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Search Publications by: Alexander Grishaev (Fed)

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Displaying 26 - 46 of 46

Structural and Dynamical Order of a Disordered Protein: Molecular Insights into Conformational Switching of PAGE4 at the Systems Level

February 1, 2019
Author(s)
Xingcheng Ling, Prakash Kulkarni, Federico Bocci, Nicholas Schafer, Susmita Roy, Min-Yeh Tsai, Yanan He, Yihong Chen, Krithika Rajagopalan, Steven Mooney, Yu Zeng, Keith Weninger, Alexander Grishaev, Jose Onuchic, Herbert Levine, Peter Wolynes, Govindan Rangarajan, Vladimir Uversky, John Orban, Mohit Jolly
Folded proteins show a high degree of structural order and undergo (fairly constrained) collective motions related to their functions. On the other hand, intrinsically disordered proteins (IDPs), while lacking a well-defined three-dimensional structure, do

Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water"

August 30, 2018
Author(s)
Robert Best, Alessandro Borgia, Wenwei Zheng, Karin Buholzer, Madeleine Borgia, Hagen Hofmann, Daniel Nettels, Klaus Gast, Alexander Grishaev, Benjamin Schuler
The degree of compaction inferred from SAXS experiments by Riback et al. for unfolded proteins in water versus chemical denaturant is highly consistent with the results from FRET experiments. There is thus no "contradiction" between the two methods, nor

PAGE4 and Conformational Switching: Insights from Molecular Dynamics Simulations and Implications for Prostate Cancer

August 2, 2018
Author(s)
Alexander Grishaev, Xingcheng Lin, Mohit Jolly, Federico Bocci, Nicholas Schafer, Min-Yeh Tsai, Yihong Chen, Yanan He, Keith Weninger, John Orban, Prakash Kulkarni, Govindan Rangarajan, Herbert Levine, Jose Onuchic
Prostate-Associated Gene 4 (PAGE4) is a disordered protein implicated in the progression of prostate cancer. PAGE4 can be phosphorylated at two residue sites by Homeodomain-Interacting Protein Kinase 1 (HIPK1) to facilitate its binding to the Activator

A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity

May 24, 2018
Author(s)
Subrata Debnath, Dalibor Kosek, Harichandra Tagad, Stewart R. Durell, Daniel Appella, Roderico Acevedo, Alexander Grishaev, Fred Dyda, Ettore Appella, Sharlyn Mazur
Metal-dependent protein phosphatases (PPM) are evolutionarily unrelated to other serine/threonine protein phosphatases and are characterized by their requirement for supplementation with millimolar concentrations of Mg2+ or Mn2+ ions for activity in vitro

Hybrid Applications of Solution Scattering to Aid Structural Biology

November 19, 2017
Author(s)
Alexander Grishaev
Biomolecular applications of solution X-ray and neutron scattering (SAXS and SANS, respectively) started in late 1960s – early 1970s but were relatively limited in their ability to provide a detailed structural picture and lagged behind what became the two

Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods

September 13, 2017
Author(s)
Alessandro Borgia, Wenwei Zheng, Karin Buholzer, Madeleine Borgia, Anja Schuler, Hagen Hoffman, Andrea Sorrano, Daniel Nettels, Klaus Gast, Alexander Grishaev, Robert Best, Benjamin Schuler
There has been a long-standing controversy regarding the effect of chemical denaturants on the dimensions of unfolded and intrinsically disordered proteins: A wide range of experimental techniques suggest that polypeptide chains expand with increasing

Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity

June 2, 2017
Author(s)
Prakash Kulkarni, Mohit Jolly, Dongya Jia, Steven Mooney, Ajay Bhargava, Luciane Kagohara, Yihong Chen, Pengyu Hao, Yanan He, Roberft Veltri, Alexander Grishaev, Keith Weninger, Herbert Levine, John Orban
Intrinsically disordered proteins (IDPs) that lack a unique 3D structure and comprise a large fraction of the human proteome play important roles in numerous cellular functions. Prostate- Associated Gene 4 (PAGE4) is an IDP that acts as a potentiator of