about
Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTppMessing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer?Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutationsMolecular basis of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2The structure and interactions of the proline-rich domain of ASPP2A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutantsAxin cancer mutants form nanoaggregates to rewire the Wnt signaling networkCritical scaffolding regions of the tumor suppressor Axin1 are natively unfoldedIts substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.The conserved helix C region in the superfamily of interferon-gamma /interleukin-10-related cytokines corresponds to a high-affinity binding site for the HSP70 chaperone DnaK.Studying protein-protein interactions using peptide arrays.Production and purification of human Hsp90β in Escherichia coli.Novel Hsp90 partners discovered using complementary proteomic approaches.Hsp90 structure and function studied by NMR spectroscopy.The central region of HDM2 provides a second binding site for p53.Wnt/β-catenin signaling requires interaction of the Dishevelled DEP domain and C terminus with a discontinuous motif in FrizzledSulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90.Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria.Hsp90 interaction with clients.A script to highlight hydrophobicity and charge on protein surfaces.Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.3D DOSY-TROSY to determine the translational diffusion coefficient of large protein complexes.The vertebrate mitotic checkpoint protein BUBR1 is an unusual pseudokinase.Picky Hsp90-Every Game with Another Mate.Correlation of levels of folded recombinant p53 in escherichia coli with thermodynamic stability in vitro.Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones.Dancing with the Diva: Hsp90-Client Interactions.MAP7 family proteins regulate kinesin-1 recruitment and activationModulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic archMultistep mechanism of substrate binding determines chaperone activity of Hsp70Binding specificity of an alpha-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domainExpressed protein ligation for a large dimeric proteinHsp90 Breaks the Deadlock of the Hsp70 Chaperone SystemThe mechanism of Hsp90-induced oligomerizaton of TauRecombinant production and purification of the human protein TauArginine π-stacking drives binding to fibrils of the Alzheimer protein TauBehind closed gates - chaperones and charged residues determine protein fate
P50
Q21030644-18E80837-2052-4DB1-A138-13EF0E02A941Q21245770-8AC48875-3AE0-4784-96C0-D9F4620BF310Q21559553-1D27B3DE-2462-43FD-92FE-FEF88E691A54Q24336091-979DD295-1FCA-49C8-BD88-21EB3098ACE3Q24336683-846F56CE-B2E0-4001-96C0-FEC8985952F6Q24530763-FD201C07-02D8-4602-88BC-B93A7D5DA633Q28274105-FECED889-F77C-4F6D-873C-0EEF2001C367Q28298690-F01C0AE5-62F0-4165-94C1-B9098B98BC66Q28354756-259AA77B-ED9E-427B-8ADD-E47DA515D91FQ31049426-ED371CA0-46FD-4534-B0A7-EA4F2F781D4BQ33795866-8D0D0794-4D6B-4F13-A2F2-6551462C3238Q33834707-076E8A0E-7885-40AF-B787-6727BC1506FDQ33838809-509AB6F2-7A3A-428D-9672-4A2647A225DCQ34239529-1CD64EC0-0D3C-464D-B685-843755FAB0F6Q34335012-1EB2FC92-1D90-4E35-AFFE-BBE1842EE479Q35887244-82CC72C8-A482-4827-80D5-4355A7FAF5E8Q36066968-0658B322-E601-41B4-9E10-B7351B835E80Q36795860-AC8EEF29-B388-4C1B-B308-ED7002E55FD4Q38314630-F18834B4-582D-492F-ADDC-040B975317C0Q42005799-B9D71DE1-1EF2-4F84-9B99-18931071FA8CQ43589335-09D84345-3FB9-4861-BDE7-FEC4C679D82BQ46603832-D2E47833-0F9D-4A8A-8F36-0B67714953EDQ46991397-A2F1FE93-FD89-4129-B7C0-E1F9F1445AF9Q47761740-0798311D-F733-4F3F-8FEE-128DA101DF31Q50673396-5FBBDAA6-754A-4AEE-9304-62073A2D8F6FQ54414189-B5A17442-101B-4ED6-B27B-EA9F21937EB0Q54978659-8CF7A101-33EA-4992-8DCC-FAD80CF64C75Q64295769-E2AB1FC8-7A03-4BF4-83BB-47EF307EAD1DQ73220607-8AA910FA-2397-41C5-AA03-4EFD70E68154Q73943514-BFFC5DB4-75DB-40E3-B3FD-615A839C07F3Q79358875-34850C6E-C97C-4ED5-9B3F-6589D1F5068CQ83447411-0CF7E286-45D3-4417-937D-80F7FD761129Q88506523-7C7BE111-6251-4EC6-85DE-AD123A6F0FE3Q90578686-63FEAD6D-8123-4748-81E0-3836BCB3D19FQ91549713-3E128B5A-AF33-4F8B-8098-046215C0E7E9Q93039143-9044A6FA-1618-4A94-AC0A-33DBA2D275D3Q94462998-64F50898-B046-4FFD-9395-4D0CD0D4699F
P50
description
Forscher
@de
investigador
@es
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
研究者
@zh
name
Stefan Rüdiger
@ast
Stefan Rüdiger
@en
Stefan Rüdiger
@es
Stefan Rüdiger
@nl
type
label
Stefan Rüdiger
@ast
Stefan Rüdiger
@en
Stefan Rüdiger
@es
Stefan Rüdiger
@nl
prefLabel
Stefan Rüdiger
@ast
Stefan Rüdiger
@en
Stefan Rüdiger
@es
Stefan Rüdiger
@nl
P108
P106
P1153
7005538118
P21
P31
P496
0000-0002-1807-2972