Mechanism to disrupt ESCRT-mediated intracellular trafficking through Vps28-small molecules interaction: an in silico approach.

The ESCRT (Endosomal Sorting Complex Required for Transport) machinery comprising protein complexes ESCRT-0 to ESCRT-III and Vps4 plays a pivotal role in intracellular trafficking, a process of endocytosing cell surface proteins into the cell for various biological activities. The ESCRT protein complexes are sequentially assembled which interact amongst each other to form a functional ESCRT machinery. Deregulation of these events are shown to be involved in various disease development including tumor formation and viral infections.

SPIKENET: An Evidence-Based Therapy for Long COVID.

The COVID-19 pandemic has been one of the most impactful events in our lifetime, caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Multiple SARS-CoV-2 variants were reported globally, and a wide range of symptoms existed. Individuals who contract COVID-19 continue to suffer for a long time, known as long COVID or post-acute sequelae of COVID-19 (PASC).

Age and Sex in the Development of Hepatic Encephalopathy: Role of Alcohol.

Hepatic encephalopathy (HE) is a neurological condition linked to liver failure. Acute HE (Type A) occurs with acute liver failure, while chronic HE (Type C) is tied to cirrhosis and portal hypertension. HE treatments lag due to gaps in understanding its development by gender and age.

Mechanism of Multi-Organ Injury in Experimental COVID-19 and Its Inhibition by a Small Molecule Peptide.

Severe disease from SARS-CoV-2 infection often progresses to multi-organ failure and results in an increased mortality rate amongst these patients. However, underlying mechanisms of SARS- CoV-2-induced multi-organ failure and subsequent death are still largely unknown. Cytokine storm, increased levels of inflammatory mediators, endothelial dysfunction, coagulation abnormalities, and infiltration of inflammatory cells into the organs contribute to the pathogenesis of COVID-19.

Catalytically active lead(ii)-imidazolium coordination assemblies with diversified lead(ii) coordination geometries.

Five Pb(ii)-imidazolium carboxylate coordination assemblies with novel structural motifs were derived from the reaction between the corresponding flexible, semi flexible or rigid imidazolium carboxylic acid ligands and lead nitrate. The imidazolium linker present in these molecules likely plays a triple role such as the counter ion to balance the metal charge, the ligand being an integral part of the final product and the catalyst facilitating carbon-carbon bond formation reaction. These lead-imidazolium coordination assemblies exhibit, variable chemical and thermal stabilities, as well as catalytic activity.

Photoluminescent calcium azolium carboxylates with diversified calcium coordination geometry and thermal stability.

Despite the popularity and versatility of transition-metal–azolium carboxylate coordination polymers, there are very few examples of group 2 complexes supported by azolium carboxylate ligands in the literature, and there are none featuring luminescent calcium azolium carboxylates. New ionic calcium coordination networks, {[Ca2(L(1))2(H2O)4](Br)4·6H2O}∞ (1), {[(L(3))2Ca(H2O)2]2(Br)2}∞ (3), {[(L(4))2Ca(H2O)2]2(Br)2}∞ (4), and {[(L(5))2Ca3(Na)(H2O)9(Cl)](Br)6·2H2O}∞ (5) along with binuclear {[Ca2(L(2))2(H2O)9](Br)4·4H2O} (2), and trinuclear {[(L(6))2Ca3(H2O)9](Br)6} (6) were isolated from the reaction between the corresponding azolium carboxylates and calcium carbonate in aqueous solution. 1–6 were characterized by FT-IR, NMR, TGA, UV-vis, fluorescence and single crystal X-ray diffraction techniques.

Crystal structure of XoLAP, a leucine aminopeptidase, from Xanthomonas oryzae pv. oryzae.

Aminopeptidases are metalloproteinases that degrade N-terminal residues from protein and play important roles in cell growth and development by controlling cell homeostasis and protein maturation. We determined the crystal structure of XoLAP, a leucyl aminopeptidase, at 2.6 Å resolution from Xanthomonas oryzae pv.

Luminescent imidazolium carboxylate supported aggregate and infinite coordination networks of copper and zinc.

The new copper dimer [LCu(DMF)]2(NO3)4(H2O)(DMF)2 (4), where L = [{1,1'-(CH2)2-C14H8)-3,3'-(CH2CO2)2}{(HCN)2CH}], and porous coordination polymers [{L2Cu(OH2)2}2Br2]x (5) and [{L2Zn(OH2)2}2Br2]x (6) have been isolated from reactions of luminescent imidazolium carboxylate ligand, LH2Br2 (3) and the corresponding metal precursors. The reaction between Cu(NO3)2·3H2O and LH2Br2 (3) in DMF at 100 °C yielded bluish green crystals of tetracationic discrete copper dimer 4, the structure of which contains a rare tetracationic [(DMF)Cu(ii)]2 dimer unit that is bridged by four carboxylates of two L in a "paddle-wheel" structure. When the reaction was carried out in the presence of a water-ethanol-methanol mixture, light green crystals of 5 were obtained.

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of aspartyl aminopeptidase from the apeB gene of Pseudomonas aeruginosa. Retraction.

The article by Natarajan & Mathews [(2012) Acta Cryst. F68, 207–210] is retracted.

(3-Ethyl-6,7-dimeth-oxy-naphthalen-1-yl)(phen-yl)methanone.

The asymetric unit of the title mol-ecule, C(21)H(20)O(3), contains two crystallographically independent mol-ecules, A and B, which differ in the orientation of the ethyl group substituted on the naphthalene system; the dihedral angles between the ethyl group and the naphthalene system are 7.4 (3) and 68.1 (3)°, respectively, for mol-ecules A and B.

4-Amino-3-(4-chloro-phen-yl)-1H-1,2,4-triazole-5(4H)-thione.

In the title compound, C(8)H(7)ClN(4)S, the benzene ring is statistically disordered over two conformations rotated about the Cl-C⋯C-C axis, which subtend dihedral angles of 24.7 (3) and 9.9 (2) ° with respect to the triazole ring.

(Z)-2-[(4-Methyl-phen-yl)sulfon-yl]-1,2-diphenyl-ethene-selenol.

In the title compound, C(21)H(18)O(2)SSe, the dihedral angle between the cis phenyl rings is 64.3 (1)° and those between the toluene and the phenyl rings are 21.1 (2) and 72.

1'-Methyl-4'-phenyl-2''-sulfanylidene-dispiro-[indoline-3,2'-pyrrolidine-3',5''-1,3-thia-zolidine]-2,4''-dione.

The title compound, C(20)H(17)N(3)O(2)S(2), crystallizes with two mol-ecules in the asymmetric unit. The pyrrolo-dine rings have envelope conformations in both mol-ecules, the N atoms deviating by 0.574 (3) and 0.

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of aspartyl aminopeptidase from the apeB gene of Pseudomonas aeruginosa.

Aminopeptidases (APs) are a group of exopeptidases that catalyze the removal of amino acids from the N-termini of proteins and peptides. The APs are ubiquitous in nature and are of critical biological and medical importance because of their key role in protein degradation. Pseudomonas aeruginosa aspartyl aminopeptidase (PaAAP), which is encoded by the apeB gene, was expressed in Escherichia coli, purified and crystallized using the microbatch method.

4-({(E)-[2-(But-3-en-1-yl)-1-(prop-2-en-1-yl)-4-sulfanyl-1H-imidazol-5-yl]methyl-idene}amino)-3-phenyl-1H-1,2,4-triazole-5(4H)-thione.

In the title compound, C(19)H(20)N(6)S(2), the dihedral angle between the phenyl and triazole rings is 24.1 (2)° while the dihedral angles between the imidazole ring and the triazole and phenyl rings are 39.9 (2) and 55.

1-Benzoyl-4-(4-methyl-phen-yl)phthal-azine.

In the title mol-ecule, C(22)H(16)N(2)O, the tolyl and benzoyl rings make dihedral angles 50.2 (5) and 56.4 (5)°, respectively, with the phthalazine ring system while the dihedral angle between the tolyl and benzoyl rings is 0.

Crystallization and preliminary X-ray crystallographic analysis of β-ketoacyl-ACP synthase I (XoFabB) from Xanthomonas oryzae pv. oryzae.

The proteins in the fatty-acid synthesis pathway in bacteria have significant potential as targets for the development of antibacterial agents. An essential elongation step in fatty-acid synthesis is performed by β-ketoacyl-acyl carrier protein synthase I (FabB). The organism Xanthomonas oryzae pv.

Crystal structure of malonyl CoA-Acyl carrier protein transacylase from Xanthomanous oryzae pv. oryzae and its proposed binding with ACP.

Xanthomonas oryzae pv. oryzae (Xoo) is a plant bacterial pathogen that causes bacterial blight (BB) disease, resulting in serious production losses of rice. The crystal structure of malonyl CoA-acyl carrier protein transacylase (XoMCAT), encoded by the gene fabD (Xoo0880) from Xoo, was determined at 2.

2,4-Diamino-5-(4-chloro-phen-yl)-6-ethyl-pyrimidin-1-ium 2-propanamido-benzoate.

In the title salt, C(12)H(14)ClN(4) (+)·C(10)H(10)NO(3) (-), zwitterionic N-H⋯O inter-actions form an R(2) (2)(8) ring. The crystal structure is stabilized by N-H⋯O and N-H⋯N hydrogen bonds involving two different eight-membered rings. An N-H⋯O inter-action occurs between the pyrimidine ring (donor) and carboxyl-ate group (acceptor) while the other ring is formed by N-H⋯N inter-actions, which form a dimer between two symmetry-related salts.

2,4-Diamino-5-(4-chloro-phen-yl)-6-ethyl-pyrimidin-1-ium 2-acet-amido-benzoate.

The title compound, C(12)H(14)ClN(4) (+)·C(9)H(8)NO(3) (-), is a salt with a 1:1 ratio of cation and anion components inter-acting with each other forming an R(2) (2)(8) ring motif. The crystal structure is stabilized by hydrogen bonds (N-H⋯O) involving two different eight-membered rings. One of them is formed between the pyrimidine ring (donor) and the carboxylate group (acceptor) from the benzoate, whereas the other ring is formed by N-H⋯O interactions, which help to form a dimer between two symmetry-related salts in the unit cell.

3-Nitroso-2,4,6,8-tetra-phenyl-3,7-diaza-bicyclo-[3.3.1]nonan-9-one.

In the title compound, C(31)H(27)N(3)O(2), the two piperidine rings fused to each other each adopt a slightly distorted chair conformation. The phenyl rings on the N-unsubstituted piperidine ring occupy an equatorial position, while those on the N-nitroso-substituted piperidine ring are in axial positions. The NO group is approximately coplanar with the piperidine ring with a maximum deviation of 0.

Ethyl 3-methyl-2,6-diphenyl-piperidine-1-carboxyl-ate.

In the title compound, C(21)H(25)NO(2), the piperidine ring adopts a twisted boat conformation characterized by puckering parameters θ = 89.5 (1) and ϕ = 257.5 (2)°.

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of the co-chaperonin XoGroES from Xanthomonas oryzae pv. oryzae.

Bacterial blight (BB), a devastating disease caused by Xanthomonas oryzae pv. oryzae (Xoo), causes serious production losses of rice in Asian countries. Protein misfolding may interfere with the function of proteins in all living cells and must be prevented to avoid cellular disaster.