Search results for: Gordon C. K. Roberts

Items from 1 to 17 out of 17 results

chapter

Electron Transfer Partners of Cytochrome P450

Mark J. I. Paine, Nigel S. Scrutton, Andrew W. Munro, Aldo Gutierrez, more

Cytochrome P450 > 115-148

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Complete ¹H, ¹⁵N and ¹³C resonance assignments of Bacillus cereus metallo-β-lactamase and its complex with the inhibitor R-thiomandelic acid

Andreas Ioannis Karsisiotis, Christian Damblon, Gordon C. K. Roberts

Biomolecular NMR Assignments > 2014 > 8 > 2 > 313-318

β-Lactamases inactivate β-lactam antibiotics by hydrolysis of their endocyclic β-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo-β-lactamase enzymes are of particular concern since they are located on highly transmissible plasmids and have a broad spectrum of activity against almost all β-lactam antibiotics. We present here essentially...

article

Detection of a Protein Conformational Equilibrium by Electrospray Ionisation‐Ion Mobility‐Mass Spectrometry

Matthew Jenner, Jacqueline Ellis, Wei‐Cheng Huang, Emma Lloyd Raven, more

Angewandte Chemie > 123 > 36 > 8441 - 8444

In der Gasphase wurden mithilfe der Ionenmobilitätsspektrometrie Hinweise auf kompakte und gestreckte Formen der Cytochrom‐P450‐Reduktase gefunden, von denen man glaubt, dass sie in Lösung im dynamischen Gleichgewicht vorliegen. Der Anteil der beiden Konformationen (siehe Bild) kann durch die Ionenstärke der Elektrospray‐Lösung beeinflusst werden.

article

Detection of a Protein Conformational Equilibrium by Electrospray Ionisation‐Ion Mobility‐Mass Spectrometry

Matthew Jenner, Jacqueline Ellis, Wei‐Cheng Huang, Emma Lloyd Raven, more

Angewandte Chemie International Edition > 50 > 36 > 8291 - 8294

Conforming to convention: Evidence for compact and extended forms of cytochrome P450 reductase, believed to exist in dynamic equilibrium in solution, is found in the gas phase by using ion mobility spectrometry. The relative abundance of the two conformations (see picture) can be influenced by the ionic strength of the solution from which they are electrosprayed.

article

Structural and biophysical properties of the integrin-associated cytoskeletal protein talin

Gordon C. K. Roberts, David R. Critchley

Biophysical Reviews > 2009 > 1 > 2 > 61-69

Talin is a large cytoskeletal protein (2541 amino acid residues) which plays a key role in integrin-mediated events that are crucial for cell adhesion, migration, proliferation and survival. This review summarises recent work on the structure of talin and on some of the structurally better defined interactions with other proteins. The N-terminal talin head (approx. 50 kDa) consists of an atypical...

article

NMR assignment of the C-terminal actin-binding domain of talin

Benjamin T. Goult, Alexandre R. Gingras, Neil Bate, Gordon C. K. Roberts, more

Biomolecular NMR Assignments > 2008 > 2 > 1 > 17-19

Talin is a large dimeric 270 kDa adapter protein which binds the cytoplasmic face of a subset of integrin β-subunits and couples them to the actin cytoskeleton. Here we report the near complete ¹⁵N, ¹³C and ¹H chemical shift assignments for the C-terminal actin-binding domain.

article

Structural and Dynamic Characterization of a Vinculin Binding Site in the Talin Rod ^† ^, ^‡

Alexandre R. Gingras, Klaus-Peter Vogel, Heinz-Jürgen Steinhoff, Wolfgang H. Ziegler, more

Biochemistry > 2006 > 45 > 6 > 1805 - 1817

article

Validation of Model of Cytochrome P450 2D6: An in Silico Tool for Predicting Metabolism and Inhibition

Carol A. Kemp, Jack U. Flanagan, Annamaria J. van Eldik, Jean-Didier Maréchal, more

Journal of Medicinal Chemistry > 2004 > 47 > 22 > 5340 - 5346

article

Synthesis of a Simplified Bryostatin C-Ring Analogue That Binds to the CRD2 of Human PKC-α and Construction of a Novel BC-Analogue by an Unusual Julia Olefination Process

Karl J. Hale, Mark Frigerio, Soraya Manaviazar, Marc G. Hummersone, more

Organic Letters > 2003 > 5 > 4 > 499 - 502

article

DNA Adducts Formed from 4-Hydroxytamoxifen Are More Mutagenic than Those Formed by α-Acetoxytamoxifen in a Shuttle Vector Target Gene Replicated in Human Ad293 Cells ^†

Keith I. E. McLuckie, Michael N. Routledge, Karen Brown, Margaret Gaskell, more

Biochemistry > 2002 > 41 > 28 > 8899 - 8906

article

Relaxation Kinetics of Cytochrome P450 Reductase: Internal Electron Transfer Is Limited by Conformational Change and Regulated by Coenzyme Binding ^†

Aldo Gutierrez, Mark Paine, C. Roland Wolf, Nigel S. Scrutton, more

Biochemistry > 2002 > 41 > 14 > 4626 - 4637

article

Role of the Conserved Phenylalanine 181 of NADPH−Cytochrome P450 Oxidoreductase in FMN Binding and Catalytic Activity ^†

Mark J. I. Paine, Steven Ayivor, Andrew Munro, Pascale Tsan, more

Biochemistry > 2001 > 40 > 45 > 13439 - 13447

article

Dynamics of Mononuclear Cadmium β-Lactamase Revealed by the Combination of NMR and PAC Spectroscopy

Lars Hemmingsen, Christian Damblon, Jens Antony, Mikael Jensen, more

Journal of the American Chemical Society > 2001 > 123 > 42 > 10329 - 10335

article

Stopped-Flow Kinetic Studies of Flavin Reduction in Human Cytochrome P450 Reductase and Its Component Domains ^†

Aldo Gutierrez, Lu-Yun Lian, C. Roland Wolf, Nigel S. Scrutton, more

Biochemistry > 2001 > 40 > 7 > 1964 - 1975

article

The solution structure of the complex of Lactobacillus casei dihydrofolate reductase with methotrexate

Angelo R. Gargaro, Alice Soteriou, Thomas A. Frenkiel, Christopher J. Bauer, more

Journal of Molecular Biology > 1998 > 277 > 1 > 119-134

We have determined the three-dimensional solution structure of the complex of Lactobacillus casei dihydrofolate reductase (18.3 kDa, 162 amino acid residues) formed with the anticancer drug methotrexate using 2531 distance, 361 dihedral angle and 48 hydrogen bond restraints obtained from analysis of multidimensional NMR spectra. Simulated annealing calculations produced a family of 21 structures fully...

article

Modelling the Structures of Cytochrome P450 Reductases, Their Interaction with Cytochrome P450s, and Substrate Binding

Michael J. Sutcliffe, Sami Raza, Sandeep Modi, Lian Lu-Yun, more

Chemical Design Automation News > 1996 > 11 > 4 > 22

The cytochrome P450s constitute a superfamily of haem enzymes which catalyze the monooxygenation of a wide variety of endogenous and xenobiotic compounds through the insertion of one atom of molecular oxygen into the substrate, with the accompanying reduction of the other atom to water. Cytochrome P450s are divided into two classes according to their redox partners: class II enzymes require only a...

article

Functional High Level Expression of Cytochrome P450 CYP2D6 Using Baculoviral Expression Systems

Mark J. I. Paine, David Gilham, Gordon C. K. Roberts, C. Roland Wolf

Archives of Biochemistry and Biophysics > 1996 > 328 > 1 > 143-150

Cytochrome P-450 CYP2D6 plays a central role in the metabolism of many widely used therapeutic drugs including β-adrenergic antagonists, antiarrhythmics, and tricyclic antidepressants. Recombinant baculoviruses have been constructed containing the full-length human CYP2D6 cDNA and used to express CYP2D6 inSpodoptera frugiperda(Sf9) cells. High levels of recombinant protein have been produced using...

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