-
1
-
-
0017649032
-
Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin
-
PMID: 599557
-
Cleveland DW, Hwo S-Y, Kirschner MW. Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin. J Mol Biol. 1977; 116: 207–225. https://doi.org/10.1016/0022-2836(77)90213-3 PMID: 599557
-
(1977)
J Mol Biol
, vol.116
, pp. 207-225
-
-
Cleveland, D.W.1
Hwo, S.-Y.2
Kirschner, M.W.3
-
2
-
-
84949116801
-
The relationship between truncation and phosphorylation at the C-terminus of tau protein in the paired helical filaments of Alzheimer’s disease
-
PMID: 25717290
-
Flores-Rodríguez P, Ontiveros-Torres MA, Cárdenas-Aguayo MC, Luna-Arias JP, Meraz-Ríos MA, Vir-amontes-Pintos A, et al. The relationship between truncation and phosphorylation at the C-terminus of tau protein in the paired helical filaments of Alzheimer’s disease. Front Neurosci. 2015; 9: 33. https://doi.org/10.3389/fnins.2015.00033 PMID: 25717290
-
(2015)
Front Neurosci
, vol.9
, pp. 33
-
-
Flores-Rodríguez, P.1
Ontiveros-Torres, M.A.2
Cárdenas-Aguayo, M.C.3
Luna-Arias, J.P.4
Meraz-Ríos, M.A.5
Vir-Amontes-Pintos, A.6
-
3
-
-
61849088424
-
Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
-
PMID: 19246243
-
Hanger DP, Anderton BH, Noble W. Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med. 2009; 15: 112–9. https://doi.org/10.1016/j.molmed.2009.01.003 PMID: 19246243
-
(2009)
Trends Mol Med
, vol.15
, pp. 112-119
-
-
Hanger, D.P.1
Anderton, B.H.2
Noble, W.3
-
4
-
-
0031007546
-
Regulated phosphorylation and dephosphorylation of tau protein: Effects on microtubule interaction, intracellular trafficking and neurodegeneration
-
PMID: 9169588
-
BILLINGSLEY ML, KINCAID RL. Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration. Biochem J. 1997; 323: 577–591. https://doi.org/10.1042/bj3230577 PMID: 9169588
-
(1997)
Biochem J
, vol.323
, pp. 577-591
-
-
Billingsley, M.L.1
Kincaid, R.L.2
-
5
-
-
0031052339
-
Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5
-
PMID: 9059986
-
Sengupta A, Wu Q, Grundke-Iqbal I, Iqbal K, Singh TJ. Potentiation of GSK-3-catalyzed Alzheimer-like phosphorylation of human tau by cdk5. Mol Cell Biochem. 1997; 167: 99–105. https://doi.org/10.1023/A:1006883924775 PMID: 9059986
-
(1997)
Mol Cell Biochem
, vol.167
, pp. 99-105
-
-
Sengupta, A.1
Wu, Q.2
Grundke-Iqbal, I.3
Iqbal, K.4
Singh, T.J.5
-
6
-
-
77958513226
-
Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E
-
PMID: 20679343
-
Leroy A, Landrieu I, Huvent I, Legrand D, Codeville B, Wieruszeski J-M, et al. Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E. J Biol Chem. 2010; 285: 33435–44. https://doi.org/10.1074/jbc.M110.149419PMID: 20679343
-
(2010)
J Biol Chem
, vol.285
, pp. 33435-33444
-
-
Leroy, A.1
Landrieu, I.2
Huvent, I.3
Legrand, D.4
Codeville, B.5
Wieruszeski, J.-M.6
-
7
-
-
79959222357
-
Deconstructing GSK-3: The fine regulation of its activity
-
PMID: 21629747
-
Medina M, Wandosell F. Deconstructing GSK-3: The Fine Regulation of Its Activity. Int J Alzheimers Dis. 2011; 2011: 479249. https://doi.org/10.4061/2011/479249 PMID: 21629747
-
(2011)
Int J Alzheimers Dis
, vol.2011
, pp. 479249
-
-
Medina, M.1
Wandosell, F.2
-
8
-
-
85016475088
-
C-terminal truncation of GSK-3? enhances its dephosphorylation by PP2A
-
PMID: 28267204
-
Jin N, Wu Y, Xu W, Gong C-X, Iqbal K, Liu F. C-terminal truncation of GSK-3? enhances its dephosphorylation by PP2A. FEBS Lett. 2017; 591: 1053–1063. https://doi.org/10.1002/1873-3468.12617PMID: 28267204
-
(2017)
FEBS Lett
, vol.591
, pp. 1053-1063
-
-
Jin, N.1
Wu, Y.2
Xu, W.3
Gong, C.-X.4
Iqbal, K.5
Liu, F.6
-
9
-
-
84995973237
-
Site-specific phosphorylation of tau inhibits amyloid-? toxicity in Alzheimer’s mice
-
PMID: 27856911
-
Ittner A, Chua SW, Bertz J, Volkerling A, van der Hoven J, Gladbach A, et al. Site-specific phosphorylation of tau inhibits amyloid-? toxicity in Alzheimer’s mice. Science (80-). 2016; 354: 904–908. https://doi.org/10.1126/science.aah6205 PMID: 27856911
-
(2016)
Science (80-)
, vol.354
, pp. 904-908
-
-
Ittner, A.1
Chua, S.W.2
Bertz, J.3
Volkerling, A.4
van der Hoven, J.5
Gladbach, A.6
-
10
-
-
27644478606
-
Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation
-
PMID: 16262633
-
Liu F, Grundke-Iqbal I, Iqbal K, Gong C-X. Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation. Eur J Neurosci. 2005; 22: 1942–50. https://doi.org/10.1111/j.1460-9568.2005.04391.x PMID: 16262633
-
(2005)
Eur J Neurosci
, vol.22
, pp. 1942-1950
-
-
Liu, F.1
Grundke-Iqbal, I.2
Iqbal, K.3
Gong, C.-X.4
-
11
-
-
84995451096
-
Therapeutic strategies for the treatment of tauopathies: Hopes and challenges
-
PMID: 27751442
-
Khanna MR, Kovalevich J, Lee VM-Y, Trojanowski JQ, Brunden KR. Therapeutic strategies for the treatment of tauopathies: Hopes and challenges. Alzheimer’s Dement. 2016; 12: 1051–1065. https://doi.org/10.1016/j.jalz.2016.06.006 PMID: 27751442
-
(2016)
Alzheimer’S Dement
, vol.12
, pp. 1051-1065
-
-
Khanna, M.R.1
Kovalevich, J.2
Lee, V.M.-Y.3
Trojanowski, J.Q.4
Brunden, K.R.5
-
13
-
-
84992025495
-
Reduction of Nuak1 decreases Tau and reverses phenotypes in a tauopathy mouse model
-
Elsevier Inc.; PMID: 27720485
-
Lasagna-Reeves CA, de Haro M, Hao S, Park J, Rousseaux MWC, Al-Ramahi I, et al. Reduction of Nuak1 Decreases Tau and Reverses Phenotypes in a Tauopathy Mouse Model. Neuron. Elsevier Inc.; 2016; 92: 407–418. https://doi.org/10.1016/j.neuron.2016.09.022 PMID: 27720485
-
(2016)
Neuron
, vol.92
, pp. 407-418
-
-
Lasagna-Reeves, C.A.1
De Haro, M.2
Hao, S.3
Park, J.4
Rousseaux, M.W.C.5
Al-Ramahi, I.6
-
14
-
-
84930697518
-
Mixed mechanisms of multi-site phosphorylation
-
PMID: 25972433
-
Suwanmajo T, Krishnan J. Mixed mechanisms of multi-site phosphorylation. J R Soc Interface. 2015; 12: 20141405–20141405. https://doi.org/10.1098/rsif.2014.1405 PMID: 25972433
-
(2015)
J R Soc Interface
, vol.12
, pp. 20141405
-
-
Suwanmajo, T.1
Krishnan, J.2
-
15
-
-
38149083357
-
Rule-Based Modelling of Cellular Signalling
-
Berlin, Heidelberg: Springer Berlin Heidelberg
-
Danos V, Feret J, Fontana W, Harmer R, Krivine J. Rule-Based Modelling of Cellular Signalling. CONCUR 2007 –Concurrency Theory. Berlin, Heidelberg: Springer Berlin Heidelberg; pp. 17–41. https://doi.org/10.1007/978-3-540-74407-8_3
-
CONCUR 2007 –Concurrency Theory
, pp. 17-41
-
-
Danos, V.1
Feret, J.2
Fontana, W.3
Harmer, R.4
Krivine, J.5
-
16
-
-
4444382239
-
Formal molecular biology
-
Danos V, Laneve C. Formal molecular biology. Theor Comput Sci. 2004; 325: 69–110. https://doi.org/10.1016/j.tcs.2004.03.065
-
(2004)
Theor Comput Sci
, vol.325
, pp. 69-110
-
-
Danos, V.1
Laneve, C.2
-
17
-
-
21644485536
-
Combinatorial complexity and dynamical restriction of network flows in signal transduction
-
Faeder JR, Blinov ML, Goldstein B, Hlavacek WS. Combinatorial complexity and dynamical restriction of network flows in signal transduction. Syst Biol (Stevenage). 2005; 2: 5–15. Available: http://www.ncbi.nlm.nih.gov/pubmed/17091578
-
(2005)
Syst Biol (Stevenage)
, vol.2
, pp. 5-15
-
-
Faeder, J.R.1
Blinov, M.L.2
Goldstein, B.3
Hlavacek, W.S.4
-
18
-
-
23244465153
-
Signaling through receptors and scaffolds: Independent interactions reduce combinatorial complexity
-
PMID: 15923229
-
Borisov NM, Markevich NI, Hoek JB, Kholodenko BN. Signaling through receptors and scaffolds: independent interactions reduce combinatorial complexity. Biophys J. 2005; 89: 951–66. https://doi.org/10.1529/biophysj.105.060533 PMID: 15923229
-
(2005)
Biophys J
, vol.89
, pp. 951-966
-
-
Borisov, N.M.1
Markevich, N.I.2
Hoek, J.B.3
Kholodenko, B.N.4
-
19
-
-
66249102308
-
Multisite protein phosphorylation—from molecular mechanisms to kinetic models
-
PMID: 19438722
-
Salazar C, Höfer T. Multisite protein phosphorylation—from molecular mechanisms to kinetic models. FEBS J. 2009; 276: 3177–98. https://doi.org/10.1111/j.1742-4658.2009.07027.x PMID: 19438722
-
(2009)
FEBS J
, vol.276
, pp. 3177-3198
-
-
Salazar, C.1
Höfer, T.2
-
20
-
-
33750510335
-
PKA modulates GSK-3beta- And cdk5-catalyzed phosphorylation of tau in site- And kinase-specific manners
-
PMID: 17078951
-
Liu F, Liang Z, Shi J, Yin D, El-Akkad E, Grundke-Iqbal I, et al. PKA modulates GSK-3beta- and cdk5-catalyzed phosphorylation of tau in site- and kinase-specific manners. FEBS Lett. 2006; 580: 6269–74. https://doi.org/10.1016/j.febslet.2006.10.033 PMID: 17078951
-
(2006)
FEBS Lett
, vol.580
, pp. 6269-6274
-
-
Liu, F.1
Liang, Z.2
Shi, J.3
Yin, D.4
El-Akkad, E.5
Grundke-Iqbal, I.6
-
21
-
-
0032987650
-
Phosphorylation of tau protein by recombinant GSK-3?: Pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain
-
PMID: 10413115
-
Godemann R, Biernat J, Mandelkow E, Mandelkow E-M. Phosphorylation of tau protein by recombinant GSK-3?: pronounced phosphorylation at select Ser/Thr-Pro motifs but no phosphorylation at Ser262 in the repeat domain. FEBS Lett. 1999; 454: 157–164. https://doi.org/10.1016/S0014-5793(99)00741-3PMID: 10413115
-
(1999)
FEBS Lett
, vol.454
, pp. 157-164
-
-
Godemann, R.1
Biernat, J.2
Mandelkow, E.3
Mandelkow, E.-M.4
-
22
-
-
77955290623
-
DBSolve Optimum: A software package for kinetic modeling which allows dynamic visualization of simulation results
-
PMID: 20698988
-
Gizzatkulov NM, Goryanin II, Metelkin EA, Mogilevskaya EA, Peskov K V, Demin O V. DBSolve Optimum: a software package for kinetic modeling which allows dynamic visualization of simulation results. BMC Syst Biol. 2010; 4: 109. https://doi.org/10.1186/1752-0509-4-109 PMID: 20698988
-
(2010)
BMC Syst Biol
, vol.4
, pp. 109
-
-
Gizzatkulov, N.M.1
Goryanin, I.I.2
Metelkin, E.A.3
Mogilevskaya, E.A.4
Peskov, K.V.5
Demin, O.V.6
-
23
-
-
52049100425
-
Structure of a protein phosphatase 2A holoenzyme: Insights into B55-mediated Tau dephosphorylation
-
PMID: 18922469
-
Xu Y, Chen Y, Zhang P, Jeffrey PD, Shi Y. Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation. Mol Cell. 2008; 31: 873–885. https://doi.org/10.1016/j.molcel.2008.08.006 PMID: 18922469
-
(2008)
Mol Cell
, vol.31
, pp. 873-885
-
-
Xu, Y.1
Chen, Y.2
Zhang, P.3
Jeffrey, P.D.4
Shi, Y.5
-
24
-
-
84954491235
-
Comparison of asymptotic confidence sets for regression in small samples
-
PMID: 26099035
-
Kolobkov D, Demin O, Metelkin E. Comparison of asymptotic confidence sets for regression in small samples. J Biopharm Stat. 2016; 26: 742–57. https://doi.org/10.1080/10543406.2015.1052818 PMID: 26099035
-
(2016)
J Biopharm Stat
, vol.26
, pp. 742-757
-
-
Kolobkov, D.1
Demin, O.2
Metelkin, E.3
-
25
-
-
84899771032
-
Biphasic responses in multi-site phosphorylation systems
-
PMID: 24108693
-
Suwanmajo T, Krishnan J. Biphasic responses in multi-site phosphorylation systems. J R Soc Interface. 2013; 10: 20130742–20130742. https://doi.org/10.1098/rsif.2013.0742 PMID: 24108693
-
(2013)
J R Soc Interface
, vol.10
, pp. 20130742
-
-
Suwanmajo, T.1
Krishnan, J.2
-
26
-
-
84995973237
-
Site-specific phosphorylation of tau inhibits amyloid-? toxicity in Alzheimer’s mice
-
PMID: 27856911
-
Ittner A, Chua SW, Bertz J, Volkerling A, van der Hoven J, Gladbach A, et al. Site-specific phosphorylation of tau inhibits amyloid-? toxicity in Alzheimer’s mice. Science. 2016; 354: 2–66. https://doi.org/10.1126/science.aah6205 PMID: 27856911
-
(2016)
Science
, vol.354
, pp. 2-66
-
-
Ittner, A.1
Chua, S.W.2
Bertz, J.3
Volkerling, A.4
van der Hoven, J.5
Gladbach, A.6
-
27
-
-
33745827715
-
Site-specific phosphorylation and caspase cleavage differentially impact tau-microtubule interactions and tau aggregation
-
PMID: 16687396
-
Ding H, Matthews T a, Johnson GVW. Site-specific phosphorylation and caspase cleavage differentially impact tau-microtubule interactions and tau aggregation. J Biol Chem. 2006; 281: 19107–14. https://doi.org/10.1074/jbc.M511697200 PMID: 16687396
-
(2006)
J Biol Chem
, vol.281
, pp. 19107-19114
-
-
Ding, H.1
Matthews, T.A.2
Johnson, G.V.W.3
-
28
-
-
84979083907
-
Modification of the Drosophila model of in vivo Tau toxicity reveals protective phosphorylation by GSK3?
-
PMID: 24429107
-
Povellato G, Tuxworth RI, Hanger DP, Tear G. Modification of the Drosophila model of in vivo Tau toxicity reveals protective phosphorylation by GSK3?. Biol Open. 2014; 3: 1–11. https://doi.org/10.1242/bio. 20136692 PMID: 24429107
-
(2014)
Biol Open
, vol.3
, pp. 1-11
-
-
Povellato, G.1
Tuxworth, R.I.2
Hanger, D.P.3
Tear, G.4
-
29
-
-
79954575396
-
Combinatorial Tau pseudopho-sphorylation: Markedly different regulatory effects on microtubule assembly and dynamic instability than the sum of the individual parts
-
PMID: 21288907
-
Kiris E, Ventimiglia D, Sargin ME, Gaylord MR, Altinok A, Rose K, et al. Combinatorial Tau Pseudopho-sphorylation: MARKEDLY DIFFERENT REGULATORY EFFECTS ON MICROTUBULE ASSEMBLY AND DYNAMIC INSTABILITY THAN THE SUM OF THE INDIVIDUAL PARTS. J Biol Chem. 2011; 286: 14257–14270. https://doi.org/10.1074/jbc.M111.219311 PMID: 21288907
-
(2011)
J Biol Chem
, vol.286
, pp. 14257-14270
-
-
Kiris, E.1
Ventimiglia, D.2
Sargin, M.E.3
Gaylord, M.R.4
Altinok, A.5
Rose, K.6
-
30
-
-
84891832231
-
Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3?
-
PMID: 24165324
-
Kawakami F, Shimada N, Ohta E, Kagiya G, Kawashima R, Maekawa T, et al. Leucine-rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase-3?. FEBS J. 2013; 1–11. https://doi.org/10.1111/febs.12579 PMID: 24165324
-
(2013)
FEBS J
, pp. 1-11
-
-
Kawakami, F.1
Shimada, N.2
Ohta, E.3
Kagiya, G.4
Kawashima, R.5
Maekawa, T.6
-
31
-
-
84924106368
-
A phase II trial of tideglusib in Alzheimer’s disease
-
PMID: 25537011
-
Lovestone S, Boada M, Dubois B, Hüll M, Rinne JO, Huppertz H-J, et al. A phase II trial of tideglusib in Alzheimer’s disease. J Alzheimers Dis. 2015; 45: 75–88. https://doi.org/10.3233/JAD-141959 PMID: 25537011
-
(2015)
J Alzheimers Dis
, vol.45
, pp. 75-88
-
-
Lovestone, S.1
Boada, M.2
Dubois, B.3
Hüll, M.4
Rinne, J.O.5
Huppertz, H.-J.6
-
32
-
-
84936942984
-
Cerebrospinal fluid P-Tau181P: Biomarker for improved differential dementia diagnosis
-
Struyfs H, Niemantsverdriet E, Goossens J, Fransen E, Martin J-J, De Deyn PP, et al. Cerebrospinal Fluid P-Tau181P: Biomarker for Improved Differential Dementia Diagnosis. Front Neurol. 2015; 6: 1–8.
-
(2015)
Front Neurol
, vol.6
, pp. 1-8
-
-
Struyfs, H.1
Niemantsverdriet, E.2
Goossens, J.3
Fransen, E.4
Martin, J.-J.5
De Deyn, P.P.6
-
33
-
-
85018653782
-
Comparison of CSF markers and semi-quantitative amyloid PET in Alzheimer’s disease diagnosis and in cognitive impairment prognosis using the ADNI-2 database
-
PMID: 28441967
-
Ben Bouallègue F, Mariano-Goulart D, Payoux P. Comparison of CSF markers and semi-quantitative amyloid PET in Alzheimer’s disease diagnosis and in cognitive impairment prognosis using the ADNI-2 database. Alzheimers Res Ther. Alzheimer’s Research & Therapy; 2017; 9: 32. https://doi.org/10.1186/ s13195-017-0260-z PMID: 28441967
-
(2017)
Alzheimers Res Ther. Alzheimer’S Research & Therapy
, vol.9
, pp. 32
-
-
Ben Bouallègue, F.1
Mariano-Goulart, D.2
Payoux, P.3
-
34
-
-
77955930256
-
NMR spectroscopy of the neuronal tau protein: Normal function and implication in Alzheimer’s disease
-
PMID: 20658994
-
Landrieu I, Leroy A, Smet-Nocca C, Huvent I, Amniai L, Hamdane M, et al. NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer’s disease. Biochem Soc Trans. 2010; 38: 1006–11. https://doi.org/10.1042/BST0381006 PMID: 20658994
-
(2010)
Biochem Soc Trans
, vol.38
, pp. 1006-1011
-
-
Landrieu, I.1
Leroy, A.2
Smet-Nocca, C.3
Huvent, I.4
Amniai, L.5
Hamdane, M.6
-
35
-
-
33645396918
-
NMR analysis of a Tau phosphorylation pattern
-
PMID: 16536530
-
Landrieu I, Lacosse L, Leroy A, Wieruszeski J, Trivelli X, Sillen A, et al. NMR analysis of a Tau phosphorylation pattern. J Am Chem Soc. 2006; 128: 3575–83. https://doi.org/10.1021/ja054656+ PMID: 16536530
-
(2006)
J Am Chem Soc
, vol.128
, pp. 3575-3583
-
-
Landrieu, I.1
Lacosse, L.2
Leroy, A.3
Wieruszeski, J.4
Trivelli, X.5
Sillen, A.6
-
36
-
-
80052638024
-
Characterization of the AT180 epitope of phosphorylated Tau protein by a combined nuclear magnetic resonance and fluorescence spectroscopy approach
-
PMID: 21871442
-
Amniai L, Lippens G, Landrieu I. Characterization of the AT180 epitope of phosphorylated Tau protein by a combined nuclear magnetic resonance and fluorescence spectroscopy approach. Biochem Biophys Res Commun. 2011; 412: 743–6. https://doi.org/10.1016/j.bbrc.2011.08.046 PMID: 21871442
-
(2011)
Biochem Biophys Res Commun
, vol.412
, pp. 743-746
-
-
Amniai, L.1
Lippens, G.2
Landrieu, I.3
-
37
-
-
84920479139
-
Cross talk between PI3K-AKT-GSK-3? and PP2A pathways determines tau hyperphosphorylation
-
PMID: 25219467
-
Wang Y, Yang R, Gu J, Yin X, Jin N, Xie S, et al. Cross talk between PI3K-AKT-GSK-3? and PP2A pathways determines tau hyperphosphorylation. Neurobiol Aging. 2015; 36: 188–200. https://doi.org/10.1016/j.neurobiolaging.2014.07.035 PMID: 25219467
-
(2015)
Neurobiol Aging
, vol.36
, pp. 188-200
-
-
Wang, Y.1
Yang, R.2
Gu, J.3
Yin, X.4
Jin, N.5
Xie, S.6
-
39
-
-
84948703497
-
GSK-3? is dephosphorylated by PP2A in a Leu309 methylation-independent manner
-
Wang J, editor. PMID: 26484916
-
Chu D, Tan J, Xie S, Jin N, Yin X, Gong C-X, et al. GSK-3? is Dephosphorylated by PP2A in a Leu309 Methylation-Independent Manner. Wang J, editor. J Alzheimers Dis. 2016; 49: 365–75. https://doi.org/10.3233/JAD-150497 PMID: 26484916
-
(2016)
J Alzheimers Dis
, vol.49
, pp. 365-375
-
-
Chu, D.1
Tan, J.2
Xie, S.3
Jin, N.4
Yin, X.5
Gong, C.-X.6
-
40
-
-
79959736543
-
Glycogen synthase kinase-3? regulates Tyr307 phosphorylation of protein phosphatase-2A via protein tyrosine phosphatase 1B but not Src
-
PMID: 21554241
-
Yao X-Q, Zhang X-X, Yin Y-Y, Liu B, Luo D-J, Liu D, et al. Glycogen synthase kinase-3? regulates Tyr307 phosphorylation of protein phosphatase-2A via protein tyrosine phosphatase 1B but not Src. Biochem J. 2011; 437: 335–44. https://doi.org/10.1042/BJ20110347 PMID: 21554241
-
(2011)
Biochem J
, vol.437
, pp. 335-344
-
-
Yao, X.-Q.1
Zhang, X.-X.2
Yin, Y.-Y.3
Liu, B.4
Luo, D.-J.5
Liu, D.6
-
41
-
-
84870659704
-
High-resolution mapping of linear antibody epitopes using ultrahigh-density peptide microarrays
-
PMID: 22984286
-
Buus S, Rockberg J, Forsström B, Nilsson P, Uhlen M, Schafer-Nielsen C. High-resolution mapping of linear antibody epitopes using ultrahigh-density peptide microarrays. Mol Cell Proteomics. 2012; 11: 1790–800. https://doi.org/10.1074/mcp.M112.020800 PMID: 22984286
-
(2012)
Mol Cell Proteomics
, vol.11
, pp. 1790-1800
-
-
Buus, S.1
Rockberg, J.2
Forsström, B.3
Nilsson, P.4
Uhlen, M.5
Schafer-Nielsen, C.6
|