Biophysical characterization of a recombinant aminopeptidase II from the thermophilic bacterium Bacillus stearothermophilus.
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Chemical and thermal unfolding of a global staphylococcal virulence regulator with a flexible C-terminal endAminopeptidase T of M29 Family Acts as A Novel Intracellular Virulence Factor for Listeria monocytogenes Infection.Halotolerant aminopeptidase M29 from Mesorhizobium SEMIA 3007 with biotechnological potential and its impact on biofilm synthesis.A staphylococcal anti-sigma factor possesses a single-domain, carries different denaturant-sensitive regions and unfolds via two intermediates.
P2860
Biophysical characterization of a recombinant aminopeptidase II from the thermophilic bacterium Bacillus stearothermophilus.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 29 October 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Biophysical characterization o ...... m Bacillus stearothermophilus.
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Biophysical characterization o ...... m Bacillus stearothermophilus.
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type
label
Biophysical characterization o ...... m Bacillus stearothermophilus.
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Biophysical characterization o ...... m Bacillus stearothermophilus.
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Biophysical characterization o ...... m Bacillus stearothermophilus.
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Biophysical characterization o ...... m Bacillus stearothermophilus.
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P2093
P2860
P1476
Biophysical characterization o ...... m Bacillus stearothermophilus.
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P2093
Huei-Fen Lo
Long-Liu Lin
Meng-Chun Chi
Min-Guan Lin
Tzu-Fan Wang
P2860
P2888
P356
10.1007/S10867-013-9332-X
P577
2013-10-29T00:00:00Z