TonB-dependent transporters: regulation, structure, and function
N Noinaj, M Guillier, TJ Barnard… - Annual review of …, 2010 - annualreviews.org
TonB-dependent transporters (TBDTs) are bacterial outer membrane proteins that bind and
transport ferric chelates, called siderophores, as well as vitamin B12, nickel complexes, and …
transport ferric chelates, called siderophores, as well as vitamin B12, nickel complexes, and …
Colicin biology
E Cascales, SK Buchanan, D Duché… - Microbiology and …, 2007 - Am Soc Microbiol
Colicins are proteins produced by and toxic for some strains of Escherichia coli. They are
produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic …
produced by strains of E. coli carrying a colicinogenic plasmid that bears the genetic …
High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor
Heterotrimeric guanine nucleotide–binding protein (G protein)–coupled receptors constitute
the largest family of eukaryotic signal transduction proteins that communicate across the …
the largest family of eukaryotic signal transduction proteins that communicate across the …
[PDF][PDF] A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes
M Caffrey - Acta Crystallographica Section F: Structural Biology …, 2015 - journals.iucr.org
The lipid cubic phase or in meso method is a robust approach for crystallizing membrane
proteins for structure determination. The uptake of the method is such that it is experiencing …
proteins for structure determination. The uptake of the method is such that it is experiencing …
Crystallizing membrane proteins using lipidic mesophases
M Caffrey, V Cherezov - Nature protocols, 2009 - nature.com
A detailed protocol for crystallizing membrane proteins that makes use of lipidic
mesophases is described. This has variously been referred to as the lipid cubic phase or in …
mesophases is described. This has variously been referred to as the lipid cubic phase or in …
[HTML][HTML] Overcoming the challenges of membrane protein crystallography
EP Carpenter, K Beis, AD Cameron, S Iwata - Current opinion in structural …, 2008 - Elsevier
Membrane protein structural biology is still a largely unconquered area, given that
approximately 25% of all proteins are membrane proteins and yet less than 150 unique …
approximately 25% of all proteins are membrane proteins and yet less than 150 unique …
The structural biology of β-barrel membrane proteins: a summary of recent reports
JW Fairman, N Noinaj, SK Buchanan - Current opinion in structural biology, 2011 - Elsevier
The outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts all contain
transmembrane β-barrel proteins. These β-barrel proteins serve essential functions in cargo …
transmembrane β-barrel proteins. These β-barrel proteins serve essential functions in cargo …
Influence of solubilizing environments on membrane protein structures
Membrane protein structures are stabilized by weak interactions and are influenced by
additional interactions with the solubilizing environment. Structures of influenza virus A M2 …
additional interactions with the solubilizing environment. Structures of influenza virus A M2 …
TonB or not TonB: is that the question?
KD Krewulak, HJ Vogel - Biochemistry and cell biology, 2011 - cdnsciencepub.com
Bacteria are able to survive in low-iron environments by sequestering this metal ion from
iron-containing proteins and other biomolecules such as transferrin, lactoferrin, heme …
iron-containing proteins and other biomolecules such as transferrin, lactoferrin, heme …
Crystallizing membrane proteins for structure determination: use of lipidic mesophases
M Caffrey - Annual review of biophysics, 2009 - annualreviews.org
The principal route to determine the structure and the function and interactions of membrane
proteins is via macromolecular crystallography. For macromolecular crystallography to be …
proteins is via macromolecular crystallography. For macromolecular crystallography to be …