scholarly article | Q13442814 |
P356 | DOI | 10.1038/NSB0294-111 |
P953 | full work available at URL | http://www.nature.com/articles/nsb0294-111.pdf |
http://www.nature.com/articles/nsb0294-111 | ||
P698 | PubMed publication ID | 7656014 |
P2093 | author name string | J. P. Springer | |
W. K. Hagmann | |||
P. R. Gooley | |||
J. F. O'Connell | |||
A. I. Marcy | |||
B. L. Bush | |||
G. C. Cuca | |||
J. D. Hermes | |||
S. P. Salowe | |||
C. K. Esser | |||
P2860 | cites work | Journal of Magnetic Resonance | Q3186925 |
Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases | Q27642074 | ||
First structure of a snake venom metalloproteinase: a prototype for matrix metalloproteinases/collagenases | Q27731442 | ||
Refined 1.8 A X-ray crystal structure of astacin, a zinc-endopeptidase from the crayfish Astacus astacus L. Structure determination, refinement, molecular structure and comparison with thermolysin | Q27732101 | ||
On the size of the active site in proteases. I. Papain | Q27860826 | ||
The Protein Data Bank: a computer-based archival file for macromolecular structures | Q27860989 | ||
Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins' | Q28264338 | ||
Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a | Q28276423 | ||
Structure of thermolysin refined at 1.6 A resolution | Q28279663 | ||
β-Sheet topology and the relatedness of proteins | Q28295058 | ||
Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways | Q28492838 | ||
Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling | Q29618924 | ||
Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin | Q34167009 | ||
Substrate specificities and inhibition of two hemorrhagic zinc proteases Ht-c and Ht-d from Crotalus atrox venom | Q34181593 | ||
Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations | Q36449550 | ||
Heteronuclear filters in two-dimensional [1H,1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions | Q37878796 | ||
Zinc coordination, function, and structure of zinc enzymes and other proteins | Q37946601 | ||
Human fibroblast stromelysin catalytic domain: expression, purification, and characterization of a C-terminally truncated form | Q38334423 | ||
Substrate specificity of the human matrix metalloproteinase stromelysin and the development of continuous fluorometric assays | Q41104859 | ||
CHARMM: A program for macromolecular energy, minimization, and dynamics calculations | Q53340989 | ||
A protease from Astacus fluviatilis as an aid in protein sequencing. | Q55062929 | ||
Four-dimensional carbon-13/carbon-13-edited nuclear Overhauser enhancement spectroscopy of a protein in solution: application to interleukin 1.beta | Q57904872 | ||
Structural basis of the action of thermolysin and related zinc peptidases | Q59701722 | ||
Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts | Q62870407 | ||
Conformation of two non-immunosuppressive FK506 analogs when bound to FKBP by isotope-filtered NMR | Q67541508 | ||
A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substances | Q67686744 | ||
The origin of matrix metalloproteinases and their familial relationships | Q67975786 | ||
Characterization of zinc-binding sites in human stromelysin-1: stoichiometry of the catalytic domain and identification of a cysteine ligand in the proenzyme | Q68118352 | ||
Determination of the tautomeric form of the imidazole ring of L-histidine in basic solution by carbon-13 magnetic resonance spectroscopy | Q69481407 | ||
Comparative sequence specificities of human 72- and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin) | Q70461729 | ||
The structure of thermolysin: An electron density map at 2.3 Å resolution | Q70506797 | ||
Secondary structure and zinc ligation of human recombinant short-form stromelysin by multidimensional heteronuclear NMR | Q72609641 | ||
Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experiments | Q72609645 | ||
Inhibition of matrix metalloproteinases by N-carboxyalkyl peptides | Q72696588 | ||
Three-dimensional structure of thermolysin | Q81712793 | ||
P433 | issue | 2 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 111-8 | |
P577 | publication date | 1994-02-01 | |
P1433 | published in | Nature structural biology | Q26842658 |
P1476 | title | The NMR structure of the inhibited catalytic domain of human stromelysin-1 | |
The NMR structure of the inhibited catalytic domain of human stromelysin–1 | |||
P478 | volume | 1 |