Search Results - "Strynadka, N.C.J"
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Structural and biochemical characterization of SpoIIIAF, a component of a sporulation-essential channel in Bacillus subtilis
Published in Journal of structural biology (01-10-2018)“…Environmental stress factors initiate the developmental process of sporulation in some Gram-positive bacteria including Bacillus subtilis. Upon sporulation…”
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Recent structural advances towards understanding of the bacterial type III secretion injectisome
Published in Trends in biochemical sciences (Amsterdam. Regular ed.) (01-09-2022)“…The bacterial injectisome is a structurally conserved, syringe-shaped nanomachine that spans the Gram-negative envelope and forms a continuous channel for type…”
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Molecular docking programs successfully predict the binding of a β-lactamase inhibitory protein to TEM-1 β-lactamase
Published in Nature structural biology (01-03-1996)“…Crystallization of the 1:1 molecular complex between the beta-lactamase TEM-1 and the beta-lactamase inhibitory protein BLIP has provided an opportunity to put…”
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Structural characterization of SpoIIIAB sporulation-essential protein in Bacillus subtilis
Published in Journal of structural biology (01-05-2018)“…Endospore formation in the Gram-positive bacterium Bacillus subtilis initiates in response to nutrient depletion and involves a series of morphological changes…”
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Binding Hot Spots in the TEM1–BLIP Interface in Light of its Modular Architecture
Published in Journal of molecular biology (19-01-2007)“…Proteins bind one another in aqua’s solution to form tight and specific complexes. Previously we have shown that this is achieved through the modular…”
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Structural insight into the Staphylococcus aureus ATP-driven exporter of virulent peptide toxins
Published in Science advances (01-09-2020)Get full text
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Structural Analysis of the Essential Self-Cleaving Type III Secretion Proteins EscU And SpaS
Published in Nature (London) (28-05-2009)“…During infection by Gram-negative pathogenic bacteria, the type III secretion system (T3SS) is assembled to allow for the direct transmission of bacterial…”
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Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II
Published in Biochemistry (Easton) (22-10-1991)“…One- and two-dimensional NMR techniques were used to study both the influence of mutations on the structure of recombinant normal cardiac troponin C (cTnC3)…”
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