Výsledky vyhledávání - "Pat Loulakis"

SRT1720, SRT2183, SRT1460, and Resveratrol Are Not Direct Activators of SIRT1

Autor: Jane M. Withka, David A. Griffith, John E. Bleasdale, Declan Flynn, Brian J. Stockman, Pat Loulakis, Kay Ahn, Xiayang Qiu, Jessica Ward, David Cunningham, Venkataraman Thanabal, Michelle Pacholec, Alison H. Varghese, Brandon Pabst, Boris A. Chrunyk, Robert S. Garofalo, Matt Griffor

Publikováno v: Journal of Biological Chemistry. 285:8340-8351

Sirtuins catalyze NAD(+)-dependent protein deacetylation and are critical regulators of transcription, apoptosis, metabolism, and aging. There are seven human sirtuins (SIRT1-7), and SIRT1 has been implicated as a key mediator of the pathways downstr

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce433ade6151df51a9b60b2e829af876
https://doi.org/10.1074/jbc.m109.088682

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Crystal structure of activin receptor type IIB kinase domain from human at 2.0 Angstrom resolution

Autor: Zhi Xie, Matt Griffor, Seungil Han, Pat Loulakis

Publikováno v: Protein science : a publication of the Protein Society. 16(10)

Activin receptor type IIB (ActRIIB), a type II TGF-beta serine/threonine kinase receptor, is integral to the activin and myostatin signaling pathway. Ligands such as activin and myostatin bind to activin type II receptors (ActRIIA, ActRIIB), and the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53bf5abf47fbedea85cb9aaa4a6298f6
https://pubmed.ncbi.nlm.nih.gov/17893364

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Phosphorylation of serine residues in histidine-tag sequences attached to recombinant protein kinases: a cause of heterogeneity in mass and complications in function

Autor: Ping Du, Anil Mistry, Kieran F. Geoghegan, Peter K. LeMotte, Kevin Coleman, Chun Luo, Zhi Xie, Kristina Rafidi, Francis Rajamohan, Pat Loulakis, Samuel P. Simons

Publikováno v: Protein expression and purification. 44(2)

High-level recombinant expression of protein kinases in eukaryotic cells or Escherichia coli commonly gives products that are phosphorylated by autocatalysis or by the action of endogenous kinases. Here, we report that phosphorylation occurred on ser

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5c6574e0e4e5115b5b550e883289ad2
https://pubmed.ncbi.nlm.nih.gov/15946859

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Tandem mass spectrometry of multiply phosphorylated forms of a 'histidine-tag' derived from a recombinant protein kinase expressed in bacteria

Autor: Samuel P. Simons, Zhi Xie, Pat Loulakis, Kieran F. Geoghegan, Ping Du

Publikováno v: Rapid communications in mass spectrometry : RCM. 19(4)

When a histidine-tagged form of the protein kinase Aurora-2 was expressed in Escherichia coli, the purified product carried four to nine phosphate groups, although many fewer were expected. The amino-terminal tag had the sequence GSSHHHHHHSSGLVPRGSHM

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f43302bfcff1805544978703f72b8354
https://pubmed.ncbi.nlm.nih.gov/15669100

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LC-mass spectrometry analysis of N- and C-terminal boundary sequences of polypeptide fragments by limited proteolysis

Autor: Justin G. Stroh, Pat Loulakis, Anthony J. Lanzetti, Julie Xie

Publikováno v: Journal of the American Society for Mass Spectrometry. 16(1)

Limited proteolysis is an important and widely used method for analyzing the tertiary structure and determining the domain boundaries of proteins. Here we describe a novel method for determining the N- and C-terminal boundary amino acid sequences of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40365f0f929d17754e371c4b0a3d9ef7
https://pubmed.ncbi.nlm.nih.gov/15653362

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