Conformation dependence of tyrosine binding on the surface of graphene: Bent prefers over parallel orientation

Autor: Jovian Lazare, Tandabany C. Dinadayalane, Dalia Daggag

Publikováno v: Applied Surface Science. 483:178-186

Binding of tyrosine (Tyr) with two finite size graphene sheets of 62 and 186 carbon atoms was investigated using M06-2X/6-31G(d) level. Thorough conformational analysis was done for tyrosine to select few conformers to explore their complexation by c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ed6259ec5b4dcf97d431709dd9f27ef1
https://doi.org/10.1016/j.apsusc.2019.03.181

A single amino acid substitution alters ClpS2 binding specificity

Autor: Kunal Dharmadhikari, Christina Bergonzo, Makenzie Christensen, Jennifer Tullman, Emily Samuels

Publikováno v: ProteinsREFERENCES. 88(9)

ClpS2 is a small protein under development as a probe for selectively recognizing N-terminal amino acids of N-degron peptide fragments. To understand the structural basis of ClpS2 specificity for an N-terminal amino acid, all atom molecular dynamics

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae4b52d345449eaf22d407f6f921084a
https://pubmed.ncbi.nlm.nih.gov/32181926

Tyrosine binding and promiscuity in the arginine repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis

Autor: Raghuvir K. Arni, Anwar Ullah, Ricardo Barros Mariutti, Gabriela C. Araujo, Mário T. Murakami

Publikováno v: Scopus
Repositório Institucional da UNESP
Universidade Estadual Paulista (UNESP)
instacron:UNESP

Made available in DSpace on 2018-12-11T17:03:02Z (GMT). No. of bitstreams: 0 Previous issue date: 2016-07-08 The arginine repressor (ArgR) regulates arginine biosynthesis in a number of microorganisms and consists of two domains interlinked by a shor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e25c52d0b4fe1dcfc63931d2386dbbc

Molecular Characteristics Predict Clinical Outcomes: Prospective Trial Correlating Response to the EGFR Tyrosine Kinase Inhibitor Gefitinib with the Presence of Sensitizing Mutations in the Tyrosine Binding Domain of the EGFR Gene

Autor: Marc Ladanyi, Ronglai Shen, Maureen F. Zakowski, Naiyer A. Rizvi, Bernard J. Park, Mark G. Kris, Jamie E. Chaft, Robert T. Heelan, Christopher G. Azzoli, Raja M. Flores, William Pao, Bhuvanesh Singh, Manjit S. Bains, Vincent A. Miller, Valerie W. Rusch, Lee M. Krug, Robert J. Downey

Publikováno v: Clinical Cancer Research. 17:3500-3506

Purpose: To determine if tumor regression following treatment with gefitinib correlates with the presence of sensitizing mutations in epidermal growth factor receptor (EGFR). Patients and Methods: Patients with resectable stage I and II non–small c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4fce8d95efc3eeeccf1f9ed41fe92d7
https://doi.org/10.1158/1078-0432.ccr-10-2102

The structure ofHaemophilus influenzaeprephenate dehydrogenase suggests unique features of bifunctional TyrA enzymes

Autor: Andrew T. Morse, Mark W. Knuth, Debanu Das, Marc C. Deller, John Wooley, Daniel McMullan, Dennis Carlton, Lian Duan, Dana Weekes, Ron Reyes, Heath E. Klock, Joanna C Grant, Tamara Astakhova, Adam Godzik, Gye Won Han, Kevin K. Jin, Piotr Kozbial, Henry J Tien, Julie Feuerhelm, Polat Abdubek, Hsiu-Ju Chiu, Sanjay Krishna, Edward Nigoghossian, Herbert L. Axelrod, Keith O. Hodgson, Henry van den Bedem, Ian A. Wilson, Ashley M. Deacon, Marc André Elsliger, Scott A. Lesley, Christine B Trame, David Marciano, Abhinav Kumar, Lukasz Jaroszewski, Qingping Xu, Thomas Clayton, Mitchell D. Miller, Anna Grzechnik, Linda Okach

Publikováno v: Acta crystallographica. Section F, Structural biology and crystallization communications, vol 66, iss Pt 10
Acta Crystallographica Section F: Structural Biology and Crystallization Communications

The crystal structure of the prephenate dehydrogenase component of the bifunctional H. influenzae TyrA reveals unique structural differences between bifunctional and monofunctional TyrA enzymes.
Chorismate mutase/prephenate dehydrogenase from Ha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d3f9d047db99dcda92126aad5910709
https://doi.org/10.1107/s1744309110021688