-
1
-
-
80052741666
-
Importance of domain closure for the autoactivation of ERK2
-
doi: 10.1021/bi200503a
-
Barr, D., Oashi, T., Burkhard, K., Lucius, S., Samadani, R., Zhang, J.,et al. (2011). Importance of domain closure for the autoactivation of ERK2. Biochemistry 50, 8038-8048. doi: 10.1021/bi200503a
-
(2011)
Biochemistry
, vol.50
, pp. 8038-8048
-
-
Barr, D.1
Oashi, T.2
Burkhard, K.3
Lucius, S.4
Samadani, R.5
Zhang, J.6
-
2
-
-
84864213113
-
Systematic functional prioritization of protein posttranslational modifications
-
doi: 10.1016/j.cell.2012.05.036
-
Beltrao, P., Albanese, V., Kenner, L. R., Swaney, D. L., Burlingame, A., Villen, J.,et al. (2012). Systematic functional prioritization of protein posttranslational modifications. Cell 150, 413-425. doi: 10.1016/j.cell.2012.05.036
-
(2012)
Cell
, vol.150
, pp. 413-425
-
-
Beltrao, P.1
Albanese, V.2
Kenner, L.R.3
Swaney, D.L.4
Burlingame, A.5
Villen, J.6
-
3
-
-
84902031172
-
Evolution and functional cross-talk of protein post-translational modifications
-
doi: 10.1002/msb.201304521
-
Beltrao, P., Bork, P., Krogan, N. J., and Van Noort, V. (2013). Evolution and functional cross-talk of protein post-translational modifications. Mol. Syst. Biol. 9, 714. doi: 10.1002/msb.201304521
-
(2013)
Mol. Syst. Biol.
, vol.9
, pp. 714
-
-
Beltrao, P.1
Bork, P.2
Krogan, N.J.3
Van Noort, V.4
-
4
-
-
0032479179
-
Anatomy of hot spots in protein interfaces
-
doi: 10.1006/jmbi.1998.1843
-
Bogan, A. A., and Thorn, K. S. (1998). Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9. doi: 10.1006/jmbi.1998.1843
-
(1998)
J. Mol. Biol.
, vol.280
, pp. 1-9
-
-
Bogan, A.A.1
Thorn, K.S.2
-
5
-
-
84883454123
-
Structural changes of CFTR R region upon phosphorylation: a plastic platform for intramolecular and intermolecular interactions
-
doi: 10.1111/febs.12422
-
Bozoky, Z., Krzeminski, M., Chong, P. A., and Forman-Kay, J. D. (2013). Structural changes of CFTR R region upon phosphorylation: a plastic platform for intramolecular and intermolecular interactions. FEBS J. 280, 4407-4416. doi: 10.1111/febs.12422
-
(2013)
FEBS J.
, vol.280
, pp. 4407-4416
-
-
Bozoky, Z.1
Krzeminski, M.2
Chong, P.A.3
Forman-Kay, J.D.4
-
6
-
-
77952387813
-
Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding
-
doi: 10.1074/jbc.M110.108167
-
Burke, J. R., Deshong, A. J., Pelton, J. G., and Rubin, S. M. (2010). Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding. J. Biol. Chem. 285, 16286-16293. doi: 10.1074/jbc.M110.108167
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 16286-16293
-
-
Burke, J.R.1
Deshong, A.J.2
Pelton, J.G.3
Rubin, S.M.4
-
7
-
-
84861790525
-
Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control
-
doi: 10.1101/gad.189837.112
-
Burke, J. R., Hura, G. L., and Rubin, S. M. (2012). Structures of inactive retinoblastoma protein reveal multiple mechanisms for cell cycle control. Genes Dev. 26, 1156-1166. doi: 10.1101/gad.189837.112
-
(2012)
Genes Dev.
, vol.26
, pp. 1156-1166
-
-
Burke, J.R.1
Hura, G.L.2
Rubin, S.M.3
-
8
-
-
84890855571
-
Multiple mechanisms for E2F binding inhibition by phosphorylation of the retinoblastoma protein C-terminal domain
-
doi: 10.1016/j.jmb.2013.09.031
-
Burke, J. R., Liban, T. J., Restrepo, T., Lee, H. W., and Rubin, S. M. (2014). Multiple mechanisms for E2F binding inhibition by phosphorylation of the retinoblastoma protein C-terminal domain. J. Mol. Biol. 426, 245-255. doi: 10.1016/j.jmb.2013.09.031
-
(2014)
J. Mol. Biol.
, vol.426
, pp. 245-255
-
-
Burke, J.R.1
Liban, T.J.2
Restrepo, T.3
Lee, H.W.4
Rubin, S.M.5
-
9
-
-
84890566950
-
Phosphorylation of cystic fibrosis transmembrane conductance regulator (CFTR) serine-511 by the combined action of tyrosine kinases and CK2: the implication of tyrosine-512 and phenylalanine-508
-
doi: 10.1007/s00726-013-1613-y
-
Cesaro, L., Marin, O., Venerando, A., Donella-Deana, A., and Pinna, L. A. (2013). Phosphorylation of cystic fibrosis transmembrane conductance regulator (CFTR) serine-511 by the combined action of tyrosine kinases and CK2: the implication of tyrosine-512 and phenylalanine-508. Amino Acids 45, 1423-1429. doi: 10.1007/s00726-013-1613-y
-
(2013)
Amino Acids
, vol.45
, pp. 1423-1429
-
-
Cesaro, L.1
Marin, O.2
Venerando, A.3
Donella-Deana, A.4
Pinna, L.A.5
-
10
-
-
0035123060
-
The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization
-
doi: 10.1038/84995
-
Chacko, B. M., Qin, B., Correia, J. J., Lam, S. S., De Caestecker, M. P., and Lin, K. (2001). The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization. Nat. Struct. Biol. 8, 248-253. doi: 10.1038/84995
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 248-253
-
-
Chacko, B.M.1
Qin, B.2
Correia, J.J.3
Lam, S.S.4
De Caestecker, M.P.5
Lin, K.6
-
11
-
-
84856708226
-
Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl
-
doi: 10.1038/nsmb.2231
-
Dou, H., Buetow, L., Hock, A., Sibbet, G. J., Vousden, K. H., and Huang, D. T. (2012). Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl. Nat. Struct. Mol. Biol. 19, 184-192. doi: 10.1038/nsmb.2231
-
(2012)
Nat. Struct. Mol. Biol.
, vol.19
, pp. 184-192
-
-
Dou, H.1
Buetow, L.2
Hock, A.3
Sibbet, G.J.4
Vousden, K.H.5
Huang, D.T.6
-
12
-
-
0033638454
-
The molecular basis of FHA domain: phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms
-
doi: 10.1016/S1097-2765(00)00114-3
-
Durocher, D., Taylor, I. A., Sarbassova, D., Haire, L. F., Westcott, S. L., Jackson, S. P.,et al. (2000). The molecular basis of FHA domain: phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Mol. Cell. 6, 1169-1182. doi: 10.1016/S1097-2765(00)00114-3
-
(2000)
Mol. Cell.
, vol.6
, pp. 1169-1182
-
-
Durocher, D.1
Taylor, I.A.2
Sarbassova, D.3
Haire, L.F.4
Westcott, S.L.5
Jackson, S.P.6
-
13
-
-
34548736602
-
Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin
-
doi: 10.1529/biophysj.106.095802
-
Espinoza-Fonseca, L. M., Kast, D., and Thomas, D. D. (2007). Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin. Biophys. J. 93, 2083-2090. doi: 10.1529/biophysj.106.095802
-
(2007)
Biophys. J.
, vol.93
, pp. 2083-2090
-
-
Espinoza-Fonseca, L.M.1
Kast, D.2
Thomas, D.D.3
-
14
-
-
51949096545
-
Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin
-
doi: 10.1021/ja803143g
-
Espinoza-Fonseca, L. M., Kast, D., and Thomas, D. D. (2008). Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin. J. Am. Chem. Soc. 130, 12208-12209. doi: 10.1021/ja803143g
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 12208-12209
-
-
Espinoza-Fonseca, L.M.1
Kast, D.2
Thomas, D.D.3
-
15
-
-
66149124079
-
Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2
-
doi: 10.1073/pnas.0811023106
-
Ferreon, J. C., Lee, C. W., Arai, M., Martinez-Yamout, M. A., Dyson, H. J., and Wright, P. E. (2009). Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2. Proc. Natl. Acad. Sci. U.S.A. 106, 6591-6596. doi: 10.1073/pnas.0811023106
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 6591-6596
-
-
Ferreon, J.C.1
Lee, C.W.2
Arai, M.3
Martinez-Yamout, M.A.4
Dyson, H.J.5
Wright, P.E.6
-
16
-
-
77956504709
-
Intrinsic disorder and protein multibinding in domain, terminal, and linker regions
-
doi: 10.1039/c005144f
-
Fong, J. H., and Panchenko, A. R. (2010). Intrinsic disorder and protein multibinding in domain, terminal, and linker regions. Mol. Biosyst. 6, 1821-1828. doi: 10.1039/c005144f
-
(2010)
Mol. Biosyst.
, vol.6
, pp. 1821-1828
-
-
Fong, J.H.1
Panchenko, A.R.2
-
17
-
-
84896734187
-
Functional divergence and evolutionary turnover in mammalian phosphoproteomes
-
doi: 10.1371/journal.pgen.1004062
-
Freschi, L., Osseni, M., and Landry, C. R. (2014). Functional divergence and evolutionary turnover in mammalian phosphoproteomes. PLoS Genet. 10:e1004062. doi: 10.1371/journal.pgen.1004062
-
(2014)
PLoS Genet
, vol.10
-
-
Freschi, L.1
Osseni, M.2
Landry, C.R.3
-
18
-
-
33344455174
-
Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction
-
doi: 10.1016/j.molcel.2006.01.022
-
Furdui, C. M., Lew, E. D., Schlessinger, J., and Anderson, K. S. (2006). Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction. Mol. Cell 21, 711-717. doi: 10.1016/j.molcel.2006.01.022
-
(2006)
Mol. Cell
, vol.21
, pp. 711-717
-
-
Furdui, C.M.1
Lew, E.D.2
Schlessinger, J.3
Anderson, K.S.4
-
19
-
-
84892456405
-
System level dynamics of post-translational modifications
-
doi: 10.1016/j.copbio.2013.12.009
-
Gajadhar, A. S., and White, F. M. (2014). System level dynamics of post-translational modifications. Curr. Opin. Biotechnol. 28C, 83-87. doi: 10.1016/j.copbio.2013.12.009
-
(2014)
Curr. Opin. Biotechnol.
, vol.28 C
, pp. 83-87
-
-
Gajadhar, A.S.1
White, F.M.2
-
20
-
-
79955539577
-
Induced ectopic kinetochore assembly bypasses the requirement for CENP-A nucleosomes
-
doi: 10.1016/j.cell.2011.03.031
-
Gascoigne, K. E., Takeuchi, K., Suzuki, A., Hori, T., Fukagawa, T., and Cheeseman, I. M. (2011). Induced ectopic kinetochore assembly bypasses the requirement for CENP-A nucleosomes. Cell 145, 410-422. doi: 10.1016/j.cell.2011.03.031
-
(2011)
Cell
, vol.145
, pp. 410-422
-
-
Gascoigne, K.E.1
Takeuchi, K.2
Suzuki, A.3
Hori, T.4
Fukagawa, T.5
Cheeseman, I.M.6
-
21
-
-
33646266474
-
Conformational changes in protein loops and helices induced by post-translational phosphorylation
-
doi: 10.1371/journal.pcbi.0020032
-
Groban, E. S., Narayanan, A., and Jacobson, M. P. (2006). Conformational changes in protein loops and helices induced by post-translational phosphorylation. PLoS Comput. Biol. 2:e32. doi: 10.1371/journal.pcbi.0020032
-
(2006)
PLoS Comput. Biol.
, vol.2
-
-
Groban, E.S.1
Narayanan, A.2
Jacobson, M.P.3
-
22
-
-
13644250683
-
Phosphorylation effects on cis/trans isomerization and the backbone conformation of serine-proline motifs: accelerated molecular dynamics analysis
-
doi: 10.1021/ja0446707
-
Hamelberg, D., Shen, T., and Mccammon, J. A. (2005). Phosphorylation effects on cis/trans isomerization and the backbone conformation of serine-proline motifs: accelerated molecular dynamics analysis. J. Am. Chem. Soc. 127, 1969-1974. doi: 10.1021/ja0446707
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 1969-1974
-
-
Hamelberg, D.1
Shen, T.2
Mccammon, J.A.3
-
23
-
-
79956188298
-
Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization
-
doi: 10.1088/1478-3975/8/3/035007
-
Hashimoto, K., Nishi, H., Bryant, S., and Panchenko, A. R. (2011). Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization. Phys. Biol. 8, 035007. doi: 10.1088/1478-3975/8/3/035007
-
(2011)
Phys. Biol.
, vol.8
, pp. 035007
-
-
Hashimoto, K.1
Nishi, H.2
Bryant, S.3
Panchenko, A.R.4
-
24
-
-
35648942123
-
Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture
-
doi: 10.1016/j.molcel.2007.08.023
-
Hassler, M., Singh, S., Yue, W. W., Luczynski, M., Lakbir, R., Sanchez-Sanchez, F.,et al. (2007). Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture. Mol. Cell. 28, 371-385. doi: 10.1016/j.molcel.2007.08.023
-
(2007)
Mol. Cell.
, vol.28
, pp. 371-385
-
-
Hassler, M.1
Singh, S.2
Yue, W.W.3
Luczynski, M.4
Lakbir, R.5
Sanchez-Sanchez, F.6
-
25
-
-
33847696075
-
Receptor tyrosine kinases: mechanisms of activation and signaling
-
doi: 10.1016/j.ceb.2007.02.010
-
Hubbard, S. R., and Miller, W. T. (2007). Receptor tyrosine kinases: mechanisms of activation and signaling. Curr. Opin. Cell Biol 19, 117-123. doi: 10.1016/j.ceb.2007.02.010
-
(2007)
Curr. Opin. Cell Biol
, vol.19
, pp. 117-123
-
-
Hubbard, S.R.1
Miller, W.T.2
-
26
-
-
0037013143
-
The conformational plasticity of protein kinases
-
doi: 10.1016/S0092-8674(02)00741-9
-
Huse, M., and Kuriyan, J. (2002). The conformational plasticity of protein kinases. Cell 109, 275-282. doi: 10.1016/S0092-8674(02)00741-9
-
(2002)
Cell
, vol.109
, pp. 275-282
-
-
Huse, M.1
Kuriyan, J.2
-
27
-
-
2342473198
-
The importance of intrinsic disorder for protein phosphorylation
-
doi: 10.1093/nar/gkh253
-
Iakoucheva, L. M., Radivojac, P., Brown, C. J., O'Connor, T. R., Sikes, J. G., Obradovic, Z.,et al. (2004). The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res. 32, 1037-1049. doi: 10.1093/nar/gkh253
-
(2004)
Nucleic Acids Res.
, vol.32
, pp. 1037-1049
-
-
Iakoucheva, L.M.1
Radivojac, P.2
Brown, C.J.3
O'Connor, T.R.4
Sikes, J.G.5
Obradovic, Z.6
-
28
-
-
42049091009
-
Regulation of the Rad53 protein kinase in signal amplification by oligomer assembly and disassembly
-
doi: 10.4161/cc.7.6.5595
-
Jia-Lin Ma, N., and Stern, D. F. (2008). Regulation of the Rad53 protein kinase in signal amplification by oligomer assembly and disassembly. Cell Cycle 7, 808-817. doi: 10.4161/cc.7.6.5595
-
(2008)
Cell Cycle
, vol.7
, pp. 808-817
-
-
Jia-Lin Ma, N.1
Stern, D.F.2
-
29
-
-
77950872530
-
Bioinformatic and experimental survey of 14-3-3-binding sites
-
doi: 10.1042/BJ20091834
-
Johnson, C., Crowther, S., Stafford, M. J., Campbell, D. G., Toth, R., and Mackintosh, C. (2010). Bioinformatic and experimental survey of 14-3-3-binding sites. Biochem. J. 427, 69-78. doi: 10.1042/BJ20091834
-
(2010)
Biochem. J.
, vol.427
, pp. 69-78
-
-
Johnson, C.1
Crowther, S.2
Stafford, M.J.3
Campbell, D.G.4
Toth, R.5
Mackintosh, C.6
-
30
-
-
0026562948
-
Glycogen phosphorylase: control by phosphorylation and allosteric effectors
-
Johnson, L. N. (1992). Glycogen phosphorylase: control by phosphorylation and allosteric effectors. FASEB J. 6, 2274-2282.
-
(1992)
FASEB J.
, vol.6
, pp. 2274-2282
-
-
Johnson, L.N.1
-
31
-
-
70349330577
-
The regulation of protein phosphorylation
-
doi: 10.1042/BST0370627
-
Johnson, L. N. (2009). The regulation of protein phosphorylation. Biochem. Soc. Trans. 37, 627-641. doi: 10.1042/BST0370627
-
(2009)
Biochem. Soc. Trans.
, vol.37
, pp. 627-641
-
-
Johnson, L.N.1
-
32
-
-
0035413607
-
Structural basis for control by phosphorylation
-
doi: 10.1021/cr000225s
-
Johnson, L. N., and Lewis, R. J. (2001). Structural basis for control by phosphorylation. Chem. Rev. 101, 2209-2242. doi: 10.1021/cr000225s
-
(2001)
Chem. Rev.
, vol.101
, pp. 2209-2242
-
-
Johnson, L.N.1
Lewis, R.J.2
-
33
-
-
84858599263
-
Cbl exposes its RING finger
-
doi: 10.1038/nsmb.2241
-
Kales, S. C., Ryan, P. E., and Lipkowitz, S. (2012). Cbl exposes its RING finger. Nat. Struct. Mol. Biol. 19, 131-133. doi: 10.1038/nsmb.2241
-
(2012)
Nat. Struct. Mol. Biol.
, vol.19
, pp. 131-133
-
-
Kales, S.C.1
Ryan, P.E.2
Lipkowitz, S.3
-
34
-
-
77952395653
-
Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chain
-
doi: 10.1073/pnas.1001941107
-
Kast, D., Espinoza-Fonseca, L. M., Yi, C., and Thomas, D. D. (2010). Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chain. Proc. Natl. Acad. Sci. U.S.A. 107, 8207-8212. doi: 10.1073/pnas.1001941107
-
(2010)
Proc. Natl. Acad. Sci. U.S.A.
, vol.107
, pp. 8207-8212
-
-
Kast, D.1
Espinoza-Fonseca, L.M.2
Yi, C.3
Thomas, D.D.4
-
35
-
-
84890133861
-
Multisite phosphorylation networks as signal processors for Cdk1
-
doi: 10.1038/nsmb.2706
-
Koivomagi, M., Ord, M., Iofik, A., Valk, E., Venta, R., Faustova, I.,et al. (2013). Multisite phosphorylation networks as signal processors for Cdk1. Nat. Struct. Mol. Biol. 20, 1415-1424. doi: 10.1038/nsmb.2706
-
(2013)
Nat. Struct. Mol. Biol.
, vol.20
, pp. 1415-1424
-
-
Koivomagi, M.1
Ord, M.2
Iofik, A.3
Valk, E.4
Venta, R.5
Faustova, I.6
-
36
-
-
84861210634
-
Multisite phosphorylation disrupts arginine-glutamate salt bridge networks required for binding of cytoplasmic linker-associated protein 2 (CLASP2) to end-binding protein 1 (EB1)
-
doi: 10.1074/jbc.M111.316661
-
Kumar, P., Chimenti, M. S., Pemble, H., Schonichen, A., Thompson, O., Jacobson, M. P.,et al. (2012). Multisite phosphorylation disrupts arginine-glutamate salt bridge networks required for binding of cytoplasmic linker-associated protein 2 (CLASP2) to end-binding protein 1 (EB1). J. Biol. Chem. 287, 17050-17064. doi: 10.1074/jbc.M111.316661
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 17050-17064
-
-
Kumar, P.1
Chimenti, M.S.2
Pemble, H.3
Schonichen, A.4
Thompson, O.5
Jacobson, M.P.6
-
37
-
-
71049118572
-
SysPTM: a systematic resource for proteomic research on post-translational modifications
-
doi: 10.1074/mcp.M900030-MCP200
-
Li, H., Xing, X., Ding, G., Li, Q., Wang, C., Xie, L.,et al. (2009). SysPTM: a systematic resource for proteomic research on post-translational modifications. Mol. Cell. Proteomics 8, 1839-1849. doi: 10.1074/mcp.M900030-MCP200
-
(2009)
Mol. Cell. Proteomics
, vol.8
, pp. 1839-1849
-
-
Li, H.1
Xing, X.2
Ding, G.3
Li, Q.4
Wang, C.5
Xie, L.6
-
38
-
-
84885180170
-
Mutations in DNA-binding loop of NFAT5 transcription factor produce unique outcomes on protein-DNA binding and dynamics
-
doi: 10.1021/jp403310a
-
Li, M., Shoemaker, B. A., Thangudu, R. R., Ferraris, J. D., Burg, M. B., and Panchenko, A. R. (2013). Mutations in DNA-binding loop of NFAT5 transcription factor produce unique outcomes on protein-DNA binding and dynamics. J. Phys. Chem. B 117, 13226-13234. doi: 10.1021/jp403310a
-
(2013)
J. Phys. Chem. B
, vol.117
, pp. 13226-13234
-
-
Li, M.1
Shoemaker, B.A.2
Thangudu, R.R.3
Ferraris, J.D.4
Burg, M.B.5
Panchenko, A.R.6
-
39
-
-
51649107040
-
Mechanistic insights into phosphoprotein-binding FHA domains
-
doi: 10.1021/ar700148u
-
Liang, X., and Van Doren, S. R. (2008). Mechanistic insights into phosphoprotein-binding FHA domains. Acc. Chem. Res. 41, 991-999. doi: 10.1021/ar700148u
-
(2008)
Acc. Chem. Res.
, vol.41
, pp. 991-999
-
-
Liang, X.1
Van Doren, S.R.2
-
40
-
-
84864684030
-
Phosphorylation of histone H3 Ser10 establishes a hierarchy for subsequent intramolecular modification events
-
doi: 10.1038/nsmb.2310
-
Liokatis, S., Stutzer, A., Elsasser, S. J., Theillet, F. X., Klingberg, R., Van Rossum, B.,et al. (2012). Phosphorylation of histone H3 Ser10 establishes a hierarchy for subsequent intramolecular modification events. Nat. Struct. Mol. Biol. 19, 819-823. doi: 10.1038/nsmb.2310
-
(2012)
Nat. Struct. Mol. Biol.
, vol.19
, pp. 819-823
-
-
Liokatis, S.1
Stutzer, A.2
Elsasser, S.J.3
Theillet, F.X.4
Klingberg, R.5
Van Rossum, B.6
-
41
-
-
84876035030
-
Deciphering post-translational modification codes
-
doi: 10.1016/j.febslet.2013.01.047
-
Lothrop, A. P., Torres, M. P., and Fuchs, S. M. (2013). Deciphering post-translational modification codes. FEBS Lett. 587, 1247-1257. doi: 10.1016/j.febslet.2013.01.047
-
(2013)
FEBS Lett.
, vol.587
, pp. 1247-1257
-
-
Lothrop, A.P.1
Torres, M.P.2
Fuchs, S.M.3
-
42
-
-
0029916122
-
A human peptidyl-prolyl isomerase essential for regulation of mitosis
-
doi: 10.1038/380544a0
-
Lu, K. P., Hanes, S. D., and Hunter, T. (1996). A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380, 544-547. doi: 10.1038/380544a0
-
(1996)
Nature
, vol.380
, pp. 544-547
-
-
Lu, K.P.1
Hanes, S.D.2
Hunter, T.3
-
43
-
-
0036535975
-
Pinning down proline-directed phosphorylation signaling
-
doi: 10.1016/S0962-8924(02)02253-5
-
Lu, K. P., Liou, Y. C., and Zhou, X. Z. (2002). Pinning down proline-directed phosphorylation signaling. Trends Cell Biol. 12, 164-172. doi: 10.1016/S0962-8924(02)02253-5
-
(2002)
Trends Cell Biol.
, vol.12
, pp. 164-172
-
-
Lu, K.P.1
Liou, Y.C.2
Zhou, X.Z.3
-
44
-
-
84862579690
-
Multisite phosphoregulation of Cdc25 activity refines the mitotic entrance and exit switches
-
doi: 10.1073/pnas.1201366109
-
Lu, L. X., Domingo-Sananes, M. R., Huzarska, M., Novak, B., and Gould, K. L. (2012). Multisite phosphoregulation of Cdc25 activity refines the mitotic entrance and exit switches. Proc. Natl. Acad. Sci. U.S.A. 109, 9899-9904. doi: 10.1073/pnas.1201366109
-
(2012)
Proc. Natl. Acad. Sci. U.S.A.
, vol.109
, pp. 9899-9904
-
-
Lu, L.X.1
Domingo-Sananes, M.R.2
Huzarska, M.3
Novak, B.4
Gould, K.L.5
-
45
-
-
33846630988
-
Strengths of hydrogen bonds involving phosphorylated amino acid side chains
-
doi: 10.1021/ja063019w
-
Mandell, D. J., Chorny, I., Groban, E. S., Wong, S. E., Levine, E., Rapp, C. S.,et al. (2007). Strengths of hydrogen bonds involving phosphorylated amino acid side chains. J. Am. Chem. Soc. 129, 820-827. doi: 10.1021/ja063019w
-
(2007)
J. Am. Chem. Soc.
, vol.129
, pp. 820-827
-
-
Mandell, D.J.1
Chorny, I.2
Groban, E.S.3
Wong, S.E.4
Levine, E.5
Rapp, C.S.6
-
46
-
-
0037032835
-
The protein kinase complement of the human genome
-
doi: 10.1126/science.1075762
-
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002). The protein kinase complement of the human genome. Science 298, 1912-1934. doi: 10.1126/science.1075762
-
(2002)
Science
, vol.298
, pp. 1912-1934
-
-
Manning, G.1
Whyte, D.B.2
Martinez, R.3
Hunter, T.4
Sudarsanam, S.5
-
47
-
-
0037334895
-
One-thousand-and-one substrates of protein kinase CK2?
-
doi: 10.1096/fj.02-0473rev
-
Meggio, F., and Pinna, L. A. (2003). One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17, 349-368. doi: 10.1096/fj.02-0473rev
-
(2003)
FASEB J.
, vol.17
, pp. 349-368
-
-
Meggio, F.1
Pinna, L.A.2
-
48
-
-
84891836984
-
Locking the active conformation of c-Src kinase through the phosphorylation of the activation loop
-
doi: 10.1016/j.jmb.2013.10.001
-
Meng, Y., and Roux, B. (2014). Locking the active conformation of c-Src kinase through the phosphorylation of the activation loop. J. Mol. Biol. 426, 423-435. doi: 10.1016/j.jmb.2013.10.001
-
(2014)
J. Mol. Biol.
, vol.426
, pp. 423-435
-
-
Meng, Y.1
Roux, B.2
-
49
-
-
84864184970
-
Deciphering a global network of functionally associated post-translational modifications
-
doi: 10.1038/msb.2012.31
-
Minguez, P., Parca, L., Diella, F., Mende, D. R., Kumar, R., Helmer-Citterich, M.,et al. (2012). Deciphering a global network of functionally associated post-translational modifications. Mol. Syst. Biol. 8:599. doi: 10.1038/msb.2012.31
-
(2012)
Mol. Syst. Biol.
, vol.8
, pp. 599
-
-
Minguez, P.1
Parca, L.2
Diella, F.3
Mende, D.R.4
Kumar, R.5
Helmer-Citterich, M.6
-
50
-
-
84855283469
-
Coherent conformational degrees of freedom as a structural basis for allosteric communication
-
doi: 10.1371/journal.pcbi.1002301
-
Mitternacht, S., and Berezovsky, I. N. (2011). Coherent conformational degrees of freedom as a structural basis for allosteric communication. PLoS Comput. Biol. 7:e1002301. doi: 10.1371/journal.pcbi.1002301
-
(2011)
PLoS Comput. Biol.
, vol.7
-
-
Mitternacht, S.1
Berezovsky, I.N.2
-
51
-
-
33748456399
-
Analysis of molecular recognition features (MoRFs)
-
doi: 10.1016/j.jmb.2006.07.087
-
Mohan, A., Oldfield, C. J., Radivojac, P., Vacic, V., Cortese, M. S., Dunker, A. K.,et al. (2006). Analysis of molecular recognition features (MoRFs). J. Mol. Biol. 362, 1043-1059. doi: 10.1016/j.jmb.2006.07.087
-
(2006)
J. Mol. Biol.
, vol.362
, pp. 1043-1059
-
-
Mohan, A.1
Oldfield, C.J.2
Radivojac, P.3
Vacic, V.4
Cortese, M.S.5
Dunker, A.K.6
-
52
-
-
0032562180
-
Electrostatics and the membrane association of Src: theory and experiment
-
doi: 10.1021/bi972012b
-
Murray, D., Hermida-Matsumoto, L., Buser, C. A., Tsang, J., Sigal, C. T., Ben-Tal, N.,et al. (1998). Electrostatics and the membrane association of Src: theory and experiment. Biochemistry 37, 2145-2159. doi: 10.1021/bi972012b
-
(1998)
Biochemistry
, vol.37
, pp. 2145-2159
-
-
Murray, D.1
Hermida-Matsumoto, L.2
Buser, C.A.3
Tsang, J.4
Sigal, C.T.5
Ben-Tal, N.6
-
53
-
-
15244339850
-
Site-directed spin labeling reveals a conformational switch in the phosphorylation domain of smooth muscle myosin
-
doi: 10.1073/pnas.0401664102
-
Nelson, W. D., Blakely, S. E., Nesmelov, Y. E., and Thomas, D. D. (2005). Site-directed spin labeling reveals a conformational switch in the phosphorylation domain of smooth muscle myosin. Proc. Natl. Acad. Sci. U.S.A. 102, 4000-4005. doi: 10.1073/pnas.0401664102
-
(2005)
Proc. Natl. Acad. Sci. U.S.A.
, vol.102
, pp. 4000-4005
-
-
Nelson, W.D.1
Blakely, S.E.2
Nesmelov, Y.E.3
Thomas, D.D.4
-
54
-
-
84878702840
-
Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes
-
doi: 10.1039/c3mb25514j
-
Nishi, H., Fong, J. H., Chang, C., Teichmann, S. A., and Panchenko, A. R. (2013). Regulation of protein-protein binding by coupling between phosphorylation and intrinsic disorder: analysis of human protein complexes. Mol. Biosyst. 9, 1620-1626. doi: 10.1039/c3mb25514j
-
(2013)
Mol. Biosyst.
, vol.9
, pp. 1620-1626
-
-
Nishi, H.1
Fong, J.H.2
Chang, C.3
Teichmann, S.A.4
Panchenko, A.R.5
-
55
-
-
82955239916
-
Phosphorylation in protein-protein binding: effect on stability and function
-
doi: 10.1016/j.str.2011.09.021
-
Nishi, H., Hashimoto, K., and Panchenko, A. R. (2011). Phosphorylation in protein-protein binding: effect on stability and function. Structure 19, 1807-1815. doi: 10.1016/j.str.2011.09.021
-
(2011)
Structure
, vol.19
, pp. 1807-1815
-
-
Nishi, H.1
Hashimoto, K.2
Panchenko, A.R.3
-
56
-
-
84873570232
-
CENP-T provides a structural platform for outer kinetochore assembly
-
doi: 10.1038/emboj.2012.348
-
Nishino, T., Rago, F., Hori, T., Tomii, K., Cheeseman, I. M., and Fukagawa, T. (2013). CENP-T provides a structural platform for outer kinetochore assembly. EMBO J. 32, 424-436. doi: 10.1038/emboj.2012.348
-
(2013)
EMBO J.
, vol.32
, pp. 424-436
-
-
Nishino, T.1
Rago, F.2
Hori, T.3
Tomii, K.4
Cheeseman, I.M.5
Fukagawa, T.6
-
57
-
-
84866597525
-
Allosteric post-translational modification codes
-
doi: 10.1016/j.tibs.2012.07.001
-
Nussinov, R., Tsai, C. J., Xin, F., and Radivojac, P. (2012). Allosteric post-translational modification codes. Trends Biochem. Sci. 37, 447-455. doi: 10.1016/j.tibs.2012.07.001
-
(2012)
Trends Biochem. Sci.
, vol.37
, pp. 447-455
-
-
Nussinov, R.1
Tsai, C.J.2
Xin, F.3
Radivojac, P.4
-
58
-
-
33750456519
-
Global, in vivo , and site-specific phosphorylation dynamics in signaling networks
-
doi: 10.1016/j.cell.2006.09.026
-
Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P.,et al. (2006). Global, in vivo , and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648. doi: 10.1016/j.cell.2006.09.026
-
(2006)
Cell
, vol.127
, pp. 635-648
-
-
Olsen, J.V.1
Blagoev, B.2
Gnad, F.3
Macek, B.4
Kumar, C.5
Mortensen, P.6
-
59
-
-
77951644400
-
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis
-
ra3. doi: 10.1126/scisignal.2000475
-
Olsen, J. V., Vermeulen, M., Santamaria, A., Kumar, C., Miller, M. L., Jensen, L. J.,et al. (2010). Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci. Signal. 3:ra3. doi: 10.1126/scisignal.2000475
-
(2010)
Sci. Signal.
, vol.3
-
-
Olsen, J.V.1
Vermeulen, M.2
Santamaria, A.3
Kumar, C.4
Miller, M.L.5
Jensen, L.J.6
-
60
-
-
84859882285
-
Structural role of RKS motifs in chromatin interactions: a molecular dynamics study of HP1 bound to a variably modified histone tail
-
doi: 10.1016/j.bpj.2012.03.030
-
Papamokos, G. V., Tziatzos, G., Papageorgiou, D. G., Georgatos, S. D., Politou, A. S., and Kaxiras, E. (2012). Structural role of RKS motifs in chromatin interactions: a molecular dynamics study of HP1 bound to a variably modified histone tail. Biophys. J. 102, 1926-1933. doi: 10.1016/j.bpj.2012.03.030
-
(2012)
Biophys. J.
, vol.102
, pp. 1926-1933
-
-
Papamokos, G.V.1
Tziatzos, G.2
Papageorgiou, D.G.3
Georgatos, S.D.4
Politou, A.S.5
Kaxiras, E.6
-
61
-
-
34548379387
-
Processive phosphorylation: mechanism and biological importance
-
doi: 10.1016/j.cellsig.2007.06.006
-
Patwardhan, P., and Miller, W. T. (2007). Processive phosphorylation: mechanism and biological importance. Cell. Signal. 19, 2218-2226. doi: 10.1016/j.cellsig.2007.06.006
-
(2007)
Cell. Signal.
, vol.19
, pp. 2218-2226
-
-
Patwardhan, P.1
Miller, W.T.2
-
62
-
-
0035575586
-
SH2 domains, interaction modules and cellular wiring
-
doi: 10.1016/S0962-8924(01)02154-7
-
Pawson, T., Gish, G. D., and Nash, P. (2001). SH2 domains, interaction modules and cellular wiring. Trends Cell Biol. 11, 504-511. doi: 10.1016/S0962-8924(01)02154-7
-
(2001)
Trends Cell Biol.
, vol.11
, pp. 504-511
-
-
Pawson, T.1
Gish, G.D.2
Nash, P.3
-
63
-
-
84891797010
-
Identification of enriched PTM crosstalk motifs from large-scale experimental data sets
-
doi: 10.1021/pr4005579
-
Peng, M., Scholten, A., Heck, A. J., and Van Breukelen, B. (2014). Identification of enriched PTM crosstalk motifs from large-scale experimental data sets. J. Proteome Res. 13, 249-259. doi: 10.1021/pr4005579
-
(2014)
J. Proteome Res.
, vol.13
, pp. 249-259
-
-
Peng, M.1
Scholten, A.2
Heck, A.J.3
Van Breukelen, B.4
-
65
-
-
80052238651
-
Circadian conformational change of the Neurospora clock protein FREQUENCY triggered by clustered hyperphosphorylation of a basic domain
-
doi: 10.1016/j.molcel.2011.06.033
-
Querfurth, C., Diernfellner, A. C., Gin, E., Malzahn, E., Hofer, T., and Brunner, M. (2011). Circadian conformational change of the Neurospora clock protein FREQUENCY triggered by clustered hyperphosphorylation of a basic domain. Mol. Cell 43, 713-722. doi: 10.1016/j.molcel.2011.06.033
-
(2011)
Mol. Cell
, vol.43
, pp. 713-722
-
-
Querfurth, C.1
Diernfellner, A.C.2
Gin, E.3
Malzahn, E.4
Hofer, T.5
Brunner, M.6
-
66
-
-
0031897460
-
Carbon source-dependent phosphorylation of hexokinase PII and its role in the glucose-signaling response in yeast
-
Randez-Gil, F., Sanz, P., Entian, K. D., and Prieto, J. A. (1998). Carbon source-dependent phosphorylation of hexokinase PII and its role in the glucose-signaling response in yeast. Mol. Cell. Biol. 18, 2940-2948.
-
(1998)
Mol. Cell. Biol.
, vol.18
, pp. 2940-2948
-
-
Randez-Gil, F.1
Sanz, P.2
Entian, K.D.3
Prieto, J.A.4
-
67
-
-
84883183501
-
Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response
-
doi: 10.1038/nrm3640
-
Reinhardt, H. C., and Yaffe, M. B. (2013). Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response. Nat. Rev. Mol. Cell Biol. 14, 563-580. doi: 10.1038/nrm3640
-
(2013)
Nat. Rev. Mol. Cell Biol.
, vol.14
, pp. 563-580
-
-
Reinhardt, H.C.1
Yaffe, M.B.2
-
68
-
-
84871513029
-
Deciphering the retinoblastoma protein phosphorylation code
-
doi: 10.1016/j.tibs.2012.10.007
-
Rubin, S. M. (2013). Deciphering the retinoblastoma protein phosphorylation code. Trends Biochem. Sci. 38, 12-19. doi: 10.1016/j.tibs.2012.10.007
-
(2013)
Trends Biochem. Sci.
, vol.38
, pp. 12-19
-
-
Rubin, S.M.1
-
69
-
-
66249102308
-
Multisite protein phosphorylation - from molecular mechanisms to kinetic models
-
doi: 10.1111/j.1742-4658.2009.07027.x
-
Salazar, C., and Hofer, T. (2009). Multisite protein phosphorylation - from molecular mechanisms to kinetic models. FEBS J. 276, 3177-3198. doi: 10.1111/j.1742-4658.2009.07027.x
-
(2009)
FEBS J.
, vol.276
, pp. 3177-3198
-
-
Salazar, C.1
Hofer, T.2
-
70
-
-
0025222214
-
Evidence that the reversible MAO-A inhibitor moclobemide increases prolactin secretion by a serotonergic mechanism in healthy male volunteers
-
doi: 10.1016/0024-3205(90)90529-Z
-
Scheinin, M., Koulu, M., Karhuvaara, S., and Zimmer, R. H. (1990). Evidence that the reversible MAO-A inhibitor moclobemide increases prolactin secretion by a serotonergic mechanism in healthy male volunteers. Life Sci. 47, 1491-1499. doi: 10.1016/0024-3205(90)90529-Z
-
(1990)
Life Sci.
, vol.47
, pp. 1491-1499
-
-
Scheinin, M.1
Koulu, M.2
Karhuvaara, S.3
Zimmer, R.H.4
-
71
-
-
77649117952
-
Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data
-
doi: 10.1186/1745-6150-5-6
-
Schweiger, R., and Linial, M. (2010). Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data. Biol. Direct 5:6. doi: 10.1186/1745-6150-5-6
-
(2010)
Biol. Direct
, vol.5
, pp. 6
-
-
Schweiger, R.1
Linial, M.2
-
72
-
-
0022371434
-
Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin
-
Sellers, J. R. (1985). Mechanism of the phosphorylation-dependent regulation of smooth muscle heavy meromyosin. J. Biol. Chem. 260, 15815-15819.
-
(1985)
J. Biol. Chem.
, vol.260
, pp. 15815-15819
-
-
Sellers, J.R.1
-
73
-
-
33846671062
-
Tuning bulk electrostatics to regulate protein function
-
doi: 10.1016/j.cell.2007.01.018
-
Serber, Z., and Ferrell, J. E. Jr. (2007). Tuning bulk electrostatics to regulate protein function. Cell 128, 441-444. doi: 10.1016/j.cell.2007.01.018
-
(2007)
Cell
, vol.128
, pp. 441-444
-
-
Serber, Z.1
Ferrell Jr., J.E.2
-
74
-
-
24644442164
-
The folding energy landscape and phosphorylation: modeling the conformational switch of the NFAT regulatory domain
-
doi: 10.1096/fj.04-3590hyp
-
Shen, T., Zong, C., Hamelberg, D., Mccammon, J. A., and Wolynes, P. G. (2005). The folding energy landscape and phosphorylation: modeling the conformational switch of the NFAT regulatory domain. FASEB J. 19, 1389-1395. doi: 10.1096/fj.04-3590hyp
-
(2005)
FASEB J.
, vol.19
, pp. 1389-1395
-
-
Shen, T.1
Zong, C.2
Hamelberg, D.3
Mccammon, J.A.4
Wolynes, P.G.5
-
75
-
-
66149108395
-
Molecular dynamics simulations reveal that Tyr-317 phosphorylation reduces Shc binding affinity for phosphotyrosyl residues of epidermal growth factor receptor
-
doi: 10.1016/j.bpj.2008.11.018
-
Suenaga, A., Hatakeyama, M., Kiyatkin, A. B., Radhakrishnan, R., Taiji, M., and Kholodenko, B. N. (2009). Molecular dynamics simulations reveal that Tyr-317 phosphorylation reduces Shc binding affinity for phosphotyrosyl residues of epidermal growth factor receptor. Biophys. J. 96, 2278-2288. doi: 10.1016/j.bpj.2008.11.018
-
(2009)
Biophys. J.
, vol.96
, pp. 2278-2288
-
-
Suenaga, A.1
Hatakeyama, M.2
Kiyatkin, A.B.3
Radhakrishnan, R.4
Taiji, M.5
Kholodenko, B.N.6
-
76
-
-
34250821717
-
Mechanism of coupled folding and binding of an intrinsically disordered protein
-
doi: 10.1038/nature05858
-
Sugase, K., Dyson, H. J., and Wright, P. E. (2007). Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447, 1021-1025. doi: 10.1038/nature05858
-
(2007)
Nature
, vol.447
, pp. 1021-1025
-
-
Sugase, K.1
Dyson, H.J.2
Wright, P.E.3
-
77
-
-
84879613791
-
Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
-
doi: 10.1038/nmeth.2519
-
Swaney, D. L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S.,et al. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nat. Methods 10, 676-682. doi: 10.1038/nmeth.2519
-
(2013)
Nat. Methods
, vol.10
, pp. 676-682
-
-
Swaney, D.L.1
Beltrao, P.2
Starita, L.3
Guo, A.4
Rush, J.5
Fields, S.6
-
78
-
-
0034743516
-
Structure of GSK3Β reveals a primed phosphorylation mechanism
-
doi: 10.1038/89624
-
ter Haar, E., Coll, J. T., Austen, D. A., Hsiao, H. M., Swenson, L., and Jain, J. (2001). Structure of GSK3Β reveals a primed phosphorylation mechanism. Nat. Struct. Biol. 8, 593-596. doi: 10.1038/89624
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 593-596
-
-
Ter Haar, E.1
Coll, J.T.2
Austen, D.A.3
Hsiao, H.M.4
Swenson, L.5
Jain, J.6
-
79
-
-
84879836180
-
The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein
-
doi: 10.1371/journal.pone.0068175
-
Vassall, K. A., Bessonov, K., De Avila, M., Polverini, E., and Harauz, G. (2013). The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein. PLoS ONE 8:e68175. doi: 10.1371/journal.pone.0068175
-
(2013)
PLoS ONE
, vol.8
-
-
Vassall, K.A.1
Bessonov, K.2
De Avila, M.3
Polverini, E.4
Harauz, G.5
-
80
-
-
84896757081
-
The next level of complexity: crosstalk of posttranslational modifications
-
doi: 10.1002/pmic.201300344
-
Venne, A. S., Kollipara, L., and Zahedi, R. P. (2014). The next level of complexity: crosstalk of posttranslational modifications. Proteomics 14, 513-524. doi: 10.1002/pmic.201300344
-
(2014)
Proteomics
, vol.14
, pp. 513-524
-
-
Venne, A.S.1
Kollipara, L.2
Zahedi, R.P.3
-
81
-
-
78651272733
-
From sequence to structural analysis in protein phosphorylation motifs
-
(Landmark Ed.)
-
Via, A., Diella, F., Gibson, T. J., and Helmer-Citterich, M. (2011). From sequence to structural analysis in protein phosphorylation motifs. Front. Biosci. (Landmark Ed.) 16:1261-1275.
-
(2011)
Front. Biosci.
, vol.16
, pp. 1261-1275
-
-
Via, A.1
Diella, F.2
Gibson, T.J.3
Helmer-Citterich, M.4
-
82
-
-
52949123249
-
Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc
-
doi: 10.1073/pnas.0806216105
-
Wang, Z., Gucek, M., and Hart, G. W. (2008). Cross-talk between GlcNAcylation and phosphorylation: site-specific phosphorylation dynamics in response to globally elevated O-GlcNAc. Proc. Natl. Acad. Sci. U.S.A. 105, 13793-13798. doi: 10.1073/pnas.0806216105
-
(2008)
Proc. Natl. Acad. Sci. U.S.A.
, vol.105
, pp. 13793-13798
-
-
Wang, Z.1
Gucek, M.2
Hart, G.W.3
-
83
-
-
84875991401
-
Dual coordination of post translational modifications in human protein networks
-
doi: 10.1371/journal.pcbi.1002933
-
Woodsmith, J., Kamburov, A., and Stelzl, U. (2013). Dual coordination of post translational modifications in human protein networks. PLoS Comput. Biol. 9:e1002933. doi: 10.1371/journal.pcbi.1002933
-
(2013)
PLoS Comput. Biol.
, vol.9
-
-
Woodsmith, J.1
Kamburov, A.2
Stelzl, U.3
-
84
-
-
0032749078
-
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
-
doi: 10.1006/jmbi.1999.3110
-
Wright, P. E., and Dyson, H. J. (1999). Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331. doi: 10.1006/jmbi.1999.3110
-
(1999)
J. Mol. Biol.
, vol.293
, pp. 321-331
-
-
Wright, P.E.1
Dyson, H.J.2
-
85
-
-
84869387778
-
Post-translational modifications induce significant yet not extreme changes to protein structure
-
doi: 10.1093/bioinformatics/bts541
-
Xin, F., and Radivojac, P. (2012). Post-translational modifications induce significant yet not extreme changes to protein structure. Bioinformatics 28, 2905-2913. doi: 10.1093/bioinformatics/bts541
-
(2012)
Bioinformatics
, vol.28
, pp. 2905-2913
-
-
Xin, F.1
Radivojac, P.2
-
86
-
-
0031470652
-
The structural basis for 14-3-3: phosphopeptide binding specificity
-
doi: 10.1016/S0092-8674(00)80487-0
-
Yaffe, M. B., Rittinger, K., Volinia, S., Caron, P. R., Aitken, A., Leffers, H.,et al. (1997). The structural basis for 14-3-3: phosphopeptide binding specificity. Cell 91, 961-971. doi: 10.1016/S0092-8674(00)80487-0
-
(1997)
Cell
, vol.91
, pp. 961-971
-
-
Yaffe, M.B.1
Rittinger, K.2
Volinia, S.3
Caron, P.R.4
Aitken, A.5
Leffers, H.6
-
87
-
-
84866689134
-
Cell cycle regulation by the intrinsically disordered proteins p21 and p27
-
doi: 10.1042/BST20120092
-
Yoon, M. K., Mitrea, D. M., Ou, L., and Kriwacki, R. W. (2012). Cell cycle regulation by the intrinsically disordered proteins p21 and p27. Biochem. Soc. Trans. 40, 981-988. doi: 10.1042/BST20120092
-
(2012)
Biochem. Soc. Trans.
, vol.40
, pp. 981-988
-
-
Yoon, M.K.1
Mitrea, D.M.2
Ou, L.3
Kriwacki, R.W.4
-
88
-
-
78651323535
-
Phospho3D 2.0: an enhanced database of three-dimensional structures of phosphorylation sites
-
doi: 10.1093/nar/gkq936
-
Zanzoni, A., Carbajo, D., Diella, F., Gherardini, P. F., Tramontano, A., Helmer-Citterich, M.,et al. (2011). Phospho3D 2.0: an enhanced database of three-dimensional structures of phosphorylation sites. Nucleic Acids Res. 39, D268-D271. doi: 10.1093/nar/gkq936
-
(2011)
Nucleic Acids Res.
, vol.39
-
-
Zanzoni, A.1
Carbajo, D.2
Diella, F.3
Gherardini, P.F.4
Tramontano, A.5
Helmer-Citterich, M.6
|