scholarly article | Q13442814 |
P50 | author | Clarice de Azevedo Souza | Q85887347 |
P2093 | author name string | Roberto N De Guzman | |
Gregory V Plano | |||
Sukanya Chaudhury | |||
P2860 | cites work | CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice | Q24286950 |
LcrG-LcrV interaction is required for control of Yops secretion in Yersinia pestis | Q24548891 | ||
Roles of LcrG and LcrV during type III targeting of effector Yops by Yersinia enterocolitica | Q24548902 | ||
Interaction of the Yersinia pestis type III regulatory proteins LcrG and LcrV occurs at a hydrophobic interface | Q24797087 | ||
Assembly and structure of the T3SS | Q26865556 | ||
Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells | Q27028058 | ||
The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague | Q27643133 | ||
NMR Structure of the N-terminal Coiled Coil Domain of the Andes Hantavirus Nucleocapsid Protein | Q27651453 | ||
Structural Instability Tuning as a Regulatory Mechanism in Protein-Protein Interactions | Q27676032 | ||
Substrate-Activated Conformational Switch on Chaperones Encodes a Targeting Signal in Type III Secretion | Q27676993 | ||
Structure of theYersinia pestistip protein LcrV refined to 1.65 Å resolution | Q27678232 | ||
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation | Q27860508 | ||
Using NMRView to visualize and analyze the NMR spectra of macromolecules | Q27860567 | ||
NMRPipe: a multidimensional spectral processing system based on UNIX pipes | Q27860859 | ||
The PSIPRED protein structure prediction server | Q27860953 | ||
The type III secretion injectisome | Q29617944 | ||
Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy. | Q30360846 | ||
Virulence role of V antigen of Yersinia pestis at the bacterial surface | Q30778457 | ||
EspB from enterohaemorrhagic Escherichia coli is a natively partially folded protein | Q30981321 | ||
Yersinia type III secretion: send in the effectors | Q34774578 | ||
The Yersinia Ysc-Yop 'type III' weaponry | Q34931776 | ||
Control of effector export by the Pseudomonas aeruginosa type III secretion proteins PcrG and PcrV. | Q35071514 | ||
Yersinia pestis LcrV forms a stable complex with LcrG and may have a secretion-related regulatory role in the low-Ca2+ response | Q35620091 | ||
LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis | Q36101650 | ||
The Salmonella type III secretion system inner rod protein PrgJ is partially folded. | Q36127196 | ||
Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR | Q36280194 | ||
Positional preference of proline in alpha-helices | Q36281580 | ||
What's the point of the type III secretion system needle? | Q36638746 | ||
Roles of YopN, LcrG and LcrV in controlling Yops secretion by Yersinia pestis. | Q36984033 | ||
Structure and biophysics of type III secretion in bacteria | Q37014297 | ||
Effectors of animal and plant pathogens use a common domain to bind host phosphoinositides | Q37167670 | ||
Linking folding and binding | Q37373866 | ||
Overcoming the solubility limit with solubility-enhancement tags: successful applications in biomolecular NMR studies | Q37592032 | ||
Intrinsically disordered proteins: regulation and disease | Q37868137 | ||
LcrG is required for efficient translocation of Yersinia Yop effector proteins into eukaryotic cells. | Q39571764 | ||
DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of Yersinia pestis KIM5. | Q39573090 | ||
The type III secretion chaperone SycE promotes a localized disorder-to-order transition in the natively unfolded effector YopE. | Q40642883 | ||
Regulation by Ca2+ in the Yersinia low-Ca2+ response | Q40840513 | ||
Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein | Q41381050 | ||
The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles | Q41456399 | ||
Interactions of the type III secretion pathway proteins LcrV and LcrG from Yersinia pestis are mediated by coiled-coil domains. | Q41471377 | ||
PcrG protects the two long helical oligomerization domains of PcrV, by an interaction mediated by the intramolecular coiled-coil region of PcrG. | Q41895565 | ||
NMR characterization of the interaction of the Salmonella type III secretion system protein SipD and bile salts | Q42126458 | ||
Inter-molecular coiled-coil formation in human apolipoprotein E C-terminal domain | Q44659103 | ||
An optimized system for expression and purification of secreted bacterial proteins | Q45076251 | ||
Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurements | Q46172640 | ||
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding | Q46559043 | ||
Amphipathic alpha-helix bundle organization of lipid-free chicken apolipoprotein A-I. | Q50519411 | ||
Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded alpha-helical coiled-coils | Q70648566 | ||
Coiled-coil domains in proteins secreted by type III secretion systems | Q73663925 | ||
Protein chemical shift analysis: a practical guide | Q77922368 | ||
P433 | issue | 19 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Yersinia pestis | Q153875 |
molecular chaperones | Q422496 | ||
protein folding | Q847556 | ||
P304 | page(s) | 3096-3109 | |
P577 | publication date | 2015-08-07 | |
P1433 | published in | Journal of Molecular Biology | Q925779 |
P1476 | title | The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded | |
P478 | volume | 427 |
Q64075941 | The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells | cites work | P2860 |
Search more.