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- Axelsson, L., et al.
(author)
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Two-proton emission in the decay of Ar-31
- 1998
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In: Nuclear Physics A. - 0375-9474. ; 628:3, s. 345-362
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Journal article (peer-reviewed)abstract
- Several beta-delayed two-proton branches were observed in the decay of Ar-31, the most intense ones proceeding through the isobaric analogue state (IAS) in Cl-31. The mechanism of the two-proton emission is studied via the energy and angular distributions of the two protons, Simultaneous emission of the two protons fits the present data well, sequential decays might also describe them. Independent of the decay mechanism, a spin of 5/2 for the IAS is suggested, An improved limit on the direct two-proton emission fi om the ground state of Ar-31 is presented, (C) 1998 Elsevier Science B.V.
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- Baumann, T., et al.
(author)
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Longitudinal momentum distributions of C-16,C-18 fragments after one-neutron removal from C-17,C-19
- 1998
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In: Physics Letters, Section B: Nuclear, Elementary Particle and High-Energy Physics. - 0370-2693. ; 439:3-4, s. 256-261
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Journal article (peer-reviewed)abstract
- The fragment separator FRS at GSI was used as an energy-loss spectrometer to measure the longitudinal momentum distributions of C-16,C-18 fragments after one-neutron removal reactions in C-17,C-19 impinging on a carbon target at about 910 MeV/u. The distributions in the projectile frames are characterized by a FWHM of 141 +/- 6 MeV/c for C-16 and 69 +/- 3 MeV/c for C-18. Th, results are compared with experimental data obtained at lower energies and discussed within existing theoretical models. (C) 1998 Elsevier Science B.V. AU rights reserved.
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- Morgunova, E, et al.
(author)
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Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed
- 1999
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In: Science (New York, N.Y.). - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 284:5420, s. 1667-1670
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Journal article (peer-reviewed)abstract
- Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.
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