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Article ; Online: Candidate molecular targets uncovered in mouse lifespan extension studies.

Vedunova, Maria / Borysova, Olga / Kozlov, Grigory / Zharova, Anna-Maria / Morgunov, Ivan / Moskalev, Alexey

2024 , Page(s) 1–16

Abstract: Introduction: Multiple interventions have demonstrated an increase in mouse lifespan. However, non-standardized controls, sex or strain-specific factors, and insufficient focus on targets, hinder the translation of these findings into clinical ... ...

Abstract	Introduction: Multiple interventions have demonstrated an increase in mouse lifespan. However, non-standardized controls, sex or strain-specific factors, and insufficient focus on targets, hinder the translation of these findings into clinical applications. Areas covered: We examined the effects of genetic and drug-based interventions on mice from databases DrugAge, GenAge, the Mouse Phenome Database, and publications from PubMed that led to a lifespan extension of more than 10%, identifying specific molecular targets that were manipulated to achieve the maximum lifespan in mice. Subsequently, we characterized 10 molecular targets influenced by these interventions, with particular attention given to clinical trials and potential indications for each. Expert opinion: To increase the translational potential of mice life-extension studies to clinical research several factors are crucial: standardization of mice lifespan research approaches, the development of clear criteria for control and experimental groups, the establishment of criteria for potential geroprotectors, and focusing on targets and their clinical application. Pinpointing the targets affected by geroprotectors helps in understanding species-specific differences and identifying potential side effects, ensuring the safety and effectiveness of clinical trials. Additionally, target review facilitates the optimization of treatment protocols and the evaluation of the clinical feasibility of translating research findings into practical therapies for humans.
Language	English
Publishing date	2024-04-30
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	2055208-7
ISSN	1744-7631 ; 1472-8222
ISSN (online)	1744-7631
ISSN	1472-8222
DOI	10.1080/14728222.2024.2346597
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Article ; Online: Optically stimulated electron paramagnetic resonance: Simplicity, versatility, information content.

Kozlov, V O / Fomin, A A / Ryzhov, I I / Kozlov, G G

Journal of magnetic resonance (San Diego, Calif. : 1997)

2023 Volume 351, Page(s) 107427

Abstract: A simple technique for observing optically stimulated electron paramagnetic resonance (OSEPR) is proposed and investigated. The versatility and information content of the described technique is demonstrated by the example of the OSEPR spectra of systems ... ...

Abstract	A simple technique for observing optically stimulated electron paramagnetic resonance (OSEPR) is proposed and investigated. The versatility and information content of the described technique is demonstrated by the example of the OSEPR spectra of systems that are unpopular for this type of spectroscopy: a crystal with rare-earth ions Nd
Language	English
Publishing date	2023-04-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	1469665-4
ISSN	1096-0856 ; 1557-8968 ; 1090-7807 ; 0022-2364
ISSN (online)	1096-0856 ; 1557-8968
ISSN	1090-7807 ; 0022-2364
DOI	10.1016/j.jmr.2023.107427
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Article ; Online: Burst kinetics and CNNM binding are evolutionarily conserved properties of phosphatases of regenerating liver.

Fakih, Rayan / Goldstein, Robert H / Kozlov, Guennadi / Gehring, Kalle

The Journal of biological chemistry

2023 Volume 299, Issue 4, Page(s) 103055

Abstract: Phosphatases of regenerating liver (PRL or PTP4A) are a family of enigmatic protein phosphatases implicated in cell growth and metabolism. Despite their relevance in metastatic cancer, much remains unknown about the PRL family. They act as ... ...

Abstract	Phosphatases of regenerating liver (PRL or PTP4A) are a family of enigmatic protein phosphatases implicated in cell growth and metabolism. Despite their relevance in metastatic cancer, much remains unknown about the PRL family. They act as pseudophosphatases to regulate the CNNM family of magnesium transporters yet also have enzymatic activity on unknown substrates. In mammals, PRLs are mostly found trapped in an intermediate state that regulates their pseudophosphatase activity. Phosphocysteine, which is formed as an intermediate in the phosphatase catalytic cycle, is inefficiently hydrolyzed leading to burst enzyme kinetics and turnover numbers of less than one per hour. In flies, PRLs have recently been shown to have neuroprotective and neurodevelopmental roles raising the question whether they act as phosphatases, pseudophosphatases, or both. Here, we characterize the evolutionary development of PRLs and ask whether their unique structural and functional properties are conserved. We purified recombinant PRL proteins from 15 phylogenetically diverse organisms and characterized their catalytic activities and ability to bind CNNM proteins. We observed PRLs from humans to amoebae form a stable phosphocysteine intermediate and exhibit burst kinetics. Isothermal titration calorimetry experiments confirmed that the PRL-CNNM interaction is broadly conserved with nanomolar affinity in vertebrates. Lastly, we determined the crystal structure of the Drosophila melanogaster PRL-CNNM complex and identified mutants that specifically impair either phosphatase activity or CNNM binding. Our results reveal the unique properties of PRLs are conserved throughout the animal kingdom and open the door to using model organisms to dissect PRL function in cell signaling.
MeSH term(s)	Animals ; Humans ; Protein Tyrosine Phosphatases/metabolism ; Kinetics ; Drosophila melanogaster/metabolism ; Signal Transduction ; Liver/metabolism ; Mammals/metabolism
Chemical Substances	Protein Tyrosine Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2023-02-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.103055
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Article: Use of industrial composts for the degradative disposal of pesticides

Kozlov, Grigorii / Alekseev, Elisey / Chermenskaya, Taisiya

Biocatalysis and agricultural biotechnology. 2022 July, v. 42

2022

Abstract: Destruction of pesticides using municipal solid waste (MSW) composting is one of the only rational uses for such waste. Voluminous production of compost featuring high heavy-metal-content, and negative costs of such material, make it possible to ... ...

Abstract	Destruction of pesticides using municipal solid waste (MSW) composting is one of the only rational uses for such waste. Voluminous production of compost featuring high heavy-metal-content, and negative costs of such material, make it possible to inexpensively implement certain large-scale processes at minimal cost. One of these is bioremediation of pesticides which, for various reasons (banned, expired, fall in demand, loss of activity, etc.), cannot be used as intended. An important aspect, however, is that not all pesticides are successfully degraded using MSW industrial compost. Mandatory checks are necessary to ensure that methods are effective for each active substance present in the materials undergoing remediation or destruction. This paper presents research results on the degradation of thiamethoxam, clothianidin, fludioxonil, and E-azoxystrobin using industrial composts produced at the ‘SPbGUP MPBO-2’ waste facility (Yanino region, St. Petersburg, Russia). It was shown that the compost contains microorganisms previously described in the literature as degraders of one or more of the pesticides analyzed. These include fungi of the genera Cladosporium and Phanerochaete. A number of degradative bacteria are also present, such as: Stenotrophomonas maltophilia; Bacillus subtilis and another Bacillus spp.; Pseudomonas; Achromobacter; Mesorhizobium; Microbacterium; and Pseudoxanthomonas. Degradation of thiamethoxam and clothianidin in compost was shown. A resistance to degradation, however, was noted with fludioxonil and E-azoxystrobin.
Keywords	Achromobacter ; Bacillus subtilis ; Cladosporium ; Mesorhizobium ; Microbacterium ; Phanerochaete ; Pseudomonas ; Pseudoxanthomonas ; Russia ; Stenotrophomonas maltophilia ; active ingredients ; agricultural biotechnology ; biocatalysis ; bioremediation ; clothianidin ; composts ; fludioxonil ; municipal solid waste ; thiamethoxam
Language	English
Dates of publication	2022-07
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	2642052-1
ISSN	1878-8181
ISSN	1878-8181
DOI	10.1016/j.bcab.2022.102378
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Calnexin cycle - structural features of the ER chaperone system.

Kozlov, Guennadi / Gehring, Kalle

The FEBS journal

2020 Volume 287, Issue 20, Page(s) 4322–4340

Abstract: The endoplasmic reticulum (ER) is the major folding compartment for secreted and membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for folding N-glycosylated proteins. Recent structures of components of the calnexin ... ...

Abstract	The endoplasmic reticulum (ER) is the major folding compartment for secreted and membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for folding N-glycosylated proteins. Recent structures of components of the calnexin cycle have deepened our understanding of quality control mechanisms and protein folding pathways in the ER. In the calnexin cycle, proteins carrying monoglucosylated glycans bind to the lectin chaperones calnexin and calreticulin, which recruit a variety of function-specific chaperones to mediate protein disulfide formation, proline isomerization, and general protein folding. Upon trimming by glucosidase II, the glycan without an inner glucose residue is no longer able to bind to the lectin chaperones. For proteins that have not yet folded properly, the enzyme UDP-glucose:glycoprotein glucosyltransferase (UGGT) acts as a checkpoint by adding a glucose back to the N-glycan. This allows the misfolded proteins to re-associate with calnexin and calreticulin for additional rounds of chaperone-mediated refolding and prevents them from exiting the ERs. Here, we review progress in structural studies of the calnexin cycle, which reveal common features of how lectin chaperones recruit function-specific chaperones and how UGGT recognizes misfolded proteins.
MeSH term(s)	Animals ; Calnexin/chemistry ; Calnexin/metabolism ; Endoplasmic Reticulum/metabolism ; Humans ; Molecular Chaperones/metabolism
Chemical Substances	Molecular Chaperones ; Calnexin (139873-08-8)
Language	English
Publishing date	2020-04-27
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15330
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Article: Calnexin cycle – structural features of the ER chaperone system

Kozlov, Guennadi / Gehring, Kalle

FEBS journal. 2020 Oct., v. 287, no. 20

2020

Abstract: The endoplasmic reticulum (ER) is the major folding compartment for secreted and membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for folding N‐glycosylated proteins. Recent structures of components of the calnexin ... ...

Abstract	The endoplasmic reticulum (ER) is the major folding compartment for secreted and membrane proteins and is the site of a specific chaperone system, the calnexin cycle, for folding N‐glycosylated proteins. Recent structures of components of the calnexin cycle have deepened our understanding of quality control mechanisms and protein folding pathways in the ER. In the calnexin cycle, proteins carrying monoglucosylated glycans bind to the lectin chaperones calnexin and calreticulin, which recruit a variety of function‐specific chaperones to mediate protein disulfide formation, proline isomerization, and general protein folding. Upon trimming by glucosidase II, the glycan without an inner glucose residue is no longer able to bind to the lectin chaperones. For proteins that have not yet folded properly, the enzyme UDP‐glucose:glycoprotein glucosyltransferase (UGGT) acts as a checkpoint by adding a glucose back to the N‐glycan. This allows the misfolded proteins to re‐associate with calnexin and calreticulin for additional rounds of chaperone‐mediated refolding and prevents them from exiting the ERs. Here, we review progress in structural studies of the calnexin cycle, which reveal common features of how lectin chaperones recruit function‐specific chaperones and how UGGT recognizes misfolded proteins.
Keywords	calnexin ; calreticulin ; disulfides ; endoplasmic reticulum ; glucose ; isomerization ; polysaccharides ; proline ; quality control
Language	English
Dates of publication	2020-10
Size	p. 4322-4340.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	NAL-AP-2-clean ; REVIEW
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15330
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: The double lives of phosphatases of regenerating liver: A structural view of their catalytic and noncatalytic activities.

Gehring, Kalle / Kozlov, Guennadi / Yang, Meng / Fakih, Rayan

The Journal of biological chemistry

2021 Volume 298, Issue 1, Page(s) 101471

Abstract: Phosphatases of regenerating liver (PRLs) are protein phosphatases involved in the control of cell growth and migration. They are known to promote cancer metastasis but, despite over 20 years of study, there is still no consensus about their mechanism of ...

Abstract	Phosphatases of regenerating liver (PRLs) are protein phosphatases involved in the control of cell growth and migration. They are known to promote cancer metastasis but, despite over 20 years of study, there is still no consensus about their mechanism of action. Recent work has revealed that PRLs lead double lives, acting both as catalytically active enzymes and as pseudophosphatases. The three known PRLs belong to the large family of cysteine phosphatases that form a phosphocysteine intermediate during catalysis. Uniquely to PRLs, this intermediate is stable, with a lifetime measured in hours. As a consequence, PRLs have very little phosphatase activity. Independently, PRLs also act as pseudophosphatases by binding CNNM membrane proteins to regulate magnesium homeostasis. In this function, an aspartic acid from CNNM inserts into the phosphatase catalytic site of PRLs, mimicking a substrate-enzyme interaction. The delineation of PRL pseudophosphatase and phosphatase activities in vivo was impossible until the recent identification of PRL mutants defective in one activity or the other. These mutants showed that CNNM binding was sufficient for PRL oncogenicity in one model of metastasis, but left unresolved its role in other contexts. As the presence of phosphocysteine prevents CNNM binding and CNNM-binding blocks catalytic activity, these two activities are inherently linked. Additional studies are needed to untangle the intertwined catalytic and noncatalytic functions of PRLs. Here, we review the current understanding of the structure and biophysical properties of PRL phosphatases.
MeSH term(s)	Animals ; Catalysis ; Humans ; Liver/enzymology ; Liver/metabolism ; Membrane Proteins/metabolism ; Neoplasms/enzymology ; Neoplasms/pathology ; Protein Tyrosine Phosphatases/metabolism
Chemical Substances	Membrane Proteins ; Protein Tyrosine Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2021-12-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.101471
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Article ; Online: Dimerization of the CNNM extracellular domain.

Shahsavan, Ashkan / Lee, Emma L / Illes, Katalin / Kozlov, Guennadi / Gehring, Kalle

Protein science : a publication of the Protein Society

2023 Volume 33, Issue 2, Page(s) e4860

Abstract: Cystathionine- ...

Abstract	Cystathionine-
MeSH term(s)	Humans ; Mice ; Animals ; Dimerization ; Magnesium/chemistry ; Mutation ; Membrane Transport Proteins ; Homeostasis ; Protein Serine-Threonine Kinases/genetics ; TRPM Cation Channels/genetics ; Cation Transport Proteins/chemistry
Chemical Substances	Magnesium (I38ZP9992A) ; Membrane Transport Proteins ; TRPM7 protein, human (EC 2.7.11.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TRPM Cation Channels ; CNNM4 protein, human ; Cation Transport Proteins
Language	English
Publishing date	2023-12-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.4860
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: LARP1 and LARP4: up close with PABP for mRNA 3' poly(A) protection and stabilization.

Mattijssen, Sandy / Kozlov, Guennadi / Fonseca, Bruno D / Gehring, Kalle / Maraia, Richard J

RNA biology

2021 Volume 18, Issue 2, Page(s) 259–274

Abstract: La-related proteins (LARPs) share a La motif (LaM) followed by an RNA recognition motif (RRM). Together these are termed the La-module that, in the prototypical nuclear La protein and LARP7, mediates binding to the UUU-3'OH termination motif of nascent ... ...

Abstract	La-related proteins (LARPs) share a La motif (LaM) followed by an RNA recognition motif (RRM). Together these are termed the La-module that, in the prototypical nuclear La protein and LARP7, mediates binding to the UUU-3'OH termination motif of nascent RNA polymerase III transcripts. We briefly review La and LARP7 activities for RNA 3' end binding and protection from exonucleases before moving to the more recently uncovered poly(A)-related activities of LARP1 and LARP4. Two features shared by LARP1 and LARP4 are direct binding to poly(A) and to the cytoplasmic poly(A)-binding protein (PABP, also known as PABPC1). LARP1, LARP4 and other proteins involved in mRNA translation, deadenylation, and decay, contain PAM2 motifs with variable affinities for the MLLE domain of PABP. We discuss a model in which these PABP-interacting activities contribute to poly(A) pruning of active mRNPs. Evidence that the SARS-CoV-2 RNA virus targets PABP, LARP1, LARP 4 and LARP 4B to control mRNP activity is also briefly reviewed. Recent data suggests that LARP4 opposes deadenylation by stabilizing PABP on mRNA poly(A) tails. Other data suggest that LARP1 can protect mRNA from deadenylation. This is dependent on a PAM2 motif with unique characteristics present in its La-module. Thus, while nuclear La and LARP7 stabilize small RNAs with 3' oligo(U) from decay, LARP1 and LARP4 bind and protect mRNA 3' poly(A) tails from deadenylases through close contact with PABP.
MeSH term(s)	Amino Acid Motifs ; Autoantigens/metabolism ; Humans ; Phylogeny ; Poly A ; Poly(A)-Binding Proteins/metabolism ; Protein Binding ; Protein Biosynthesis ; Protein Domains ; RNA Stability ; RNA, Messenger/metabolism ; RNA, Viral/metabolism ; Ribonucleoproteins/metabolism ; SARS-CoV-2/genetics ; SS-B Antigen
Chemical Substances	Autoantigens ; Larp7 protein, human ; Poly(A)-Binding Proteins ; RNA, Messenger ; RNA, Viral ; Ribonucleoproteins ; messenger ribonucleoprotein ; Poly A (24937-83-5)
Language	English
Publishing date	2021-01-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Review
ZDB-ID	2159587-2
ISSN	1555-8584 ; 1555-8584
ISSN (online)	1555-8584
ISSN	1555-8584
DOI	10.1080/15476286.2020.1868753
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Article ; Online: Raman scattering model of the spin noise.

Kozlov, G G / Fomin, A A / Petrov, M Yu / Ryzhov, I I / Zapasskii, V S

Optics express

2021 Volume 29, Issue 4, Page(s) 4770–4782

Abstract: The mechanism of formation of the polarimetric signal observed in the spin noise spectroscopy (SNS) is analyzed from the viewpoint of the light scattering theory. A rigorous calculation of the polarimetric signal (Faraday rotation or ellipticity) ... ...

Abstract	The mechanism of formation of the polarimetric signal observed in the spin noise spectroscopy (SNS) is analyzed from the viewpoint of the light scattering theory. A rigorous calculation of the polarimetric signal (Faraday rotation or ellipticity) recorded in the SNS is presented in the approximation of single scattering. We show that it is most correctly to consider this noise as a result of scattering of the probe light beam by fluctuating susceptibility of the medium. Fluctuations of the gyrotropic (antisymmetric) part of the susceptibility tensor lead to appearance of the typical for the SNS Faraday rotation noise at the Larmor frequency. At the same time, fluctuations of linear anisotropy of the medium (symmetric part of the susceptibility tensor) give rise to the ellipticity noise of the probe beam spectrally localized at the double Larmor frequency. The results of the theoretical analysis well agree with the experimental data on the ellipticity noise in cesium vapor.
Language	English
Publishing date	2021-01-28
Publishing country	United States
Document type	Journal Article
ZDB-ID	1491859-6
ISSN	1094-4087 ; 1094-4087
ISSN (online)	1094-4087
ISSN	1094-4087
DOI	10.1364/OE.415034
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