Works matching IS 03005127 AND DT 2012 AND VI 40 AND IP 5
Results: 40
Pharmacological inhibition of LRRK2 cellular phosphorylation sites provides insight into LRRK2 biology.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1158, doi. 10.1042/BST20120137
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The importance of Wnt signalling for neurodegeneration in Parkinson's disease.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1123, doi. 10.1042/BST20120122
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LRRK2 and autophagy: a common pathway for disease.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1147, doi. 10.1042/BST20120126
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A link between LRRK2, autophagy and NAADP-mediated endolysosomal calcium signallinga.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1140, doi. 10.1042/BST20120138
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An emerging role for LRRK2 in the immune system.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1134, doi. 10.1042/BST20120119
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Possible involvement of the relationship of LRRK2 and autophagy in Parkinson's disease.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1129, doi. 10.1042/BST20120095
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Cellular reprogramming: a new approach to modelling Parkinson's disease.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1152, doi. 10.1042/BST20120159
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Analysis of LRRK2 accessory repeat domains: prediction of repeat length, number and sites of Parkinson's disease mutations.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1086, doi. 10.1042/BST20120088
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Presynaptic dysfunction in Parkinson's disease: a focus on LRRK2.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1111, doi. 10.1042/BST20120124
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Phosphorylation of LRRK2: from kinase to substrate.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1102, doi. 10.1042/BST20120128
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Human leucine-rich repeat kinase 1 and 2: intersecting or unrelated functions?
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1095, doi. 10.1042/BST20120123
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MASL1: a neglected ROCO protein.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1090, doi. 10.1042/BST20120127
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LRRK2 and vesicle trafficking.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1117, doi. 10.1042/BST20120117
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Insights into LRRK2 function and dysfunction from transgenic and knockout rodent models.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1080, doi. 10.1042/BST20120151
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LRRK2 GTPase dysfunction in the pathogenesis of Parkinson's disease.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1074, doi. 10.1042/BST20120093
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Cellular effects of LRRK2 mutations.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1070, doi. 10.1042/BST20120165
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The GTPase function of LRRK2.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1063, doi. 10.1042/BST20120133
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Role of LRRK2 kinase activity in the pathogenesis of Parkinson's disease.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1058, doi. 10.1042/BST20120054
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Biochemical and functional characterization of the ROC domain of DAPK establishes a new paradigm of GTP regulation in ROCO proteins.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1052, doi. 10.1042/BST20120155
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The synaptic function of LRRK2.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1047, doi. 10.1042/BST20120113
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Genetic analysis of Parkinson's disease-linked leucine-rich repeat kinase 2.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1042, doi. 10.1042/BST20120112
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Deciphering the function of leucine-rich repeat kinase 2 and targeting its dysfunction in disease.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1039, doi. 10.1042/BST20120178
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Evolutionary selection for protein aggregation.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1032, doi. 10.1042/BST20120160
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Structures and interactions in 'bottlebrush' neurofilaments: the role of charged disordered proteins in forming hydrogel networks.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1027, doi. 10.1042/BST20120101
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Intrinsic disorder in proteins: a challenge for (un)structural biology met by ion mobility-mass spectrometry.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1021, doi. 10.1042/BST20120125
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Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1014, doi. 10.1042/BST20120171
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Native disorder mediates binding of dynein to NudE and dynactin.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1009, doi. 10.1042/BST20120180
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Regulation of protein phosphatase 1 by intrinsically disordered proteins.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 969, doi. 10.1042/BST20120094
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Diverse functional manifestations of intrinsic structural disorder in molecular chaperones.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 963, doi. 10.1042/BST20120108
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Mechanisms of small-molecule binding to intrinsically disordered proteins.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1004, doi. 10.1042/BST20120086
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Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 989, doi. 10.1042/BST20120187
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Cell cycle regulation by the intrinsically disordered proteins p21 and p27.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 981, doi. 10.1042/BST20120092
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Interplay between allostery and intrinsic disorder in an ensemble.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 975, doi. 10.1042/BST20120163
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LEA proteins: IDPs with versatile functions in cellular dehydration tolerance.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 1000, doi. 10.1042/BST20120109
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An intrinsically disordered protein, CP12: jack of all trades and master of the Calvin cycle.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 995, doi. 10.1042/BST20120097
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Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 955, doi. 10.1042/BST20120149
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Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 950, doi. 10.1042/BST20120096
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Intrinsically disordered proteins: administration not executive.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 945, doi. 10.1042/BST20120188
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Synthesis of post-translationally modified proteins.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 929, doi. 10.1042/BST20120144
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Development of inhibitors as research tools for carbohydrate-processing enzymes.
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- Biochemical Society Transactions, 2012, v. 40, n. 5, p. 913, doi. 10.1042/BST20120201
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