scholarly article | Q13442814 |
P2093 | author name string | James L Cole | |
Walter F Stafford | |||
John J Correia | |||
P2860 | cites work | Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences | Q24644640 |
Modern analytical ultracentrifugation in protein science: a tutorial review | Q24645050 | ||
Insights into interferon regulatory factor activation from the crystal structure of dimeric IRF5 | Q27652424 | ||
Structure of a complex of the ATPase SecA and the protein-translocation channel | Q27652526 | ||
Semi-rigid solution structures of heparin by constrained X-ray scattering modelling: new insight into heparin-protein complexes | Q27658090 | ||
Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling | Q27860847 | ||
Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents | Q28359584 | ||
On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation | Q29616488 | ||
Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques | Q30447247 | ||
Analysis of weight average sedimentation velocity data | Q30604327 | ||
Signal peptides are allosteric activators of the protein translocase | Q33662560 | ||
Modern applications of analytical ultracentrifugation | Q33689917 | ||
Analysis of PKR activation using analytical ultracentrifugation | Q34079750 | ||
The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugation | Q34759704 | ||
Energetics of SecA dimerization | Q34761920 | ||
E. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domain | Q34769240 | ||
Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study | Q34909320 | ||
Probing the affinity of SecA for signal peptide in different environments | Q34979875 | ||
Heparin activates PKR by inducing dimerization | Q35706998 | ||
Selective photoaffinity labeling identifies the signal peptide binding domain on SecA | Q35750297 | ||
Paradoxical interactions between human delta hepatitis agent RNA and the cellular protein kinase PKR | Q35866566 | ||
Weak self-association in a carbohydrate system | Q35878618 | ||
The double-stranded-RNA-binding motif: interference and much more | Q35968493 | ||
Protein translocation by the Sec61/SecY channel | Q36280355 | ||
THERMODYNAMIC POTENTIALS OF SYMMETRICAL ELECTROLYTES. | Q36404425 | ||
Interferon action and the double-stranded RNA-dependent enzymes ADAR1 adenosine deaminase and PKR protein kinase | Q36557550 | ||
The surprising complexity of signal sequences | Q36571413 | ||
Analytical ultracentrifugation for the study of protein association and assembly | Q36578705 | ||
Oligomeric states of the SecA and SecYEG core components of the bacterial Sec translocon | Q36608490 | ||
The double-stranded RNA-dependent protein kinase is also activated by heparin | Q69397069 | ||
Energetics of vinca alkaloid interactions with tubulin | Q74178203 | ||
Protein-protein and ligand-protein interactions studied by analytical ultracentrifugation | Q83210999 | ||
The thermodynamics of vinca alkaloid-induced tubulin spirals formation | Q83937049 | ||
Complex behavior in solution of homodimeric SecA. | Q36639172 | ||
Activation of PKR: an open and shut case? | Q36695833 | ||
Mechanism of PKR Activation by dsRNA. | Q36943661 | ||
Bacterial protein secretion through the translocase nanomachine | Q36972407 | ||
Protein translocation across the bacterial cytoplasmic membrane. | Q37031528 | ||
Analytical ultracentrifugation: sedimentation velocity and sedimentation equilibrium | Q37264240 | ||
Viral evasion and subversion of pattern-recognition receptor signalling | Q37319381 | ||
RNA dimerization promotes PKR dimerization and activation | Q37389973 | ||
The ATPase cycle of the mitotic motor CENP-E. | Q37432167 | ||
Effect of kinetics on sedimentation velocity profiles and the role of intermediates | Q37629275 | ||
Identification of the heparin-binding domains of the interferon-induced protein kinase, PKR | Q37672476 | ||
SecA: a tale of two protomers | Q37742750 | ||
Analysis of tubulin oligomers by analytical ultracentrifugation | Q37751201 | ||
Insight into protein-protein interactions from analytical ultracentrifugation | Q37775643 | ||
Ultra-weak reversible protein-protein interactions | Q37845484 | ||
Role of the amino-terminal residues of the interferon-induced protein kinase in its activation by double-stranded RNA and heparin | Q38306294 | ||
Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane | Q39647998 | ||
A therapeutic antibody and its antigen form different complexes in serum than in phosphate-buffered saline: a study by analytical ultracentrifugation | Q39872323 | ||
The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation. | Q41006640 | ||
Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch | Q41825978 | ||
The concentration-dependence of macromolecular parameters | Q41971526 | ||
Magnesium-dependent interaction of PKR with adenovirus VAI. | Q42128194 | ||
Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA. | Q42739776 | ||
NUTS and BOLTS: applications of fluorescence-detected sedimentation | Q43115502 | ||
A role for the two-helix finger of the SecA ATPase in protein translocation. | Q43181763 | ||
The biotin repressor: thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding | Q44228081 | ||
Interaction of the trp RNA-binding attenuation protein (TRAP) with anti-TRAP. | Q44852933 | ||
Mutational analysis of the energetics of the GrpE.DnaK binding interface: equilibrium association constants by sedimentation velocity analytical ultracentrifugation | Q44890778 | ||
Mechanism of PKR activation: dimerization and kinase activation in the absence of double-stranded RNA. | Q45164974 | ||
Interaction of vinblastine with calf brain tubulin: effects of magnesium ions | Q45287833 | ||
Macromolecular interaction of halichondrin B analogues eribulin (E7389) and ER-076349 with tubulin by analytical ultracentrifugation. | Q45935600 | ||
Detection of protein aggregates by sedimentation velocity analytical ultracentrifugation (SV-AUC): sources of variability and their relative importance | Q46171269 | ||
Structural and biophysical characterization of the 40 kDa PEG-interferon-alpha2a and its individual positional isomers | Q46494538 | ||
Analysis of the function of Spire in actin assembly and its synergy with formin and profilin | Q46879547 | ||
Effects of efavirenz binding on the subunit equilibria of HIV-1 reverse transcriptase | Q46964863 | ||
Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants | Q47884569 | ||
Interaction of vinblastine with calf brain tubulin: multiple equilibria | Q48289034 | ||
Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques. | Q51940791 | ||
Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile | Q52420901 | ||
Calcium-induced dimerization of troponin-C. | Q52725148 | ||
Thermodynamic linkage between tubulin self-association and the binding of vinblastine. | Q52763219 | ||
Stoichiometry of the vinblastine-induced self-association of calf brain tubulin. | Q52763225 | ||
Velocity sedimentation study of ligand-induced protein self-association. | Q53765269 | ||
Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA. | Q54535975 | ||
P433 | issue | 1 | |
P304 | page(s) | 120-128 | |
P577 | publication date | 2011-05-27 | |
P1433 | published in | Biophysical Chemistry | Q15760978 |
P1476 | title | The use of analytical sedimentation velocity to extract thermodynamic linkage | |
P478 | volume | 159 |
Q39055569 | (S)Pinning down protein interactions by NMR. |
Q28544960 | Analysis of antibody aggregate content at extremely high concentrations using sedimentation velocity with a novel interference optics |
Q92270792 | Binary Colloidal Nanoparticles with a Large Size Ratio in Analytical Ultracentrifugation |
Q88150617 | Determination of Interaction Parameters for Reversibly Self-Associating Antibodies: A Comparative Analysis |
Q90692927 | Molecular Interaction Characterization Strategies for the Development of New Biotherapeutic Antibody Modalities |
Q89849097 | New technologies to analyse protein function: an intrinsic disorder perspective |
Q38098433 | Protein-protein interactions: switch from classical methods to proteomics and bioinformatics-based approaches |
Q92192845 | Proteomics and Non-proteomics Approaches to Study Stable and Transient Protein-Protein Interactions |
Q36219330 | Thermodynamic Interrogation of the Assembly of a Viral Genome Packaging Motor Complex. |
Q46523852 | Trimerization Dictates Solution Opalescence of a Monoclonal Antibody |
Q52594676 | Weak IgG self- and hetero-association characterized by fluorescence analytical ultracentrifugation. |
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