Assemblies of salen-type oxidovanadium(iv) complexes: substituent effects and in vitro protein tyrosine phosphatase inhibition

2014 ◽  
Vol 43 (45) ◽  
pp. 17044-17053 ◽  
Author(s):  
Piotr Zabierowski ◽  
Janusz Szklarzewicz ◽  
Ryszard Gryboś ◽  
Barbara Modryl ◽  
Wojciech Nitek
Keyword(s):  
Systematic Study ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Substituent Effects ◽  
Complex Molecules ◽  
Protein Tyrosine ◽  
Phosphatase Inhibition ◽  
Vitro Protein

A systematic study of 5,5′-disubstituted oxidovanadium(iv) complexes with a chiral salen type ligand showed variable assemblies of complex molecules dependent on steric and electronic factors of the substituents.

Analysis of in vitro interactions of protein tyrosine phosphatase 1B with insulin receptors

2001 ◽  
Vol 173 (1-2) ◽  
pp. 109-120 ◽  
Author(s):  
Xin-Yuan Wang ◽  
Katrin Bergdahl ◽  
Anna Heijbel ◽  
Charlotta Liljebris ◽  
John E. Bleasdale
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Insulin Receptors ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
In Vitro Interactions

Protein-tyrosine phosphatase activity of CD45 is activated by sequential phosphorylation by two kinases

1994 ◽  
Vol 14 (8) ◽  
pp. 5523-5532
Author(s):  
D R Stover ◽  
K A Walsh
Keyword(s):  
T Cell Activation ◽  
Protein Tyrosine Phosphatase ◽  
Time Course ◽  
Cell Activation ◽  
Regulatory Mechanism ◽  
Transmembrane Protein ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine

We describe a potential regulatory mechanism for the transmembrane protein-tyrosine phosphatase CD45. Phosphorylation on both tyrosine and serine residues in vitro results in an activation of CD45 specifically toward one artificial substrate but not another. The activation of these kinases appears to be order dependent, as it is enhanced when phosphorylation of tyrosine precedes that of serine but phosphorylation in the reverse order yields no activation. Any of four protein-tyrosine kinases tested, in combination with the protein-serine/threonine kinase, casein kinase II, was capable of mediating this activation in vitro. The time course of phosphorylation of CD45 in response to T-cell activation is consistent with the possibility that this regulatory mechanism is utilized in vivo.

scholarly journals Six New 3,5-Dimethylcoumarins from Chelonopsis praecox, Chelonopsis odontochila and Chelonopsis pseudobracteata

2021 ◽  
Author(s):  
Chang-An Geng ◽  
Zhen-Tao Deng ◽  
Qian Huang ◽  
Chun-Lei Xiang ◽  
Ji-Jun Chen
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
2D Nmr ◽  
Cell Protein ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Aerial Parts ◽  
Spectroscopic Analyses ◽  
New Compounds

AbstractTen 3,5-dimethylcoumarins (1–6 and 8‒11) involving six new ones (1–6), together with a known 3-methylcoumarin (7), were isolated from the aerial parts of three Chelonopsis plants, C. praecox, C. odontochila, and C. pseudobracteata. The structures of the new compounds were determined by extensive HRESIMS, 1D and 2D NMR spectroscopic analyses. According to the substitution at C-5, these coumarins were classified into 5-methyl, 5-hydroxymethyl, 5-formyl, and 5-nor types. All the isolates were assayed for their inhibition on α-glucosidase, protein tyrosine phosphatase 1B, and T-cell protein tyrosine phosphatase in vitro. Graphic Abstract

scholarly journals Simulasi Docking Senyawa Aglikon Kurkuligosida A dan Turunannya pada Protein Tyrosine Phosphatase 1B (PTP1B)

2019 ◽  
Vol 16 (2) ◽  
pp. 216
Author(s):  
Nursamsiar Nursamsiar ◽  
Akbar Awaluddin ◽  
Megawati Megawati ◽  
Yulita M. Soko ◽  
Muhammad Aswad
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Autodock 4.2 ◽  
Diabetes Melitus

Senyawa aglikon kurkuligosida A memiliki struktur yang mirip dengan senyawa licoagrochalcone yang terbukti memiliki aktivitas penghambatan yang kuat secara in vitro pada Protein Tyrosine Phosphatase 1B (PTP1B), yang dianggap sebagai target terapeutik untuk pengobatan diabetes melitus tipe 2. Penelitian ini bertujuan untuk mengetahui interaksi antara senyawa aglikon kurkuligosida A dan turunannya dengan PTP1B menggunakan metode simulasi docking. Simulasi docking dilakukan dengan menggunakan perangkat lunak AutoDock 4.2. Hasil docking menunjukan semua senyawa yang diuji dapat berinteraksi dengan sisi aktif PTP1B. Interaksi terbaik ditunjukkan oleh senyawa 31 (3,5-dihidroksibensil-3,5-dinitrobenzoate), senyawa 39 (3,5-dihidroksibensil-4-nitrobenzoate) dan senyawa 52 (4-hidroksibensil-4-nitro bensoat) dengan nilai energi bebas ikatan berturut-turut –9,40 kkal/mol ; –9,19 kkal/mol dan –9,03 kkal/mol. Ketiga senyawa tersebut memiliki interaksi dengan sisi aktif PTP1B dengan residu asam amino Ser216 dan Arg221. Semua senyawa turunan aglikon kurkuligosida A yang diuji juga memiliki pola pengikatan yang sama dengan ligan alami pada PTP1B.

In Vitro Enzymatic Assays of Protein Tyrosine Phosphatase 1B

2001 ◽  
Vol 13 (1) ◽  
Author(s):  
Thomas Lubben ◽  
Jill Clampit ◽  
Michael Stashko ◽  
James Trevillyan ◽  
Michael R. Jirousek
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatase 1B ◽  
Enzymatic Assays ◽  
Protein Tyrosine

Selective Inhibitors of the Protein Tyrosine Phosphatase SHP2 Block Cellular Motility and Growth of Cancer Cells in vitro and in vivo

ChemMedChem ◽  
2015 ◽  
Vol 10 (5) ◽  
pp. 815-826 ◽  
Author(s):  
Stefanie Grosskopf ◽  
Chris Eckert ◽  
Christoph Arkona ◽  
Silke Radetzki ◽  
Kerstin Böhm ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Cellular Motility ◽  
Selective Inhibitors ◽  
Protein Tyrosine
Sign in / Sign up

Export Citation Format

Share Document