Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Laavanya, Parthasarathi"'
Publikováno v:
Acta Crystallographica Section E, Vol 66, Iss 7, Pp m853-m854 (2010)
In the structure of the title compound, [Fe(C7H7N2O2)3]·CH3CH2OH, the FeIII atom is in a distorted octahedral O6 environment with the three hydroxamate O atoms (and the three carbonyl O atoms) arranged in a fac configuration and one of the hydroxama
Externí odkaz:
https://doaj.org/article/acf623e26145496aab59c0d5c970b057
Autor:
Laavanya, Parthasarathi, Krishnamoorthy, Bellie Sundaram, Panchanatheswaran, Krishnaswamy *, Manoharan, Mariappan
Publikováno v:
In Journal of Molecular Structure: THEOCHEM 2005 716(1):149-158
Autor:
Marie Jose Gil, Zoya A. Starikova, Laavanya Parthasarathi, Eimear C. O'Brien, Declan Gaynor, Ahmed Alagha, Etelka Farkas, Kevin B. Nolan, Helge Müller-Bunz
Publikováno v:
Inorganica Chimica Acta. 368:58-66
The attempted acetylation of anthranilic hydroxamic acid (2-aminobenzohydroxamic acid) as a possible dual inhibitor of the catalytic sites in prostaglandin-H-synthase (PGHS) gave the cyclic hydroxamic acid 3-hydroxy-2-methyl-3 H -quinazolin-4-one (Ch
Autor:
Heide Daxecker, Markus Raab, Denis C. Shields, Kenneth H. Mok, Laavanya Parthasarathi, Marc Devocelle, Niamh Moran, Colm O'Dushlaine, Elise Bernard, Tia E. Keyes, Min-Kyu Cho, Lynda Cosgrave, Sarah O'Neill, Kelly Aylward
Publikováno v:
ACS Chemical Biology. 4:457-471
A synthetic cell-permeable peptide corresponding to the highly conserved alpha-integrin signature motif, Palmityl-K(989)VGFFKR(995) (Pal-FF), induces integrin activation and aggregation in human platelets. Systematic replacement of the F(992)-F(993)
Autor:
Laavanya Parthasarathi, Kristian Vlahoviček, Sándor Pongor, Oliviero Carugo, Alessandro Pintar
Publikováno v:
Nucleic Acids Research
The WWW servers at http://www.icgeb.org/protein/ are dedicated to the analysis of protein 3D structures submitted by the users as the Protein Data Bank (PDB) files. CX computes an atomic protrusion index that makes it possible to highlight the protru
Autor:
Derek Murphy, Berenice Ortiz, Maria Meehan, Armida W. M. Fabius, Niamh H. Foley, Laavanya Parthasarathi, Jacqueline Ryan, Timothy A. Chan, Niamh Moran, Caroline A. Jefferies, Elisa Lazzari, Raymond L. Stallings
Publikováno v:
Molecular Cancer, Vol 11, Iss 1, p 6 (2012)
Molecular Cancer
Molecular Cancer
Background Protein tyrosine phosphatase receptor delta (PTPRD) is a member of a large family of protein tyrosine phosphatases which negatively regulate tyrosine phosphorylation. Neuroblastoma is a major childhood cancer arising from precursor cells o
Publikováno v:
Atlas of Genetics and Cytogenetics in Oncology and Haematology.
Review on PTPRD (protein tyrosine phosphatase, receptor type, D), with data on DNA, on the protein encoded, and where the gene is implicated.
Publikováno v:
Acta Crystallographica Section E, Vol 66, Iss 7, Pp m853-m854 (2010)
Acta Crystallographica Section E: Structure Reports
Acta Crystallographica Section E: Structure Reports
In the structure of the title compound, [Fe(C7H7N2O2)3]·CH3CH2OH, the FeIII atom is in a distorted octahedral O6 environment with the three hydroxamate O atoms (and the three carbonyl O atoms) arranged in a fac configuration and one of the hydroxama
Publikováno v:
Biochemical and biophysical research communications. 392(3)
The capacity of platelets to form a thrombus is mediated by integrin alpha(IIb)beta(3). The cytoplasmic tail of alpha(IIb) contains a highly conserved motif, (989)KVGFFKR(995), which plays a critical role in regulating integrin activation and acts as
Publikováno v:
ChemInform. 40
Most biological functions are regulated through complex networks of transient protein interactions, and, thus, finding effective ways to modulate them would represent an important step towards defining the next generation of drugs. In this study, we