Výsledky vyhledávání - "Udayar, Ilangovan"

The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase

Autor: Tao Huang, Andrew P. Hinck, Udayar Ilangovan, Shengnan Zhang, Paul F. Fitzpatrick

Publikováno v: Journal of Molecular Biology. 426:1483-1497

Tyrosine hydroxylase (TyrH) catalyzes the hydroxylation of tyrosine to form 3,4-dihydroxyphenylalanine in the biosynthesis of the catecholamine neurotransmitters. The activity of the enzyme is regulated by phosphorylation of serine residues in a regu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::533cba685ede3f3a4e06a97601833ab6
https://doi.org/10.1016/j.jmb.2013.12.015

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Human Polyhomeotic Homolog 3 (PHC3) Sterile Alpha Motif (SAM) Linker Allows Open-Ended Polymerization of PHC3 SAM

Autor: Chongwoo A. Kim, Virgil Schirf, Andrew P. Hinck, Yogeet Kaur, Borries Demeler, Belinda Z. Leal, Angela K. Robinson, David R. Nanyes, Udayar Ilangovan

Publikováno v: Biochemistry. 51:5379-5386

Sterile alpha motifs (SAMs) are frequently found in eukaryotic genomes. An intriguing property of many SAMs is their ability to self-associate, forming an open-ended polymer structure whose formation has been shown to be essential for the function of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a5342da2a53edf80bf381599aa95105
https://doi.org/10.1021/bi3004318

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The TβR-I Pre-Helix Extension Is Structurally Ordered in the Unbound Form and Its Flanking Prolines Are Essential for Binding

Autor: Udayar Ilangovan, Andrew P. Hinck, Tao Huang, Pardeep Mahlawat, Donald G. McEwen, Cynthia S. Hinck, Jay C. Groppe, Jorge E. Zuniga

Publikováno v: Journal of Molecular Biology. 412:601-618

Transforming growth factor β isoforms (TGF-β) are among the most recently evolved members of a signaling superfamily with more than 30 members. TGF-β play vital roles in regulating cellular growth and differentiation, and they signal through a hig

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69a7ad02093ba4fb6bbe233a7683d32f
https://doi.org/10.1016/j.jmb.2011.07.046

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Identification of Nucleic Acid Binding Residues in the FCS Domain of the Polycomb Group Protein Polyhomeotic

Autor: Jeremy M Berg, Udayar Ilangovan, Corey V. Tong, Renjing Wang, Chongwoo A. Kim, Barbara T. Amann, Angela K. Robinson, Belinda Z. Leal, Andrew P. Hinck

Publikováno v: Biochemistry. 50:4998-5007

Polycomb group (PcG) proteins maintain the silent state of developmentally important genes. Recent evidence indicates that noncoding RNAs also play an important role in targeting PcG proteins to chromatin and PcG-mediated chromatin organization, alth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::020816e22ac96bd30b85da2b9e022c50
https://doi.org/10.1021/bi101487s

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Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase

Autor: Udayar Ilangovan, Andrew P. Hinck, S. Colette Daubner, Paul F. Fitzpatrick, Jun Li

Publikováno v: Archives of Biochemistry and Biophysics. 505:250-255

The physiological role of the liver enzyme phenylalanine hydroxylase (PheH)1 is to catalyze the hydroxylation of excess phenylalanine in the diet to form tyrosine, using tetrahydrobiopterin (BH4) as the source of electrons for this monooxygenation re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9e492ff38855cc2e857f27a8048db75
https://doi.org/10.1016/j.abb.2010.10.009

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Structural Transitions of the RING1B C-Terminal Region upon Binding the Polycomb cbox Domain

Autor: Chongwoo A. Kim, Udayar Ilangovan, Eileen M. Lafer, Virgil Schirf, Renjing Wang, Patricia M. Schwarz, Andrew P. Hinck, Angela K. Robinson, Borries Demeler

Publikováno v: Biochemistry. 47:8007-8015

Polycomb group (PcG) proteins are required for maintaining cell identity and stem cell self-renewal. RING1B and Polycomb (Pc) are two components of a multiprotein complex called polycomb repression complex 1 (PRC1) that is essential for establishing

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::080fb8721d387ed1a75ccf3eabe52f8a
https://doi.org/10.1021/bi800857f

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Staphylococcus aureus Sortase A Transpeptidase

Autor: William Thieu, Udayar Ilangovan, Nuttee Suree, Jeremy J. Clemens, Robert T. Clubb, Mandar T. Naik, Dean Campbell, Chu Kong Liew, Michael E. Jung

Publikováno v: Journal of Biological Chemistry. 281:1817-1826

Many virulence factors in Gram-positive bacteria are covalently anchored to the cell-wall peptidoglycan by sortase enzymes, a group of widely distributed cysteine transpeptidases. The Staphylococcus aureus Sortase A protein (SrtA) is the archetypal m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::83890637e70f244a4a5ea07cf62c195a
https://doi.org/10.1074/jbc.m506123200

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Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus

Autor: Olaf Schneewind, Udayar Ilangovan, Robert T. Clubb, Junji Iwahara, Hung Ton-That

Publikováno v: Proceedings of the National Academy of Sciences. 98:6056-6061

Surface proteins of Gram-positive bacteria play important roles during the pathogenesis of human infections and require sortase for anchoring to the cell-wall envelope. Sortase cleaves surface proteins at the LPXTG motif and catalyzes the formation o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd7f1b436bc68ce12917ad869fb7b714
https://doi.org/10.1073/pnas.101064198

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