Optimization and stabilization of Rho small GTPase proteins for solution NMR studies: The case of Rnd1.

scientific article published on November 2011

Optimization and stabilization of Rho small GTPase proteins for solution NMR studies: The case of Rnd1. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.4161/SGTP.19257
P8608Fatcat IDrelease_aqmydbqcgvbvfm355qiijie3zm
P932PMC publication ID3337157
P698PubMed publication ID22545226
P5875ResearchGate publication ID224868832

P2093author name stringMatthias Buck
Shufen Cao
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A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesionQ24321771
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Thermodynamic characterization of two homologous protein complexes: associations of the semaphorin receptor plexin-B1 RhoGTPase binding domain with Rnd1 and active Rac1.Q42606532
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His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectorsQ58008654
The button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMRQ73924705
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P433issue6
P407language of work or nameEnglishQ1860
P304page(s)295-304
P577publication date2011-11-01
P1433published inSmall GTPases (journal)Q15709529
P1476titleOptimization and stabilization of Rho small GTPase proteins for solution NMR studies: The case of Rnd1.
P478volume2

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cites work (P2860)
Q39614422Backbone assignment and secondary structure of Rnd1, an unusual Rho family small GTPase
Q51359776Characterizing Plexin GTPase Interactions Using Gel Filtration, Surface Plasmon Resonance Spectrometry, and Isothermal Titration Calorimetry.
Q48875568STI1 antagonizes cytoskeleton collapse mediated by small GTPase Rnd1 and regulates neurite growth.

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