A
Algirdas Velyvis
Researcher at University of Toronto
Publications - 17
Citations - 1124
Algirdas Velyvis is an academic researcher from University of Toronto. The author has contributed to research in topics: Allosteric regulation & Nuclear magnetic resonance spectroscopy. The author has an hindex of 15, co-authored 17 publications receiving 1000 citations. Previous affiliations of Algirdas Velyvis include Hospital for Sick Children & University of California, Berkeley.
Papers
More filters
Journal ArticleDOI
Variable Control of Ets-1 DNA Binding by Multiple Phosphates in an Unstructured Region
Miles A. Pufall,Gregory M. Lee,Mary L. Nelson,Hyun Seo Kang,Algirdas Velyvis,Lewis E. Kay,Lawrence P. McIntosh,Barbara J. Graves +7 more
TL;DR: How multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity is reported, which serves as a “rheostat” for cell signaling to fine-tune transcription at the level of DNA binding.
Journal ArticleDOI
Solution NMR of supramolecular complexes: providing new insights into function
TL;DR: A strategy is developed in the laboratory that involves the use of labeled methyl groups of isoleucine, leucine and valine residues in proteins as probes, along with experiments that significantly enhance the lifetimes of the resulting signals.
Journal ArticleDOI
A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase
TL;DR: The utility of modern solution NMR spectroscopy in understanding protein function, even for systems with aggregate molecular masses in the hundreds of kilodaltons is emphasized, despite the fact that the R state is “invisible” in spectra.
Journal ArticleDOI
An Economical Method for Production of 2H,13CH3-Threonine for Solution NMR Studies of Large Protein Complexes: Application to the 670 kDa Proteasome
TL;DR: An inexpensive biosynthetic strategy for the production of L-[α- 2H; β−2H;γ-13C]-Thr that can then be directly added during protein expression to produce highly deuterated proteins with Thr methyl group probes of structure and dynamics is described.
Journal ArticleDOI
ClpB N-terminal domain plays a regulatory role in protein disaggregation
Rina Rosenzweig,Patrick Farber,Algirdas Velyvis,Enrico Rennella,Michael P. Latham,Lewis E. Kay +5 more
TL;DR: It is demonstrated that ClpB recognizes exposed hydrophobic stretches in unfolded or aggregated client proteins via a substrate-binding groove in its NTD, and that the NTD has regulatory roles that include blocking the translocation channel in the absence of substrate and destabilizing client proteins upon binding, thus priming them for subsequent unfolding and disaggregation.