Metabolic pathways in the post-genome era

JA Papin, ND Price, SJ Wiback, DA Fell… - Trends in biochemical …, 2003 - cell.com
Metabolic pathways are a central paradigm in biology. Historically, they have been defined
on the basis of their step-by-step discovery. However, the genome-scale metabolic networks …

Chemometrics

SD Brown, TB Blank, ST Sum, LG Weyer - Analytical chemistry, 1994 - ACS Publications
INTRODUCTION Chemometrics is the discipline concerned with the ap-plication of statistical
and mathematical methods, as well as those methods based on mathematical logic, to …

Atomic-resolution structure of a disease-relevant Aβ (1–42) amyloid fibril

MA Wälti, F Ravotti, H Arai, CG Glabe, JS Wall… - Proceedings of the …, 2016 - pnas.org
Amyloid-β (Aβ) is present in humans as a 39-to 42-amino acid residue metabolic product of
the amyloid precursor protein. Although the two predominant forms, Aβ (1–40) and Aβ (1 …

Combined automated NOE assignment and structure calculation with CYANA

P Güntert, L Buchner - Journal of biomolecular NMR, 2015 - Springer
The automated assignment of NOESY cross peaks has become a fundamental technique for
NMR protein structure analysis. A widely used algorithm for this purpose is implemented in …

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

F Delaglio, S Grzesiek, GW Vuister, G Zhu… - Journal of biomolecular …, 1995 - Springer
The NMRPipe system is a UNIX software environment of processing, graphics, and analysis
tools designed to meet current routine and research-oriented multidimensional processing …

Torsion angle dynamics for NMR structure calculation with the new program DYANA

P Güntert, C Mumenthaler, K Wüthrich - Journal of molecular biology, 1997 - Elsevier
The new program Dyana (DYnamics Algorithm for Nmr Applications) for efficient calculation
of three-dimensional protein and nucleic acid structures from distance constraints and …

NMR solution structure of the human prion protein

R Zahn, A Liu, T Lührs, R Riek… - Proceedings of the …, 2000 - pnas.org
The NMR structures of the recombinant human prion protein, hPrP (23–230), and two C-
terminal fragments, hPrP (90–230) and hPrP (121–230), include a globular domain …

The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

C Bartels, T **a, M Billeter, P Güntert… - Journal of biomolecular …, 1995 - Springer
A new program package, XEASY, was written for interactive computer support of the
analysis of NMR spectra for three-dimensional structure determination of biological …

TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins

M Salzmann, K Pervushin, G Wider, H Senn… - Proceedings of the …, 1998 - pnas.org
The NMR assignment of 13C, 15N-labeled proteins with the use of triple resonance
experiments is limited to molecular weights below∼ 25,000 Daltons, mainly because of low …

[HTML][HTML] NMR characterization of the full-length recombinant murine prion protein, mPrP (23–231)

R Riek, S Hornemann, G Wider, R Glockshuber… - FEBS letters, 1997 - Elsevier
The recombinant murine prion protein, mPrP (23–231), was expressed in E. coli with uniform
15N-labeling. NMR experiments showed that the previously determined globular three …