scholarly journals Crystal structure of the novel PaiA N -acetyltransferase from Thermoplasma acidophilum involved in the negative control of sporulation and degradative enzyme production

2011 ◽  
Vol 79 (8) ◽  
pp. 2566-2577 ◽  
Author(s):  
E.V. Filippova ◽  
L. Shuvalova ◽  
G. Minasov ◽  
O. Kiryukhina ◽  
Y. Zhang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Enzyme Production ◽  
Negative Control ◽  
The Novel ◽  
Thermoplasma Acidophilum ◽  
Degradative Enzyme

scholarly journals A novel Bacillus subtilis gene involved in negative control of sporulation and degradative-enzyme production.

1990 ◽  
Vol 172 (4) ◽  
pp. 1783-1790 ◽  
Author(s):  
M Honjo ◽  
A Nakayama ◽  
K Fukazawa ◽  
K Kawamura ◽  
K Ando ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Enzyme Production ◽  
Negative Control ◽  
Degradative Enzyme ◽  
Subtilis Gene

scholarly journals Some Novel Cobalt Diphenylphosphine Complexes: Synthesis, Characterization, and Behavior in the Polymerization of 1,3-Butadiene

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 4067
Author(s):  
Giovanni Ricci ◽  
Giuseppe Leone ◽  
Giorgia Zanchin ◽  
Benedetta Palucci ◽  
Alessandra Forni ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Single Crystals ◽  
The Novel ◽  
X Ray Diffraction ◽  
X Ray ◽  
And Behavior

Some novel cobalt diphenylphosphine complexes were synthesized by reacting cobalt(II) chloride with (2-methoxyethyl)diphenylphosphine, (2-methoxyphenyl)diphenylphosphine, and 2-(1,1-dimethylpropyl)-6-(diphenylphosphino)pyridine. Single crystals suitable for X-ray diffraction studies were obtained for the first two complexes, and their crystal structure was determined. The novel compounds were then used in association with methylaluminoxane (MAO) for the polymerization of 1,3-butadiene, and their behavior was compared with that exhibited in the polymerization of the same monomer by the systems CoCl2(PnPrPh2)2/MAO and CoCl2(PPh3)2/MAO. Some significant differences were observed depending on the MAO/Co ratio used, and a plausible interpretation for such a different behavior is proposed.

scholarly journals Crystal Structure of the Streptomyces coelicolor Sortase E1 Transpeptidase Provides Insight into the Binding Mode of the Novel Class E Sorting Signal

PLoS ONE ◽  
2016 ◽  
Vol 11 (12) ◽  
pp. e0167763 ◽  
Author(s):  
Michele D. Kattke ◽  
Albert H. Chan ◽  
Andrew Duong ◽  
Danielle L. Sexton ◽  
Michael R. Sawaya ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Streptomyces Coelicolor ◽  
Binding Mode ◽  
The Novel ◽  
Sorting Signal ◽  
Insight Into ◽  
Class E

Structural insights into the novel ARM-repeat protein CTNNBL1 and its association with the hPrp19–CDC5L complex

2014 ◽  
Vol 70 (3) ◽  
pp. 780-788 ◽  
Author(s):  
Jae-Woo Ahn ◽  
Sangwoo Kim ◽  
Eun-Jung Kim ◽  
Yeo-Jin Kim ◽  
Kyung-Jin Kim
Keyword(s):  
Crystal Structure ◽  
The Novel ◽  
Molecular Architecture ◽  
Repeat Protein ◽  
Binding Partner ◽  
Catalytic Activation ◽  
Repeat Structure ◽  
Repeat Domain ◽  
Importin Α ◽  
Structural Insights

The hPrp19–CDC5L complex plays a crucial role during human pre-mRNA splicing by catalytic activation of the spliceosome. In order to elucidate the molecular architecture of the hPrp19–CDC5L complex, the crystal structure of CTNNBL1, one of the major components of this complex, was determined. Unlike canonical ARM-repeat proteins such as β-catenin and importin-α, CTNNBL1 was found to contain a twisted and extended ARM-repeat structure at the C-terminal domain and, more importantly, the protein formed a stable dimer. A highly negatively charged patch formed in the N-terminal ARM-repeat domain of CTNNBL1 provides a binding site for CDC5L, a binding partner of the protein in the hPrp19–CDC5L complex, and these two proteins form a complex with a stoichiometry of 2:2. These findings not only present the crystal structure of a novel ARM-repeat protein, CTNNBL1, but also provide insights into the detailed molecular architecture of the hPrp19–CDC5L complex.

Crystal structure of the novel Mg3MnNi2D3−x interstitial deuteride

2011 ◽  
Vol 19 (10) ◽  
pp. 1563-1566 ◽  
Author(s):  
R.V. Denys ◽  
A.R. Riabov ◽  
V.V. Berezovets ◽  
I.V. Koval’chuk ◽  
R. Černý ◽  
...  
Keyword(s):  
Crystal Structure ◽  
The Novel

scholarly journals SARS-CoV-2: preliminary study of infected human nasopharyngeal tissue by high resolution microscopy

2021 ◽  
Vol 18 (1) ◽  
Author(s):  
Brian Mondeja ◽  
Odalys Valdes ◽  
Sonia Resik ◽  
Ananayla Vizcaino ◽  
Emilio Acosta ◽  
...  
Keyword(s):  
High Resolution ◽  
Control Sample ◽  
Negative Control ◽  
High Rate ◽  
Apical Region ◽  
The Novel ◽  
Rt Pcr ◽  
Crown Shape ◽  
Novel Coronavirus ◽  
High Resolution Microscopy

Abstract Background The novel coronavirus SARS-CoV-2 is the etiological agent of COVID-19. This virus has become one of the most dangerous in recent times with a very high rate of transmission. At present, several publications show the typical crown-shape of the novel coronavirus grown in cell cultures. However, an integral ultramicroscopy study done directly from clinical specimens has not been published. Methods Nasopharyngeal swabs were collected from 12 Cuban individuals, six asymptomatic and RT-PCR negative (negative control) and six others from a COVID-19 symptomatic and RT-PCR positive for SARS CoV-2. Samples were treated with an aldehyde solution and processed by scanning electron microscopy (SEM), confocal microscopy (CM) and, atomic force microscopy. Improvement and segmentation of coronavirus images were performed by a novel mathematical image enhancement algorithm. Results The images of the negative control sample showed the characteristic healthy microvilli morphology at the apical region of the nasal epithelial cells. As expected, they do not display virus-like structures. The images of the positive sample showed characteristic coronavirus-like particles and evident destruction of microvilli. In some regions, virions budding through the cell membrane were observed. Microvilli destruction could explain the anosmia reported by some patients. Virus-particles emerging from the cell-surface with a variable size ranging from 80 to 400 nm were observed by SEM. Viral antigen was identified in the apical cells zone by CM. Conclusions The integral microscopy study showed that SARS-CoV-2 has a similar image to SARS-CoV. The application of several high-resolution microscopy techniques to nasopharyngeal samples awaits future use.

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