Erik R. P. Zuiderweg

Affiliations: 
University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
NMR studies of Biomacromolecular Conformation, Dynamics and Interactions in Solution
Website:
http://www.biochem.med.umich.edu/?q=zuiderweg
Google:
"Erik Zuiderweg"
Mean distance: 8.8 (cluster 58)
 
SNBCP
Cross-listing: MichiganTree

Parents

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Cornelis W. Hilbers grad student 1980 Radboud University Nijmegen
 (On the interaction of myo-inositol hexakisphosphate with human hemoglobin : a 31P NMR and pH-stat study)
Robert Kaptein post-doc RUG
Kurt Wüthrich post-doc 1982-1983 ETH Zürich
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Publications

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Zuiderweg ER, Hightower LE, Gestwicki JE. (2017) The remarkable multivalency of the Hsp70 chaperones. Cell Stress & Chaperones
Zuiderweg ER, Gestwicki JE. (2016) Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state. Biomolecular Nmr Assignments
Young ZT, Rauch JN, Assimon VA, et al. (2016) Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy. Cell Chemical Biology
Rauch JN, Zuiderweg ER, Gestwicki JE. (2016) Non-Canonical Interactions Between Heat Shock Cognate Protein 70 (Hsc70) and Bcl2-Associated Anthanogene (BAG) Co-Chaperones Are Important for Client Release. The Journal of Biological Chemistry
Morozova K, Clement CC, Kaushik S, et al. (2016) Hsc-70 Structural and Biological Interaction with Phosphatidylserine in Endosomal Microautophagy. The Journal of Biological Chemistry
Stull FW, Bernard SM, Sapra A, et al. (2016) Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase. Biochemistry
Fontaine SN, Rauch JN, Nordhues BA, et al. (2015) Isoform-selective Genetic Inhibition of Constitutive Cytosolic Hsp70 Activity Promotes Client Tau Degradation Using an Altered Co-chaperone Complement. The Journal of Biological Chemistry. 290: 13115-27
Bagai I, Sarangi R, Fleischhacker AS, et al. (2015) Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme. Biochemistry. 54: 2693-708
Plegaria JS, Dzul SP, Zuiderweg ER, et al. (2015) Apoprotein Structure and Metal Binding Characterization of a de Novo Designed Peptide, α3DIV, that Sequesters Toxic Heavy Metals. Biochemistry. 54: 2858-73
Spencer AL, Bagai I, Becker DF, et al. (2014) Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase. The Journal of Biological Chemistry. 289: 29836-58
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