(Q42912184)

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Label-free screening of drug-protein interactions by time-resolved Fourier transform infrared spectroscopic assays exemplified by Ras interactions

scientific article published on September 2010

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scholarly article

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Europe PubMed Central

PubMed publication ID

11 November 2017

Label-free screening of drug-protein interactions by time-resolved Fourier transform infrared spectroscopic assays exemplified by Ras interactions (English)

1 reference

Europe PubMed Central

PubMed publication ID

11 November 2017

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infrared spectroscopy

1 reference

based on heuristic

inferred from title

Carsten Kötting

1

1 reference

Europe PubMed Central

PubMed publication ID

11 November 2017

5

object named as

Klaus Gerwert

1 reference

Europe PubMed Central

PubMed publication ID

11 November 2017

2

object named as

Yan Suveyzdis

1 reference

Europe PubMed Central

PubMed publication ID

11 November 2017

Nils Metzler-Nolte

4

object named as

Nils Metzler-Nolte

1 reference

Europe PubMed Central

PubMed publication ID

11 November 2017

author name string

Ravi S Bojja

3

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Europe PubMed Central

PubMed publication ID

11 November 2017

publication date

1 September 2010

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Europe PubMed Central

PubMed publication ID

11 November 2017

Applied Spectroscopy

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Europe PubMed Central

PubMed publication ID

11 November 2017

64

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Europe PubMed Central

PubMed publication ID

11 November 2017

9

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Europe PubMed Central

PubMed publication ID

11 November 2017

967-972

1 reference

Europe PubMed Central

PubMed publication ID

11 November 2017

Proteins in action monitored by time-resolved FTIR spectroscopy

1 reference

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Targeting RAS signalling pathways in cancer therapy

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The Ras superfamily at a glance

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GEFs and GAPs: critical elements in the control of small G proteins

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1 reference

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The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants

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The guanine nucleotide-binding switch in three dimensions

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Dynamic properties of the Ras switch I region and its importance for binding to effectors

1 reference

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A phosphoryl transfer intermediate in the GTPase reaction of Ras in complex with its GTPase-activating protein

1 reference

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The GAP arginine finger movement into the catalytic site of Ras increases the activation entropy

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Hyperactive Ras in developmental disorders and cancer

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Prospects for anti-ras drugs

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Empirical rules facilitate the search for binding sites on protein surfaces

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Inhibitors of Ras/Raf-1 interaction identified by two-hybrid screening revert Ras-dependent transformation phenotypes in human cancer cells.

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Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase

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New Photoactivated Protecting Groups. 6.p-Hydroxyphenacyl: A Phototrigger for Chemical and Biochemical Probes1,2

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Time-resolved FTIR studies of the GTPase reaction of H-ras p21 reveal a key role for the beta-phosphate

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21 January 2018

Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy

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A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates

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X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp

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21 January 2018

Ras catalyzes GTP hydrolysis by shifting negative charges from gamma- to beta-phosphate as revealed by time-resolved FTIR difference spectroscopy

1 reference

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21 January 2018

Lupeol, a fruit and vegetable based triterpene, induces apoptotic death of human pancreatic adenocarcinoma cells via inhibition of Ras signaling pathway.

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Role of the arginine finger in Ras.RasGAP revealed by QM/MM calculations

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Unravelling the mechanism of dual-specificity GAPs

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Insight into catalysis of a unique GTPase reaction by a combined biochemical and FTIR approach

1 reference

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Surface Change of Ras Enabling Effector Binding Monitored in Real Time at Atomic Resolution

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Time-resolved FTIR studies provide activation free energy, activation enthalpy and activation entropy for GTPase reactions

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Systematic approach to group-specific isotopic labeling of proteins for vibrational spectroscopy

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Identifiers

10.1366/000370210792434341

1 reference

Europe PubMed Central

PubMed publication ID

11 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

11 November 2017

ResearchGate publication ID

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