about
Life in a crowded worldProtein folding: then and nowPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)What macromolecular crowding can do to a proteinStructural analysis of Bacillus subtilis SPP1 phage helicase loader protein G39PStructural Basis for the Interaction of Unstructured Neuron Specific Substrates Neuromodulin and Neurogranin with CalmodulinStructure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowdingThe Helicobacter pylori anti-sigma factor FlgM is predominantly cytoplasmic and cooperates with the flagellar basal body protein FlhAGlobPlot: Exploring protein sequences for globularity and disorderIn-cell NMR: an emerging approach for monitoring metal-related events in living cells.Denatured state structural property determines protein stabilization by macromolecular crowding: a thermodynamic and structural approach.A network-based analysis of polyanion-binding proteins utilizing yeast protein arrays.The unfoldomics decade: an update on intrinsically disordered proteins.Understanding protein non-folding.Molecular Effects of Concentrated Solutes on Protein Hydration, Dynamics, and Electrostatics.Macromolecular and Small Molecular Crowding Have Similar Effects on α-Synuclein Structure.A cell is more than the sum of its (dilute) parts: A brief history of quinary structure.Protein interactions in the Escherichia coli cytosol: an impediment to in-cell NMR spectroscopy.Impact of macromolecular crowding on DNA replication.Glutamic acid-rich proteins of rod photoreceptors are natively unfolded.Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomesFlexibility of the cytoplasmic domain of the phototaxis transducer II from Natronomonas pharaonis.Protein (19)F NMR in Escherichia coliSoft interactions and crowding.Structural disorder within Henipavirus nucleoprotein and phosphoprotein: from predictions to experimental assessment.A model of intracellular organization.Self-organization and regulation of intrinsically disordered proteins with folded N-termini.In-cell NMR in E. coli to monitor maturation steps of hSOD1.Volume exclusion and soft interaction effects on protein stability under crowded conditions.Mechanism for pH-dependent gene regulation by amino-terminus-mediated homooligomerization of Bacillus subtilis anti-trp RNA-binding attenuation protein.Temperature dependence of protein folding kinetics in living cells.DisProt: a database of protein disorder.Protein disorder in plants: a view from the chloroplast.Visualizing transient dark states by NMR spectroscopy.Effects of molecular crowding on the dynamics of intrinsically disordered proteins.Intrinsic disorder in scaffold proteins: getting more from lessExtraordinarily slow binding of guanosine to the Tetrahymena group I ribozyme: implications for RNA preorganization and functionQuantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes.Macromolecular crowding fails to fold a globular protein in cellsThe transcriptional repressor domain of Gli3 is intrinsically disordered
P2860
Q24537094-18955617-7E8F-46EA-B7AA-E28B9E9A2BF8Q24671711-E68A5A3E-149F-4FB3-8A00-2F8FEE73A46BQ26823798-EA70CEFB-966E-4C0A-887B-D5E714339E32Q27012942-76E06151-9B8B-4A1A-A033-67307C873077Q27640497-745BC9B0-9B0F-4678-BC2A-EC96900E9CA4Q27676705-30EA5D78-72F2-4239-866F-5F35677307E0Q28294869-87F38523-34D4-4A41-B2C5-845A96146B0DQ28484798-A1E3CC13-4AA8-4EF0-961D-807572089FC7Q29615737-F09ED7BE-BE6D-4B76-8521-494F87A36930Q30355333-15E9BE52-D057-4E43-AB2D-60A5B66F6E35Q30355901-7FD85AF5-38E3-4F6C-B964-A716028DBFD3Q30356926-03646A0D-D94C-4922-AD2F-EFD209395037Q30372413-5BABB3AD-DD77-4D46-BC2B-5414FDE65D67Q30385084-B9D68C92-E881-420C-8B7C-E6A706772BB5Q30392206-5E88E767-D681-450F-B64D-9DCF7BD9F5F1Q30395345-B84C72D2-490A-4AA4-BE65-1D98F8867705Q30396491-D9DBC80E-A0CD-4FA8-B6E7-F0A3B180428FQ30401276-2338728E-9A44-44D8-86E8-E2428036B854Q30428470-EC48E45F-402B-453B-9D1E-095CFA4C2310Q33226936-060003B4-BE49-4C6C-B856-BD4F05132148Q33252616-FE94659E-0DB7-49FE-AA40-9123B646DEAAQ33602520-A8A71B06-3192-4521-B55B-B13C69DE36DEQ33626348-B8AA969C-ADFC-40E0-B867-4A60E010F8F0Q33639701-89905DAD-7CB9-4E89-AF49-AC62EB84A576Q33640276-45976BCA-FAF0-4A03-B5FA-CA33AC25CE63Q33771099-9971ADC7-93AC-49B0-8837-558E32E4D9EFQ33828313-8770BAC8-5B68-4AFD-B340-5BBC1B56E105Q34009391-A768E93F-B206-4280-90D4-C37E539CF469Q34082447-F9C8CE70-A7FB-4B54-8569-C03B7D372AF3Q34100360-5049A217-3EC4-4FF3-A60C-C09B3E873D70Q34292102-283325D2-4588-428F-8400-B3064EAA6F0BQ34341031-088DA1A5-457E-4092-9FDF-390309914D4DQ34412990-AF6BD1E7-0ADA-472F-B971-302A415DFE5AQ34464287-681FC0D3-D955-4847-8213-36FE96E2769CQ34493912-9939E93D-CD6F-4502-9280-92736209D140Q34594105-47A534BD-B27C-4002-AB71-EBF23A0325DAQ34804941-ADA89154-7D35-43F2-87A0-4AD66166C2EAQ34872036-4C7EB795-91BC-41EC-8C7D-97F4BEFAD172Q35007584-F75EB555-A116-42FE-941A-A55A30E9B7BEQ35023014-9CAEC3F9-6393-494D-B7D1-C0AACFFA804B
P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
FlgM gains structure in living cells.
@ast
FlgM gains structure in living cells.
@en
FlgM gains structure in living cells.
@nl
type
label
FlgM gains structure in living cells.
@ast
FlgM gains structure in living cells.
@en
FlgM gains structure in living cells.
@nl
prefLabel
FlgM gains structure in living cells.
@ast
FlgM gains structure in living cells.
@en
FlgM gains structure in living cells.
@nl
P2093
P2860
P356
P1476
FlgM gains structure in living cells.
@en
P2093
Chetan N Patel
Gary J Pielak
Gregory B Young
Matthew M Dedmon
P2860
P304
12681-12684
P356
10.1073/PNAS.202331299
P407
P577
2002-09-23T00:00:00Z