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2001, Methods in enzymology, ISBN 0121827992, Volume 338, 339, v. 394., 2 v.
This volume and its companion, Volume 339, supplement Volumes 176, 177, 239, and 261. Chapters are written with a "hands-on" perspective. That is, practical... 
Proteins | Nuclear magnetic resonance spectroscopy | Biomolecules | Macromolecules | Analysis | Nuclear magnetic resonance
Book
Science, ISSN 0036-8075, 7/2011, Volume 333, Issue 6039, pp. 228 - 233
Journal Article
Structure, ISSN 0969-2126, 05/2011, Volume 19, Issue 5, pp. 601 - 602
The structure of the receptor for advanced glycation end products (RAGE) in complex with a peptide containing an -carboxy-ethyl-lysine (CEL) ( ) shows how the... 
BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOPHYSICS | CELL BIOLOGY | Peptides | Chains | Receptors | Lysine | Recognition
Journal Article
Journal Article
Nature Protocols, ISSN 1754-2189, 01/2007, Volume 1, Issue 6, pp. 2701 - 2709
The noninvasive character of NMR spectroscopy, combined with the sensitivity of the chemical shift, makes it ideally suited to investigate the conformation,... 
VIVO | ESCHERICHIA-COLI | BIOCHEMICAL RESEARCH METHODS | OOCYTES | ALPHA-SYNUCLEIN | PROTEINS | EXTRACTS | LIVING CELLS | Isotope Labeling - methods | Animals | Macromolecular Substances - chemistry | Nuclear Magnetic Resonance, Biomolecular - methods | Xenopus laevis | Cells, Cultured | Ovum - chemistry | Escherichia coli - chemistry
Journal Article
Journal Article
The EMBO Journal, ISSN 0261-4189, 07/2007, Volume 26, Issue 14, pp. 3451 - 3462
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2010, Volume 107, Issue 35, pp. 15318 - 15325
One of the basic principles that nature uses in evolution is to recycle successful concepts and create new functions by modifying existing units. This... 
Proteins | Protein isoforms | Germ cells | PERSPECTIVE | Somatic cells | Induced pluripotent stem cells | DNA | Stem cells | Evolution | Family members | Tumors | Oligomerization | p63 | p73 | p53 | DNA-BINDING DOMAIN | P53-DEPENDENT APOPTOSIS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | CORE DOMAIN | evolution | oligomerization | STRUCTURAL BASIS | EMBRYONIC STEM-CELLS | MUTANT P53 | TETRAMERIZATION DOMAIN | C-TERMINAL DOMAIN | P53 TUMOR-SUPPRESSOR | Alternative Splicing | Humans | Genome - genetics | Molecular Sequence Data | Trans-Activators - chemistry | Tumor Suppressor Protein p53 - genetics | DNA-Binding Proteins - metabolism | Tumor Suppressor Proteins - chemistry | Tumor Suppressor Proteins - genetics | Trans-Activators - genetics | Germ Cells - metabolism | Nuclear Proteins - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Tumor Suppressor Proteins - metabolism | Protein Structure, Secondary | Tumor Suppressor Protein p53 - metabolism | Models, Molecular | Nuclear Proteins - metabolism | Binding Sites - genetics | DNA - metabolism | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Sequence Homology, Amino Acid | Tumor Protein p73 | Animals | Protein Binding | Trans-Activators - metabolism | Mice | Transcription Factors | Tumor Suppressor Protein p53 - chemistry | Mutation | Evolution, Molecular | Pathology | Research | Genomics | protein families | Evolutionary genetics | Tumor suppressor genes | Genomes | Recycling | p53 protein
Journal Article