Відмінності між версіями «G-Protein-Linked Receptors And Tyrosine-Kinase Receptors»
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− | + | Theillet F-X, Smet-Nocca C, Liokatis S, Thongwichian R, Kosten J, et al. Cell signaling, post-translational protein modifications and NMR spectroscopy. J Biomol NMR 54: 217236. 17. Zor T, Mayr BM, Dyson HJ, Montminy MR, Wright PE Roles of phosphorylation and helix propensity inside the binding on the KIX domain of CREB-binding protein by constitutive and inducible activators. J Biol Chem 277: 4224142248. 18. Niiro H, Clark EA Selection generating inside the Immune Technique: Regulation of B-cell fate by antigen-receptor signals. Nat Rev Immunol 2: 945956. 19. Reth M Antigen receptor tail clue. Nature 338: 383384. 20. Cambier JC, Daeron M, Fridman W, Gergely J, Kinet JP, et al. New nomenclature for the Reth motif. Immunol Currently 16: 110. 21. Johnson SA, Pleiman CM, Pao L, Schneringer J, Hippen K, et al. Phosphorylated immunoreceptor signaling motifs exhibit special abilities to bind and activate Lyn and Syk tyrosine kinases. J Immunol 155: 45964603. 22. Sada K, Takano T, Yanagi S, Yamamura H Structure and function of Syk protein-tyrosine kinase. J Biochem 130: 177186. 23. Rolli V, Gallwitz M, Wossning T, Flemming A, Schamel WWA, et al. Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop. Mol Cell ten: 10571069. 24. Engels N, Wollscheid B, Wienands J Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-alpha. Eur J Immunol 31: 21262134. 25. Fu C, Turck CW, Kurosaki T, Chan AC BLNK: a central linker protein in B cell activation. Immunity 9: 93103. 26. Wienands J, Schweikert J, Wollscheid B, Jumaa H, Nielsen PJ, Reth M SLP-65: A brand new signaling component in B lymphocytes which demands expression of your antigen receptor for phosphorylation. J Exp Med 188: 791795. 27. Chiu CW, Dalton M, Ishiai M, Kurosaki T, Chan AC BLNK: molecular scaffolding by way of `cis'-mediated organization of signaling proteins. EMBO J 21: 64616472. 28. Monroe JG ITAM-mediated tonic signalling by means of pre-BCR and BCR complexes. Nat Rev Immunol 6: 283294. 29. Pedersen A, Hellberg K, Enberg J, Karlsson BG Rational improvement of cell-free protein synthesis. New Biotechnol 28: 218224. 30. Isaksson L, Mayzel M, Saline M, Pedersen A, Rosenlow J, et al. Hugely Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains. PLoS A single. 31. Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, et al. The CCPN information model for NMR spectroscopy: Improvement of a application pipeline. Proteins: Struct, Funct, Bioinf 59: 687696. 32. Solyom Z, Schwarten M, Geist L, Konrat R, Willbold D, et al. BESTTROSY experiments for time-efficient sequential resonance assignment of massive disordered proteins. J Biomol NMR 55: 311321. 33. Jaravine VA, Zhuravleva AV, Permi P, Ibraghimov I, Orekhov VY Hyperdimensional NMR spectroscopy with nonlinear sampling. J Am Chem Soc 130: 39273936. 34. Jaravine VA, Orekhov VY Targeted acquisition for real-time NMR spectroscopy. J Am Chem Soc 128: 1342113426. 35. Modig K, Jurgensen VW, Lindorff-Larsen K, [http://www.medchemexpress.com/Itacitinib.html INCB 039110] Fieber W, Bohr HG, et al. Detection of initiation web-sites in protein folding of the four helix bundle ACBP by chemical shift evaluation. FEBS Lett 581: 49654971. 36. Wider G, Dreier L Measuring protein concentrations by NMR spectroscopy. J |
Поточна версія на 05:33, 7 липня 2017
Theillet F-X, Smet-Nocca C, Liokatis S, Thongwichian R, Kosten J, et al. Cell signaling, post-translational protein modifications and NMR spectroscopy. J Biomol NMR 54: 217236. 17. Zor T, Mayr BM, Dyson HJ, Montminy MR, Wright PE Roles of phosphorylation and helix propensity inside the binding on the KIX domain of CREB-binding protein by constitutive and inducible activators. J Biol Chem 277: 4224142248. 18. Niiro H, Clark EA Selection generating inside the Immune Technique: Regulation of B-cell fate by antigen-receptor signals. Nat Rev Immunol 2: 945956. 19. Reth M Antigen receptor tail clue. Nature 338: 383384. 20. Cambier JC, Daeron M, Fridman W, Gergely J, Kinet JP, et al. New nomenclature for the Reth motif. Immunol Currently 16: 110. 21. Johnson SA, Pleiman CM, Pao L, Schneringer J, Hippen K, et al. Phosphorylated immunoreceptor signaling motifs exhibit special abilities to bind and activate Lyn and Syk tyrosine kinases. J Immunol 155: 45964603. 22. Sada K, Takano T, Yanagi S, Yamamura H Structure and function of Syk protein-tyrosine kinase. J Biochem 130: 177186. 23. Rolli V, Gallwitz M, Wossning T, Flemming A, Schamel WWA, et al. Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop. Mol Cell ten: 10571069. 24. Engels N, Wollscheid B, Wienands J Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-alpha. Eur J Immunol 31: 21262134. 25. Fu C, Turck CW, Kurosaki T, Chan AC BLNK: a central linker protein in B cell activation. Immunity 9: 93103. 26. Wienands J, Schweikert J, Wollscheid B, Jumaa H, Nielsen PJ, Reth M SLP-65: A brand new signaling component in B lymphocytes which demands expression of your antigen receptor for phosphorylation. J Exp Med 188: 791795. 27. Chiu CW, Dalton M, Ishiai M, Kurosaki T, Chan AC BLNK: molecular scaffolding by way of `cis'-mediated organization of signaling proteins. EMBO J 21: 64616472. 28. Monroe JG ITAM-mediated tonic signalling by means of pre-BCR and BCR complexes. Nat Rev Immunol 6: 283294. 29. Pedersen A, Hellberg K, Enberg J, Karlsson BG Rational improvement of cell-free protein synthesis. New Biotechnol 28: 218224. 30. Isaksson L, Mayzel M, Saline M, Pedersen A, Rosenlow J, et al. Hugely Efficient NMR Assignment of Intrinsically Disordered Proteins: Application to B- and T Cell Receptor Domains. PLoS A single. 31. Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, et al. The CCPN information model for NMR spectroscopy: Improvement of a application pipeline. Proteins: Struct, Funct, Bioinf 59: 687696. 32. Solyom Z, Schwarten M, Geist L, Konrat R, Willbold D, et al. BESTTROSY experiments for time-efficient sequential resonance assignment of massive disordered proteins. J Biomol NMR 55: 311321. 33. Jaravine VA, Zhuravleva AV, Permi P, Ibraghimov I, Orekhov VY Hyperdimensional NMR spectroscopy with nonlinear sampling. J Am Chem Soc 130: 39273936. 34. Jaravine VA, Orekhov VY Targeted acquisition for real-time NMR spectroscopy. J Am Chem Soc 128: 1342113426. 35. Modig K, Jurgensen VW, Lindorff-Larsen K, INCB 039110 Fieber W, Bohr HG, et al. Detection of initiation web-sites in protein folding of the four helix bundle ACBP by chemical shift evaluation. FEBS Lett 581: 49654971. 36. Wider G, Dreier L Measuring protein concentrations by NMR spectroscopy. J