1H, 13C, and 15N peak assignments and secondary structure of human macrophage metalloelastase (MMP-12) in its inhibitor-free state.
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Solution Structure of Inhibitor-Free Human Metalloelastase (MMP-12) Indicates an Internal Conformational AdjustmentAmbidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12.MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.
P2860
1H, 13C, and 15N peak assignments and secondary structure of human macrophage metalloelastase (MMP-12) in its inhibitor-free state.
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1H, 13C, and 15N peak assignme ...... ) in its inhibitor-free state.
@en
1H, 13C, and 15N peak assignme ...... ) in its inhibitor-free state.
@nl
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label
1H, 13C, and 15N peak assignme ...... ) in its inhibitor-free state.
@en
1H, 13C, and 15N peak assignme ...... ) in its inhibitor-free state.
@nl
prefLabel
1H, 13C, and 15N peak assignme ...... ) in its inhibitor-free state.
@en
1H, 13C, and 15N peak assignme ...... ) in its inhibitor-free state.
@nl
P1476
1H, 13C, and 15N peak assignme ...... 2) in its inhibitor-free state
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P2093
R Bhaskaran
P2888
P356
10.1007/S10858-006-9035-8
P478
36 Suppl 1
P577
2006-07-20T00:00:00Z
P5875
P6179
1020163218