Zuiderweg ER - Search Results

1

Binding of a small molecule at a protein-protein interface regulates the chaperone activity of hsp70-hsp40.

Wisén S, Bertelsen EB, Thompson AD, Patury S, Ung P, Chang L, Evans CG, Walter GM, Wipf P, Carlson HA, Brodsky JL, Zuiderweg ER, Gestwicki JE. Wisén S, et al. Among authors: zuiderweg er. ACS Chem Biol. 2010 Jun 18;5(6):611-22. doi: 10.1021/cb1000422. ACS Chem Biol. 2010. PMID: 20481474 Free PMC article.

2

The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology.

Morshauser RC, Wang H, Flynn GC, Zuiderweg ER. Morshauser RC, et al. Among authors: zuiderweg er. Biochemistry. 1995 May 16;34(19):6261-6. doi: 10.1021/bi00019a001. Biochemistry. 1995. PMID: 7756251

3

NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.

Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER. Wang H, et al. Among authors: zuiderweg er. Biochemistry. 1998 Jun 2;37(22):7929-40. doi: 10.1021/bi9800855. Biochemistry. 1998. PMID: 9609686

4

High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70.

Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, Zuiderweg ER. Morshauser RC, et al. Among authors: zuiderweg er. J Mol Biol. 1999 Jun 25;289(5):1387-403. doi: 10.1006/jmbi.1999.2776. J Mol Biol. 1999. PMID: 10373374

5

Structural insights into substrate binding by the molecular chaperone DnaK.

Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER. Pellecchia M, et al. Among authors: zuiderweg er. Nat Struct Biol. 2000 Apr;7(4):298-303. doi: 10.1038/74062. Nat Struct Biol. 2000. PMID: 10742174

6

Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.

Cai S, Stevens SY, Budor AP, Zuiderweg ER. Cai S, et al. Among authors: zuiderweg er. Biochemistry. 2003 Sep 30;42(38):11100-8. doi: 10.1021/bi030097c. Biochemistry. 2003. PMID: 14503860

7

The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG.

Stevens SY, Cai S, Pellecchia M, Zuiderweg ER. Stevens SY, et al. Among authors: zuiderweg er. Protein Sci. 2003 Nov;12(11):2588-96. doi: 10.1110/ps.03269103. Protein Sci. 2003. PMID: 14573869 Free PMC article.

8

NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.

Revington M, Holder TM, Zuiderweg ER. Revington M, et al. Among authors: zuiderweg er. J Biol Chem. 2004 Aug 6;279(32):33958-67. doi: 10.1074/jbc.M313967200. Epub 2004 Jun 2. J Biol Chem. 2004. PMID: 15175340 Free article.

9

The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.

Zhang Y, Zuiderweg ER. Zhang Y, et al. Among authors: zuiderweg er. Proc Natl Acad Sci U S A. 2004 Jul 13;101(28):10272-7. doi: 10.1073/pnas.0401313101. Epub 2004 Jul 1. Proc Natl Acad Sci U S A. 2004. PMID: 15232009 Free PMC article.

10

NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone.

Revington M, Zhang Y, Yip GN, Kurochkin AV, Zuiderweg ER. Revington M, et al. Among authors: zuiderweg er. J Mol Biol. 2005 May 27;349(1):163-83. doi: 10.1016/j.jmb.2005.03.033. Epub 2005 Apr 8. J Mol Biol. 2005. PMID: 15876376

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