271 results on '"Dosztányi, Zsuzsanna"'
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52. How mutations of intrinsically disordered protein regions can drive cancer
53. Analyzing Protein Disorder with IUPred2A
54. Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins
55. ANCHOR: web server for predicting protein binding regions in disordered proteins
56. Integron-associated Mobile Gene Cassettes Code for Folded Proteins: The Structure of Bal32a, a New Member of the Adaptable α+β Barrel Family
57. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
58. TMDET: web server for detecting transmembrane regions of proteins by using their 3D coordinates
59. PDB_TM: selection and membrane localization of transmembrane proteins in the protein data bank
60. DisProt: intrinsic protein disorder annotation in 2020
61. Transmembrane proteins in the Protein Data Bank: identification and classification
62. Servers for sequence–structure relationship analysis and prediction
63. SCide: identification of stabilization centers in proteins
64. Amino acid similarity matrices based on force fields
65. DisProt: intrinsic protein disorder annotation in 2020
66. PhaSePro: the database of proteins driving liquid–liquid phase separation
67. Large‐Scale Analysis of Redox‐Sensitive Conditionally Disordered Protein Regions Reveals Their Widespread Nature and Key Roles in High‐Level Eukaryotic Processes
68. MobiDB 3.0: More annotations for intrinsic disorder, conformational diversity and interactions in proteins
69. The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes.
70. DisProt 7.0: a major update of the database of disordered proteins
71. Corrigendum: DisProt 7.0: a major update of the database of disordered proteins
72. PhaSePro: the database of proteins driving liquid–liquid phase separation.
73. Large-scale analysis of redox-sensitive conditionally disordered protein regions reveal their widespread nature and key roles in high-level eukaryotic processes
74. IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding
75. Új lineáris motívumok azonosítása bioinformatikai módszerekkel az LC8 fehérje kölcsönhatási hálózatában
76. Additional file 1: of Systematic analysis of somatic mutations driving cancer: uncovering functional protein regions in disease development
77. Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway
78. Prediction of protein disorder based on IUPred
79. MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins
80. Interplay between folding and binding modulates protein sequences, structures, functions and regulation
81. DIBS: a repository of disordered binding sites mediating interactions with ordered proteins
82. A comprehensive assessment of long intrinsic protein disorder from the DisProt database
83. Degrons in cancer
84. MobiDB-lite: fast and highly specific consensus prediction of intrinsic disorder in proteins
85. DisProt 7.0: a major update of the database of disordered proteins
86. InterPro in 2017—beyond protein family and domain annotations
87. Systematic analysis of somatic mutations driving cancer: uncovering functional protein regions in disease development
88. What’s in a name? Why these proteins are intrinsically disordered
89. A comprehensive assessment of long intrinsic protein disorder from the DisProt database.
90. The N-Terminal Intrinsically Disordered Domain of Mgm101p Is Localized to the Mitochondrial Nucleoid
91. Prediction and Analysis of Intrinsically Disordered Proteins.
92. The N-Terminal Intrinsically Disordered Domain of Mgm101p Is Localized to the Mitochondrial Nucleoid
93. D2P2: database of disordered protein predictions
94. Disordered Binding Regions and Linear Motifs—Bridging the Gap between Two Models of Molecular Recognition
95. Is there a biological cost of protein disorder? Analysis of cancer-associated mutations
96. DIBS: a repository of disordered binding sites mediating interactions with ordered proteins.
97. Proteins with Complex Architecture as Potential Targets for Drug Design: A Case Study of Mycobacterium tuberculosis
98. The expanding view of protein–protein interactions: complexes involving intrinsically disordered proteins
99. Prediction of Protein Binding Regions in Disordered Proteins
100. Disorder and Sequence Repeats in Hub Proteins and Their Implications for Network Evolution
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