Výsledky vyhledávání - "E R, Zuiderweg"

Structure of the type III secretion and substrate-binding domain of Yersinia YopH phosphatase

Autor: C L, Smith, P, Khandelwal, K, Keliikuli, E R, Zuiderweg, M A, Saper

Publikováno v: Molecular microbiology. 42(4)

Pathogenic strains of Yersinia deploy a type III secretion system to inject the potent tyrosine phosphatase YopH into host cells, where it dephosphorylates focal adhesion-associated substrates. The amino-terminal, non-catalytic domain of YopH is bifu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::eddc8d56e29ed48ee773cfe7c5585c50
https://pubmed.ncbi.nlm.nih.gov/11737640

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Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity

Autor: S Y, Stevens, S, Sanker, C, Kent, E R, Zuiderweg

Publikováno v: Nature structural biology. 8(11)

The dimeric enzyme CTP:glycerol-3-phosphate cytidylyltransferase (GCT) displays strong negative cooperativity between the first and second binding of its substrate, CTP. Using NMR to study the allosteric mechanism of this enzyme, we observe widesprea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1ee73760440dea41ca7c5c5e924f761e
https://pubmed.ncbi.nlm.nih.gov/11685240

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Structural insights into substrate binding by the molecular chaperone DnaK

Autor: M, Pellecchia, D L, Montgomery, S Y, Stevens, C W, Vander Kooi, H P, Feng, L M, Gierasch, E R, Zuiderweg

Publikováno v: Nature structural biology. 7(4)

How substrate affinity is modulated by nucleotide binding remains a fundamental, unanswered question in the study of 70 kDa heat shock protein (Hsp70) molecular chaperones. We find here that the Escherichia coli Hsp70, DnaK, lacking the entire alpha-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e6ce89dd36ba9774fb9056e872420d19
https://pubmed.ncbi.nlm.nih.gov/10742174

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Line narrowing in spectra of proteins dissolved in a dilute liquid crystalline phase by band-selective adiabatic decoupling: application to 1HN-15N residual dipolar coupling measurements

Autor: C W, Vander Kooi, E, Kupce, E R, Zuiderweg, M, Pellecchia

Publikováno v: Journal of biomolecular NMR. 15(4)

Residual heteronuclear dipolar couplings obtained from partially oriented protein samples can provide unique NMR constraints for protein structure determination. However, partial orientation of protein samples also causes severe 1H line broadening re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f1ec252613e575bf581829fa62cd0c9f
https://pubmed.ncbi.nlm.nih.gov/10685341

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

Autor: R C, Morshauser, W, Hu, H, Wang, Y, Pang, G C, Flynn, E R, Zuiderweg

Publikováno v: Journal of molecular biology. 289(5)

The three-dimensional structure for the substrate-binding domain of the mammalian chaperone protein Hsc70 of the 70 kDa heat shock class (HSP70) is presented. This domain includes residues 383-540 (18 kDa) and is necessary for the binding of the chap

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c232e0a76faf5c9e39692898470a87c8
https://pubmed.ncbi.nlm.nih.gov/10373374

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High-resolution detection of five frequencies in a single 3D spectrum: HNHCACO--a bidirectional coherence transfer experiment

Autor: Y, Pang, L, Zeng, A V, Kurochkin, E R, Zuiderweg

Publikováno v: Journal of biomolecular NMR. 11(2)

A new triple-resonance pulse sequence, 3D HNHCACO, is introduced and discussed, which identifies sequential correlations of the backbone nuclei (H alpha (i-1), C alpha (i-1), C(i-1), NH(i), N(i)) of doubly labeled proteins in H2O. The three-dimension

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d9d2f737c6966dd9c36ac236da4e13d2
https://pubmed.ncbi.nlm.nih.gov/9679293

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Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase. Role of histidines in the conserved HXGH in catalysis

Autor: Y S, Park, P, Gee, S, Sanker, E J, Schurter, E R, Zuiderweg, C, Kent

Publikováno v: The Journal of biological chemistry. 272(24)

The CTP:glycerol-3-phosphate cytidylyltransferase (GCT) of Bacillus subtilis has been shown to be similar in primary structure to the CTP:phosphocholine cytidylyltransferases of several organisms. To identify the residues of this cytidylyltransferase

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c7b82749a92713e29ba9d06bb8a918d8
https://pubmed.ncbi.nlm.nih.gov/9182537

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Comparative modeling of proteins in the complement pathway

Autor: J, Greer, K W, Mollison, G W, Carter, E R, Zuiderweg

Publikováno v: Progress in clinical and biological research. 289

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::eb40e6bc2564adad320c50be759b322b
https://pubmed.ncbi.nlm.nih.gov/2786214

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Sequence-specific assignments in the 1H NMR spectrum of the human inflammatory protein C5a

Autor: E R, Zuiderweg, K W, Mollison, J, Henkin, G W, Carter

Publikováno v: Biochemistry. 27(10)

Full sequence-specific assignments for the 1H NMR lines of the backbone protons of the human complement factor C5a are described and documented. The results were obtained by largely following the methodology developed by Wüthrich et al. [Wüthrich,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f1835f848dc463c4658a9cd7b9820ae6
https://pubmed.ncbi.nlm.nih.gov/3408713

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