sites with the fluctuation behavior of residues

Autor: Asli Ertekin, Turkan Haliloglu, Ruth Nussinov

Publikováno v: Protein Science. 15:2265-2277

Here, we propose a binding site prediction method based on the high frequency end of the spectrum in the native state of the protein structural dynamics. The spectrum is obtained using an elastic network model (GNM). High frequency vibrating (HFV) re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89c614521ec33e33b01f70268fe0663e
https://doi.org/10.1110/ps.051815006

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Understanding the Role of Conformational Dynamics in Protein-Ligand Interactions Using NMR Relaxation Methods

Autor: Francesca Massi, Asli Ertekin

Publikováno v: eMagRes

Protein conformational dynamics is a central component of ligand-binding processes because it affects the thermodynamics and the kinetics of binding. The difference in flexibility of the protein between the free and bound states makes a significant c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f58267451589a191692418c2f94b71b9
https://doi.org/10.1002/9780470034590.emrstm1363

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