3D domain swapping: as domains continue to swap

Y Liu, D Eisenberg - Protein science, 2002 - Wiley Online Library
Abstract Three‐dimensional (3D) domain swapping creates a bond between two or more
protein molecules as they exchange their identical domains. Since the term'3D domain …

Process of protein transport by the type III secretion system

P Ghosh - Microbiology and molecular biology reviews, 2004 - Am Soc Microbiol
The type III secretion system (TTSS) of gram-negative bacteria is responsible for delivering
bacterial proteins, termed effectors, from the bacterial cytosol directly into the interior of host …

Insights into protein–protein binding by binding free energy calculation and free energy decomposition for the Ras–Raf and Ras–RalGDS complexes

H Gohlke, C Kiel, DA Case - Journal of molecular biology, 2003 - Elsevier
Absolute binding free energy calculations and free energy decompositions are presented for
the protein–protein complexes H-Ras/C-Raf1 and H-Ras/RalGDS. Ras is a central switch in …

A solvent-driven molecular spring

Z Zhang, C Han, G Yu, F Huang - Chemical Science, 2012 - pubs.rsc.org
A solvent-driven doubly threaded rotaxane dimer based on an amino-modified copillar [5]
arene was prepared using bis (trifluoromethyl) phenyl isocyanate as stoppers. By …

The unfolding story of three-dimensional domain swapping

F Rousseau, JWH Schymkowitz, LS Itzhaki - Structure, 2003 - cell.com
Three-dimensional domain swapping is the event by which a monomer exchanges part of its
structure with identical monomers to form an oligomer where each subunit has a similar …

Evolution of protein structures and functions

LN Kinch, NV Grishin - Current opinion in structural biology, 2002 - Elsevier
Within the ever-expanding repertoire of known protein sequences and structures, many
examples of evolving three-dimensional structures are emerging that illustrate the plasticity …

The βγ-crystallins: Native state stability and pathways to aggregation

E Serebryany, JA King - Progress in biophysics and molecular biology, 2014 - Elsevier
The βγ-crystallins are among the most stable and long-lived proteins in the human body.
With increasing age, however, they transform to high molecular weight light-scattering …

Protein folding: then and now

Y Chen, F Ding, H Nie, AW Serohijos, S Sharma… - Archives of biochemistry …, 2008 - Elsevier
Over the past three decades the protein folding field has undergone monumental changes.
Originally a purely academic question, how a protein folds has now become vital in …

Change in protein flexibility upon complex formation: analysis of Ras‐Raf using molecular dynamics and a molecular framework approach

H Gohlke, LA Kuhn, DA Case - PROTEINS: Structure, Function …, 2004 - Wiley Online Library
Abstract Changes in flexibility upon protein–protein complex formation of H‐Ras and the
Ras‐binding domain of C‐Raf1 have been investigated using the molecular framework …

Structural analysis of the autoinhibition of Ets-1 and its role in protein partnerships

CW Garvie, MA Pufall, BJ Graves… - Journal of Biological …, 2002 - ASBMB
The DNA-binding activity of the eukaryotic transcription factor Ets-1 (E26 avian
erythroblastosis virus oncogene-Etwenty-six) is negatively regulated by inhibitory regions …