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Article ; Online: Co-Occurrence of Congenital Aniridia Due to Nonsense

Vasilyeva, Tatyana A / Sukhanova, Natella V / Marakhonov, Andrey V / Kuzina, Natalia Yu / Shilova, Nadezhda V / Kadyshev, Vitaly V / Kutsev, Sergey I / Zinchenko, Rena A

International journal of molecular sciences

2023 Volume 24, Issue 21

Abstract: This study aims to present a clinical case involving the unique co-occurrence of congenital aniridia and Down syndrome in a young girl and to analyze the combined impact of these conditions on the patient's phenotype. The investigation involved ... ...

Abstract	This study aims to present a clinical case involving the unique co-occurrence of congenital aniridia and Down syndrome in a young girl and to analyze the combined impact of these conditions on the patient's phenotype. The investigation involved comprehensive pediatric and ophthalmological examinations alongside karyotyping and Sanger sequencing of the
MeSH term(s)	Female ; Humans ; Child ; Down Syndrome/complications ; PAX6 Transcription Factor/genetics ; Chromosomes, Human, Pair 21/genetics ; Trisomy ; Aniridia/complications ; Aniridia/genetics ; Eye Proteins/genetics ; Homeodomain Proteins/genetics ; Pedigree ; Mutation
Chemical Substances	PAX6 Transcription Factor ; Eye Proteins ; Homeodomain Proteins ; PAX6 protein, human
Language	English
Publishing date	2023-10-24
Publishing country	Switzerland
Document type	Case Reports
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms242115527
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Article ; Online: Plant Polysaccharide Array for Studying Carbohydrate-Binding Proteins.

Nikiforova, Anna V / Golovchenko, Victoria V / Mikshina, Polina V / Patova, Olga A / Gorshkova, Tatyana A / Bovin, Nikolai V / Shilova, Nadezhda V

Biochemistry. Biokhimiia

2022 Volume 87, Issue 9, Page(s) 890–902

Abstract: The specificity of the most plant carbohydrate-binding proteins (CBP), many of which are known only through bioinformatic analysis of the genome, has either not been studied at all or characterized to a limited extent. The task of deciphering the ... ...

Abstract	The specificity of the most plant carbohydrate-binding proteins (CBP), many of which are known only through bioinformatic analysis of the genome, has either not been studied at all or characterized to a limited extent. The task of deciphering the carbohydrate specificity of the proteins can be solved using glycoarrays composed of many tens or even hundreds of glycans immobilized on a glass surface. Plant carbohydrates are the most significant natural ligands for plant proteins; this work shows that plant polysaccharides without additional modification can be immobilized on the surface, bearing N-hydroxysuccinimide activated carboxyl groups. As a result, an array of 113 well-characterized polysaccharides isolated from various plant cell walls, 23 mono- and oligosaccharides - components of polysaccharides, and glycans - ligands for widely known plant lectins was designed. Upon chemical immobilization of polysaccharides, their functional activity was preserved, which was confirmed by the results of interaction with antibodies and the plant lectin ricin. Using the constructed array, a previously unknown ability of ricin to bind polysaccharides was found, which significantly expands the knowledge of its specificity, and it was also found that a large variety of antibodies to plant polysaccharides are present in human peripheral blood.
MeSH term(s)	Carbohydrates ; Humans ; Ligands ; Plant Lectins ; Polysaccharides/chemistry ; Ricin
Chemical Substances	Carbohydrates ; Ligands ; Plant Lectins ; Polysaccharides ; Ricin (9009-86-3)
Language	English
Publishing date	2022-09-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	1109-5
ISSN	1608-3040 ; 0006-2979 ; 0320-9717
ISSN (online)	1608-3040
ISSN	0006-2979 ; 0320-9717
DOI	10.1134/S0006297922090036
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Article ; Online: Complex Chromosomal Rearrangement Involving Chromosomes 10 and 11, Accompanied by Two Adjacent 11p14.1p13 and 11p13p12 Deletions, Identified in a Patient with WAGR Syndrome.

Marakhonov, Andrey V / Vasilyeva, Tatyana A / Minzhenkova, Marina E / Sukhanova, Natella V / Sparber, Peter A / Andreeva, Natalya A / Teleshova, Margarita V / Baybagisova, Fatima K-M / Shilova, Nadezhda V / Kutsev, Sergey I / Zinchenko, Rena A

International journal of molecular sciences

2023 Volume 24, Issue 23

Abstract: Three years ago, our patient, at that time a 16-month-old boy, was discovered to have bilateral kidney lesions with a giant tumor in the right kidney. Chemotherapy and bilateral nephron-sparing surgery (NSS) for Wilms tumor with nephroblastomatosis was ... ...

Abstract	Three years ago, our patient, at that time a 16-month-old boy, was discovered to have bilateral kidney lesions with a giant tumor in the right kidney. Chemotherapy and bilateral nephron-sparing surgery (NSS) for Wilms tumor with nephroblastomatosis was carried out. The patient also had eye affection, including glaucoma, eye enlargement, megalocornea, severe corneal swelling and opacity, complete aniridia, and nystagmus. The diagnosis of WAGR syndrome was suspected. De novo complex chromosomal rearrangement with balanced translocation t(10,11)(p15;p13) and a pericentric inversion inv(11)(p13q12), accompanied by two adjacent 11p14.1p13 and 11p13p12 deletions, were identified. Deletions are raised through the complex molecular mechanism of two subsequent rearrangements affecting chromosomes 11 and 10. WAGR syndrome diagnosis was clinically and molecularly confirmed, highlighting the necessity of comprehensive genetic testing in patients with congenital aniridia and/or WAGR syndrome.
MeSH term(s)	Male ; Humans ; Infant ; WAGR Syndrome/diagnosis ; WAGR Syndrome/genetics ; WAGR Syndrome/pathology ; Chromosome Deletion ; Aniridia/diagnosis ; Aniridia/genetics ; Wilms Tumor/genetics ; Kidney Neoplasms/genetics ; Chromosomes, Human, Pair 11/genetics ; Chromosome Inversion
Language	English
Publishing date	2023-11-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms242316923
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Article ; Online: Epidemiology of

Vasilyeva, Tatyana A / Marakhonov, Andrey V / Voskresenskaya, Anna A / Kadyshev, Vitaly V / Sukhanova, Natella V / Minzhenkova, Marina E / Shilova, Nadezhda V / Latyshova, Alla A / Ginter, Evgeny K / Kutsev, Sergey I / Zinchenko, Rena A

Genes

2023 Volume 14, Issue 11

Abstract: This study investigates the distribution ... ...

Abstract	This study investigates the distribution of
MeSH term(s)	Humans ; Prevalence ; PAX6 Transcription Factor/genetics ; Aniridia/epidemiology ; Aniridia/genetics ; WAGR Syndrome/genetics ; Chromosome Deletion
Chemical Substances	PAX6 Transcription Factor ; PAX6 protein, human
Language	English
Publishing date	2023-11-04
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527218-4
ISSN	2073-4425 ; 2073-4425
ISSN (online)	2073-4425
ISSN	2073-4425
DOI	10.3390/genes14112041
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Article ; Online: Removal of natural anti-αGal antibodies elicits protective immunity against Gram-negative bacterial infections.

Olivera-Ardid, Sara / Bello-Gil, Daniel / Perez-Cruz, Magdiel / Costa, Cristina / Camoez, Mariana / Dominguez, M Angeles / Ferrero-Alves, Yara / Vaquero, Jose Miguel / Khasbiullina, Nailya / Shilova, Nadezhda V / Bovin, Nicolai V / Mañez, Rafael

Frontiers in immunology

2023 Volume 14, Page(s) 1232924

Abstract: Antibody-dependent enhancement (ADE) of bacterial infections occurs when blocking or inhibitory antibodies facilitate the infectivity of pathogens. In humans, antibodies involved in ADE of bacterial infections may include those naturally produced against ...

Abstract	Antibody-dependent enhancement (ADE) of bacterial infections occurs when blocking or inhibitory antibodies facilitate the infectivity of pathogens. In humans, antibodies involved in ADE of bacterial infections may include those naturally produced against Galα1-3Galβ1-4GlcNAcβ (αGal). Here, we investigate whether eliminating circulating anti-αGal antibodies using a soluble αGal glycopolymer confers protection against Gram-negative bacterial infections. We demonstrated that the
MeSH term(s)	Humans ; Animals ; Mice ; Escherichia coli ; Punctures ; Immunoglobulin G ; Anti-Bacterial Agents ; Gram-Negative Bacterial Infections
Chemical Substances	Immunoglobulin G ; Anti-Bacterial Agents
Language	English
Publishing date	2023-08-18
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1232924
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Article ; Online: New l-Rhamnose-Binding Lectin from the Bivalve

Mizgina, Tatyana O / Chikalovets, Irina V / Bulanova, Tatyana A / Molchanova, Valentina I / Filshtein, Alina P / Ziganshin, Rustam H / Rogozhin, Eugene A / Shilova, Nadezhda V / Chernikov, Oleg V

Marine drugs

2023 Volume 22, Issue 1

Abstract: In this study, a new l-rhamnose-binding lectin (GYL-R) from the hemolymph of ... ...

Abstract	In this study, a new l-rhamnose-binding lectin (GYL-R) from the hemolymph of bivalve
MeSH term(s)	Animals ; Lectins/pharmacology ; Rhamnose ; Escherichia coli ; Tandem Mass Spectrometry ; Anti-Bacterial Agents/pharmacology ; Bivalvia
Chemical Substances	Lectins ; Rhamnose (QN34XC755A) ; Anti-Bacterial Agents
Language	English
Publishing date	2023-12-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2175190-0
ISSN	1660-3397 ; 1660-3397
ISSN (online)	1660-3397
ISSN	1660-3397
DOI	10.3390/md22010027
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Article ; Online: Antibody-Dependent Enhancement with a Focus on SARS-CoV-2 and Anti-Glycan Antibodies.

Ziganshina, Marina M / Shilova, Nadezhda V / Khalturina, Eugenia O / Dolgushina, Natalya V / V Borisevich, Sergey / Yarotskaya, Ekaterina L / Bovin, Nicolai V / Sukhikh, Gennady T

Viruses

2023 Volume 15, Issue 7

Abstract: Antibody-dependent enhancement (ADE) is a phenomenon where virus-specific antibodies paradoxically cause enhanced viral replication and/or excessive immune responses, leading to infection exacerbation, tissue damage, and multiple organ failure. ADE has ... ...

Abstract	Antibody-dependent enhancement (ADE) is a phenomenon where virus-specific antibodies paradoxically cause enhanced viral replication and/or excessive immune responses, leading to infection exacerbation, tissue damage, and multiple organ failure. ADE has been observed in many viral infections and is supposed to complicate the course of COVID-19. However, the evidence is insufficient. Since no specific laboratory markers have been described, the prediction and confirmation of ADE are very challenging. The only possible predictor is the presence of already existing (after previous infection) antibodies that can bind to viral epitopes and promote the disease enhancement. At the same time, the virus-specific antibodies are also a part of immune response against a pathogen. These opposite effects of antibodies make ADE research controversial. The assignment of immunoglobulins to ADE-associated or virus neutralizing is based on their affinity, avidity, and content in blood. However, these criteria are not clearly defined. Another debatable issue (rather terminological, but no less important) is that in most publications about ADE, all immunoglobulins produced by the immune system against pathogens are qualified as pre-existing antibodies, thus ignoring the conventional use of this term for natural antibodies produced without any stimulation by pathogens. Anti-glycan antibodies (AGA) make up a significant part of the natural immunoglobulins pool, and there is some evidence of their antiviral effect, particularly in COVID-19. AGA have been shown to be involved in ADE in bacterial infections, but their role in the development of ADE in viral infections has not been studied. This review focuses on pros and cons for AGA as an ADE trigger. We also present the results of our pilot studies, suggesting that AGAs, which bind to complex epitopes (glycan plus something else in tight proximity), may be involved in the development of the ADE phenomenon.
MeSH term(s)	Humans ; SARS-CoV-2 ; COVID-19 ; Antibodies, Viral ; Antibody-Dependent Enhancement ; Antibodies, Neutralizing ; Virus Diseases ; Viruses ; Epitopes
Chemical Substances	Antibodies, Viral ; Antibodies, Neutralizing ; Epitopes
Language	English
Publishing date	2023-07-20
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v15071584
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Article ; Online: Structural Characterization of Rat Galectin-5, an N-Tailed Monomeric Proto-Type-like Galectin.

Ruiz, Federico M / Medrano, Francisco J / Ludwig, Anna-Kristin / Kaltner, Herbert / Shilova, Nadezhda V / Bovin, Nicolai V / Gabius, Hans-Joachim / Romero, Antonio

Biomolecules

2021 Volume 11, Issue 12

Abstract: Galectins are multi-purpose effectors acting via interactions with distinct counterreceptors based on protein-glycan/protein recognition. These processes are emerging to involve several regions on the protein so that the availability of a detailed ... ...

Abstract	Galectins are multi-purpose effectors acting via interactions with distinct counterreceptors based on protein-glycan/protein recognition. These processes are emerging to involve several regions on the protein so that the availability of a detailed structural characterization of a full-length galectin is essential. We report here the first crystallographic information on the N-terminal extension of the carbohydrate recognition domain of rat galectin-5, which is precisely described as an N-tailed proto-type-like galectin. In the ligand-free protein, the three amino-acid stretch from Ser2 to Ser5 is revealed to form an extra β-strand (F0), and the residues from Thr6 to Asn12 are part of a loop protruding from strands S1 and F0. In the ligand-bound structure, amino acids Ser2-Tyr10 switch position and are aligned to the edge of the β-sandwich. Interestingly, the signal profile in our glycan array screening shows the sugar-binding site to preferentially accommodate the histo-blood-group B (type 2) tetrasaccharide and N-acetyllactosamine-based di- and oligomers. The crystal structures revealed the characteristically preformed structural organization around the central Trp77 of the CRD with involvement of the sequence signature's amino acids in binding. Ligand binding was also characterized calorimetrically. The presented data shows that the N-terminal extension can adopt an ordered structure and shapes the hypothesis that a ligand-induced shift in the equilibrium between flexible and ordered conformers potentially acts as a molecular switch, enabling new contacts in this region.
MeSH term(s)	Amino Acid Motifs ; Animals ; Carbohydrate Sequence ; Crystallography, X-Ray ; Galectins/chemistry ; Galectins/genetics ; Galectins/metabolism ; Models, Molecular ; Polysaccharides/chemistry ; Polysaccharides/metabolism ; Protein Binding ; Protein Domains ; Protein Multimerization ; Protein Structure, Secondary ; Rats ; Scattering, Small Angle
Chemical Substances	Galectins ; Polysaccharides ; galectin 5
Language	English
Publishing date	2021-12-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom11121854
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Article ; Online: Allergic reactions to tick saliva components in zebrafish model.

Contreras, Marinela / Vaz-Rodrigues, Rita / Mazuecos, Lorena / Villar, Margarita / Artigas-Jerónimo, Sara / González-García, Almudena / Shilova, Nadezhda V / Bovin, Nicolai V / Díaz-Sánchez, Sandra / Ferreras-Colino, Elisa / Pacheco, Iván / Chmelař, Jindřich / Kopáček, Petr / Cabezas-Cruz, Alejandro / Gortázar, Christian / de la Fuente, José

Parasites & vectors

2023 Volume 16, Issue 1, Page(s) 242

Abstract: Background: Alpha-Gal syndrome (AGS) is a tick-borne food allergy caused by IgE antibodies against the glycan galactose-alpha-1,3-galactose (α-Gal) present in glycoproteins and glycolipids from mammalian meat. To advance in the diagnosis and treatment ... ...

Abstract	Background: Alpha-Gal syndrome (AGS) is a tick-borne food allergy caused by IgE antibodies against the glycan galactose-alpha-1,3-galactose (α-Gal) present in glycoproteins and glycolipids from mammalian meat. To advance in the diagnosis and treatment of AGS, further research is needed to unravel the molecular and immune mechanisms underlying this syndrome. The objective of this study is the characterization of tick salivary components and proteins with and without α-Gal modifications involved in modulating human immune response against this carbohydrate. Methods: Protein and α-Gal content were determined in tick saliva components, and proteins were identified by proteomics analysis of tick saliva fractions. Pathophysiological changes were recorded in the zebrafish (Danio rerio) model after exposure to distinct Ixodes ricinus tick salivary components. Serum samples were collected from zebrafish at day 8 of exposure to determine anti-α-Gal, anti-glycan, and anti-tick saliva protein IgM antibody titers by enzyme-linked immunosorbent assay (ELISA). Results: Zebrafish treated with tick saliva and saliva protein fractions combined with non-protein fractions demonstrated significantly higher incidence of hemorrhagic type allergic reactions, abnormal behavioral patterns, or mortality when compared to the phosphate-buffered saline (PBS)-treated control group. The main tick salivary proteins identified in these fractions with possible functional implication in AGS were the secreted protein B7P208-salivary antigen p23 and metalloproteases. Anti-α-Gal and anti-tick salivary gland IgM antibody titers were significantly higher in distinct saliva protein fractions and deglycosylated saliva group when compared with PBS-treated controls. Anti-glycan antibodies showed group-related profiles. Conclusions: Results support the hypothesis that tick salivary biomolecules with and without α-Gal modifications are involved in modulating immune response against this carbohydrate.
MeSH term(s)	Animals ; Humans ; Zebrafish/metabolism ; Saliva ; Galactose ; Immunoglobulin E ; Food Hypersensitivity/etiology ; Ixodes ; Arthropod Proteins ; Immunoglobulin M ; Tick Bites ; Mammals
Chemical Substances	Galactose (X2RN3Q8DNE) ; Immunoglobulin E (37341-29-0) ; Arthropod Proteins ; Immunoglobulin M
Language	English
Publishing date	2023-07-19
Publishing country	England
Document type	Journal Article
ZDB-ID	2409480-8
ISSN	1756-3305 ; 1756-3305
ISSN (online)	1756-3305
ISSN	1756-3305
DOI	10.1186/s13071-023-05874-2
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Article ; Online: Repertoire of glycan-binding placenta-associated antibodies in healthy pregnancy and in pre-eclampsia.

Ziganshina, Marina M / Shilova, Nadezhda V / Khasbiullina, Nailia R / Terentyeva, Anastasia V / Dolgopolova, Elena L / Nokel, Alexey Yu / Yarotskaya, Ekaterina L / Shmakov, Roman G / Bovin, Nicolai V / Sukhikh, Gennady T

Scandinavian journal of immunology

2022 Volume 95, Issue 6, Page(s) e13157

Abstract: A possible mechanism of the immune tolerance in pregnancy is production of blocking antibodies which reside in placenta and protect foetal allogeneic cells from the mother's immune system. Their epitope specificity, as well as the nature of the ... ...

Abstract	A possible mechanism of the immune tolerance in pregnancy is production of blocking antibodies which reside in placenta and protect foetal allogeneic cells from the mother's immune system. Their epitope specificity, as well as the nature of the biomolecules masked by them, is unknown. For better understanding of this phenomenon, we attempted to characterize the specificity of antibodies isolated from placentas of women with healthy pregnancy and pre-eclampsia (PE). It was found that: (1) the repertoire of placental antibodies is significantly less variable and qualitatively different from the peripheral blood; (2) with PE, the repertoire of placental antibodies is narrower than in healthy pregnancy; (3) some antibodies are found almost exclusively in the placenta, and some - only in the placenta of healthy women.
MeSH term(s)	Antibodies ; Epitopes ; Female ; Humans ; Placenta ; Polysaccharides ; Pre-Eclampsia ; Pregnancy
Chemical Substances	Antibodies ; Epitopes ; Polysaccharides
Language	English
Publishing date	2022-03-16
Publishing country	England
Document type	Journal Article
ZDB-ID	120476-2
ISSN	1365-3083 ; 0300-9475
ISSN (online)	1365-3083
ISSN	0300-9475
DOI	10.1111/sji.13157
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