LIVIVO - Das Suchportal für Lebenswissenschaften

switch to English language
Zurück zur letzten Suche Suchhistorie
Erweiterte Suche

Ihre letzten Suchen

  1. AU="Patra, Dhabaleswar"
  2. AU="Knill, Carly"
  3. AU=Jabbour Elias
  4. AU="Rodríguez-Maresca, Manuel Ángel"
  5. AU="Yang, Chang-Jung"
  6. AU="Atul Kaushik"
  7. AU="Peters, Jaime"
  8. AU="Dorothee von Laer"
  9. AU="Sreeja Attur"
  10. AU=Song Kyung Chul
  11. AU=Klimovich Pavel V.
  12. AU="Jingbo Chen"
  13. AU="Viazlo, Oleksander"
  14. AU="Toshiki Iwabuchi"
  15. AU="Dissanayake, Lakmali"
  16. AU="Michael Denkinger"
  17. AU="Abilio J. F. N. Sobral"
  18. AU="Geller, Alan"
  19. AU=Petrat Sren
  20. AU="Sterling, Shanique"
  21. AU="Qi, Zeqiang"
  22. AU="Thongstisubskul, A"
  23. AU="Daniel C. Schneider, PhD"
  24. AU="Völker, Christoph"
  25. AU="El Aoud, S"
  26. AU="Yi, Tongpei"
  27. AU="Anil K. Mantha"
  28. AU="Artzner, Christoph"
  29. AU=Diana Giovanni
  30. AU="Kinloch, Sabine"
  31. AU="Nuertey, David"
  32. AU="Ojubolamo, Olakunle"

Suchergebnis

Treffer 1 - 10 von insgesamt 18

Suchoptionen

  1. Artikel: Negative Cooperativity and High Affinity in Chitooligosaccharide Binding by a Mycobacterium smegmatis Protein Containing LysM and Lectin Domains

    Patra, Dhabaleswar / Mishra Padmanabh / Vijayan Mamannamana / Surolia Avadhesha

    Biochemistry. 2016 Jan. 12, v. 55, no. 1

    2016  

    Abstract: LysM domains have been recognized in bacteria and eukaryotes as carbohydrate-binding protein modules, but the mechanism of their binding to chitooligosaccharides has been underexplored. Binding of a Mycobacterium smegmatis protein containing a lectin ( ... ...

    Abstract LysM domains have been recognized in bacteria and eukaryotes as carbohydrate-binding protein modules, but the mechanism of their binding to chitooligosaccharides has been underexplored. Binding of a Mycobacterium smegmatis protein containing a lectin (MSL) and one LysM domain to chitooligosaccharides has been studied using isothermal titration calorimetry and fluorescence titration that demonstrate the presence of two binding sites of nonidentical affinities per dimeric MSL-LysM molecule. The affinity of the molecule for chitooligosaccharides correlates with the length of the carbohydrate chain. Its binding to chitooligosaccharides is characterized by negative cooperativity in the interactions of the two domains. Apparently, the flexibility of the long linker that connects the LysM and MSL domains plays a facilitating role in this recognition. The LysM domain in the MSL-LysM molecule, like other bacterial domains but unlike plant LysM domains, recognizes equally well peptidoglycan fragments as well as chitin polymers. Interestingly, in the case presented here, two LysM domains are enough for binding to peptidoglycan in contrast to the three reportedly required by the LysM domains of Bacillus subtilis and Lactococcus lactis. Also, the affinity of the MSL-LysM molecule for chitooligosaccharides is higher than that of LysM–chitooligosaccharide interactions reported so far.
    Schlagwörter Bacillus subtilis ; Lactococcus lactis ; Mycobacterium smegmatis ; bacteria ; binding sites ; calorimetry ; carbohydrate binding ; chitin ; chitooligosaccharides ; eukaryotic cells ; fluorescence ; lectins ; peptidoglycans ; polymers ; titration
    Sprache Englisch
    Erscheinungsverlauf 2016-0112
    Umfang p. 49-61.
    Erscheinungsort American Chemical Society
    Dokumenttyp Artikel
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021%2Facs.biochem.5b00841
    Datenquelle NAL Katalog (AGRICOLA)

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 217: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  2. Artikel ; Online: Negative Cooperativity and High Affinity in Chitooligosaccharide Binding by a Mycobacterium smegmatis Protein Containing LysM and Lectin Domains.

    Patra, Dhabaleswar / Mishra, Padmanabh / Vijayan, Mamannamana / Surolia, Avadhesha

    Biochemistry

    2016  Band 55, Heft 1, Seite(n) 49–61

    Abstract: LysM domains have been recognized in bacteria and eukaryotes as carbohydrate-binding protein modules, but the mechanism of their binding to chitooligosaccharides has been underexplored. Binding of a Mycobacterium smegmatis protein containing a lectin ( ... ...

    Abstract LysM domains have been recognized in bacteria and eukaryotes as carbohydrate-binding protein modules, but the mechanism of their binding to chitooligosaccharides has been underexplored. Binding of a Mycobacterium smegmatis protein containing a lectin (MSL) and one LysM domain to chitooligosaccharides has been studied using isothermal titration calorimetry and fluorescence titration that demonstrate the presence of two binding sites of nonidentical affinities per dimeric MSL-LysM molecule. The affinity of the molecule for chitooligosaccharides correlates with the length of the carbohydrate chain. Its binding to chitooligosaccharides is characterized by negative cooperativity in the interactions of the two domains. Apparently, the flexibility of the long linker that connects the LysM and MSL domains plays a facilitating role in this recognition. The LysM domain in the MSL-LysM molecule, like other bacterial domains but unlike plant LysM domains, recognizes equally well peptidoglycan fragments as well as chitin polymers. Interestingly, in the case presented here, two LysM domains are enough for binding to peptidoglycan in contrast to the three reportedly required by the LysM domains of Bacillus subtilis and Lactococcus lactis. Also, the affinity of the MSL-LysM molecule for chitooligosaccharides is higher than that of LysM-chitooligosaccharide interactions reported so far.
    Mesh-Begriff(e) Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Carbohydrate Sequence ; Chitin/analogs & derivatives ; Chitin/chemistry ; Chitin/metabolism ; Lectins/chemistry ; Lectins/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mycobacterium smegmatis/chemistry ; Mycobacterium smegmatis/metabolism ; Protein Binding ; Protein Structure, Tertiary ; Sequence Alignment
    Chemische Substanzen Bacterial Proteins ; Lectins ; oligochitosan ; Chitin (1398-61-4)
    Sprache Englisch
    Erscheinungsdatum 2016-01-12
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.5b00841
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 217: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  3. Artikel: SARS-CoV-2 viral budding and entry can be modeled using virus-like particles.

    Plescia, Caroline B / David, Emily A / Patra, Dhabaleswar / Sengupta, Ranjan / Amiar, Souad / Su, Yuan / Stahelin, Robert V

    bioRxiv : the preprint server for biology

    2020  

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China and expeditiously spread across the globe causing a global pandemic. While a select agent designation has not been made for SARS-CoV-2, ... ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China and expeditiously spread across the globe causing a global pandemic. While a select agent designation has not been made for SARS-CoV-2, closely related SARS-CoV-1 and MERS coronaviruses are classified as Risk Group 3 select agents, which restricts use of the live viruses to BSL-3 facilities. Such BSL-3 classification make SARS-CoV-2 research inaccessible to the majority of functioning research laboratories in the US; this becomes problematic when the collective scientific effort needs to be focused on such in the face of a pandemic. In this work, we assessed the four structural proteins from SARS-CoV-2 for their ability to form viruslike particles (VLPs) from human cells to form a competent system for BSL-2 studies of SARS-CoV-2. Herein, we provide methods and resources of producing, purifying, fluorescently and APEX2-labeling of SARS-CoV-2 VLPs for the evaluation of mechanisms of viral budding and entry as well as assessment of drug inhibitors under BSL-2 conditions.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-10-01
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2020.09.30.320903
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

  4. Artikel ; Online: SARS-CoV-2 viral budding and entry can be modeled using BSL-2 level virus-like particles.

    Plescia, Caroline B / David, Emily A / Patra, Dhabaleswar / Sengupta, Ranjan / Amiar, Souad / Su, Yuan / Stahelin, Robert V

    The Journal of biological chemistry

    2020  Band 296, Seite(n) 100103

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China, and expeditiously spread across the globe causing a global pandemic. Research on SARS-CoV-2, as well as the closely related SARS-CoV-1 and ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China, and expeditiously spread across the globe causing a global pandemic. Research on SARS-CoV-2, as well as the closely related SARS-CoV-1 and MERS coronaviruses, is restricted to BSL-3 facilities. Such BSL-3 classification makes SARS-CoV-2 research inaccessible to the majority of functioning research laboratories in the United States; this becomes problematic when the collective scientific effort needs to be focused on such in the face of a pandemic. However, a minimal system capable of recapitulating different steps of the viral life cycle without using the virus' genetic material could increase accessibility. In this work, we assessed the four structural proteins from SARS-CoV-2 for their ability to form virus-like particles (VLPs) from human cells to form a competent system for BSL-2 studies of SARS-CoV-2. Herein, we provide methods and resources of producing, purifying, fluorescently and APEX2-labeling of SARS-CoV-2 VLPs for the evaluation of mechanisms of viral budding and entry as well as assessment of drug inhibitors under BSL-2 conditions. These systems should be useful to those looking to circumvent BSL-3 work with SARS-CoV-2 yet study the mechanisms by which SARS-CoV-2 enters and exits human cells.
    Mesh-Begriff(e) Biomimetic Materials/chemistry ; Biomimetic Materials/metabolism ; Containment of Biohazards/classification ; Coronavirus Envelope Proteins/genetics ; Coronavirus Envelope Proteins/metabolism ; Gene Expression ; Genes, Reporter ; Government Regulation ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Humans ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Microscopy, Electron ; Nucleocapsid Proteins/genetics ; Nucleocapsid Proteins/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; SARS-CoV-2/genetics ; SARS-CoV-2/growth & development ; SARS-CoV-2/metabolism ; SARS-CoV-2/ultrastructure ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/metabolism ; Virion/genetics ; Virion/growth & development ; Virion/metabolism ; Virion/ultrastructure ; Virus Assembly/physiology ; Virus Internalization ; Virus Release/physiology ; Red Fluorescent Protein
    Chemische Substanzen Coronavirus Envelope Proteins ; Luminescent Proteins ; Nucleocapsid Proteins ; Recombinant Proteins ; Spike Glycoprotein, Coronavirus ; Viral Matrix Proteins ; envelope protein, SARS-CoV-2 ; membrane protein, SARS-CoV-2 ; spike protein, SARS-CoV-2 ; Green Fluorescent Proteins (147336-22-9)
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-11-27
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA120.016148
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Uc I Zs.108: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  5. Artikel ; Online: Structure, interactions and evolutionary implications of a domain-swapped lectin dimer from Mycobacterium smegmatis.

    Patra, Dhabaleswar / Mishra, Padmanabh / Surolia, Avadhesha / Vijayan, Mamannamana

    Glycobiology

    2014  Band 24, Heft 10, Seite(n) 956–965

    Abstract: Crystal structure determination of the lectin domain of MSMEG_3662 from Mycobacterium smegmatis and its complexes with mannose and methyl-α-mannose, the first effort of its kind on a mycobacterial lectin, reveals a structure very similar to β-prism II ... ...

    Abstract Crystal structure determination of the lectin domain of MSMEG_3662 from Mycobacterium smegmatis and its complexes with mannose and methyl-α-mannose, the first effort of its kind on a mycobacterial lectin, reveals a structure very similar to β-prism II fold lectins from plant sources, but with extensive unprecedented domain swapping in dimer formation. The two subunits in a dimer often show small differences in structure, but the two domains, not always related by 2-fold symmetry, have the same structure. Each domain carries three sugar-binding sites, similar to those in plant lectins, one on each Greek key motif. The occurrence of β-prism II fold lectins in bacteria, with characteristics similar to those from plants, indicates that this family of lectins is of ancient origin and had evolved into a mature system before bacteria and plants diverged. In plants, the number of binding sites per domain varies between one and three, whereas the number is two in the recently reported lectin domains from Pseudomonas putida and Pseudomonas aeruginosa. An analysis of the sequences of the lectins and the lectin domains shows that the level of sequence similarity among the three Greek keys in each domain has a correlation with the number of binding sites in it. Furthermore, sequence conservation among the lectins from different species is the highest for that Greek key which carries a binding site in all of them. Thus, it would appear that carbohydrate binding influences the course of the evolution of the lectin.
    Mesh-Begriff(e) Binding Sites ; Biological Evolution ; Crystallography, X-Ray ; Lectins/chemistry ; Lectins/genetics ; Mycobacterium smegmatis/chemistry ; Mycobacterium smegmatis/metabolism ; Protein Folding ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid
    Chemische Substanzen Lectins
    Sprache Englisch
    Erscheinungsdatum 2014-10
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1067689-2
    ISSN 1460-2423 ; 0959-6658
    ISSN (online) 1460-2423
    ISSN 0959-6658
    DOI 10.1093/glycob/cwu059
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 3150: Hefte anzeigen Standort:
    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)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  6. Artikel ; Online: Structures of rhodopsin in complex with G-protein-coupled receptor kinase 1.

    Chen, Qiuyan / Plasencia, Manolo / Li, Zhuang / Mukherjee, Somnath / Patra, Dhabaleswar / Chen, Chun-Liang / Klose, Thomas / Yao, Xin-Qiu / Kossiakoff, Anthony A / Chang, Leifu / Andrews, Philip C / Tesmer, John J G

    Nature

    2021  Band 595, Heft 7868, Seite(n) 600–605

    Abstract: G-protein-coupled receptor (GPCR) kinases (GRKs) selectively phosphorylate activated GPCRs, thereby priming them for ... ...

    Abstract G-protein-coupled receptor (GPCR) kinases (GRKs) selectively phosphorylate activated GPCRs, thereby priming them for desensitization
    Mesh-Begriff(e) Amino Acid Sequence ; Animals ; Binding Sites ; Cattle ; Cryoelectron Microscopy ; G-Protein-Coupled Receptor Kinase 1/chemistry ; Protein Structure, Tertiary ; Rhodopsin/chemistry ; Signal Transduction
    Chemische Substanzen Rhodopsin (9009-81-8) ; G-Protein-Coupled Receptor Kinase 1 (EC 2.7.11.14)
    Sprache Englisch
    Erscheinungsdatum 2021-07-14
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-021-03721-x
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 26: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 9: Hefte anzeigen
    Zs.MO 244: Hefte anzeigen

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  7. Artikel ; Online: Bovine serum albumin interacts with silver nanoparticles with a "side-on" or "end on" conformation.

    Dasgupta, Nandita / Ranjan, Shivendu / Patra, Dhabaleswar / Srivastava, Priyanka / Kumar, Ashutosh / Ramalingam, Chidambaram

    Chemico-biological interactions

    2016  Band 253, Seite(n) 100–111

    Abstract: As the nanoparticles (NPs) enter into the biological interface, they have to encounter immediate and first exposure to many proteins of different concentrations. The physicochemical interaction of NPs and proteins is greatly influenced not only by the ... ...

    Abstract As the nanoparticles (NPs) enter into the biological interface, they have to encounter immediate and first exposure to many proteins of different concentrations. The physicochemical interaction of NPs and proteins is greatly influenced not only by the number and type of proteins; but also the surface chemistry of NPs. To analyze the effects of NPs on proteins, the interaction between bovine serum albumin (BSA) and silver nanoparticles (AgNPs) at different concentrations were investigated. The interaction, BSA conformations, kinetics and adsorption were analyzed by UV-Visible spectrophotometer, dynamic light scattering (DLS), FT-IR spectroscopy and fluorescence quenching. DLS, FTIR and UV-visible spectrophotometric analysis confirms the interaction with minor alterations in size of the protein. Fluorescence quenching analysis confirms the side-on or end-on interaction of 1.5 molecules of BSA to AgNP. Further, pseudo-second order kinetics was determined with equilibrium contact-time of 30 min. The data of the present study determines the detailed evaluation of BSA adsorption on AgNP along with mechanism, kinetics and isotherm of the adsorption.
    Mesh-Begriff(e) Animals ; Cattle ; Circular Dichroism ; Dynamic Light Scattering ; Kinetics ; Metal Nanoparticles/chemistry ; Protein Binding ; Protein Structure, Tertiary ; Serum Albumin, Bovine/chemistry ; Serum Albumin, Bovine/metabolism ; Silver/chemistry ; Spectrophotometry, Ultraviolet ; Spectroscopy, Fourier Transform Infrared
    Chemische Substanzen Serum Albumin, Bovine (27432CM55Q) ; Silver (3M4G523W1G)
    Sprache Englisch
    Erscheinungsdatum 2016-06-25
    Erscheinungsland Ireland
    Dokumenttyp Journal Article
    ZDB-ID 218799-1
    ISSN 1872-7786 ; 0009-2797
    ISSN (online) 1872-7786
    ISSN 0009-2797
    DOI 10.1016/j.cbi.2016.05.018
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Volltext online

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Zs.A 686: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  8. Artikel ; Online: SARS-CoV-2 viral budding and entry can be modeled using virus-like particles

    Plescia, Caroline B. / David, Emily A. / Patra, Dhabaleswar / Sengupta, Ranjan / Amiar, Souad / Su, Yuan / Stahelin, Robert V.

    bioRxiv

    Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China and expeditiously spread across the globe causing a global pandemic. While a select agent designation has not been made for SARS-CoV-2, ... ...

    Abstract Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China and expeditiously spread across the globe causing a global pandemic. While a select agent designation has not been made for SARS-CoV-2, closely related SARS-CoV-1 and MERS coronaviruses are classified as Risk Group 3 select agents, which restricts use of the live viruses to BSL-3 facilities. Such BSL-3 classification make SARS-CoV-2 research inaccessible to the majority of functioning research laboratories in the US; this becomes problematic when the collective scientific effort needs to be focused on such in the face of a pandemic. In this work, we assessed the four structural proteins from SARS-CoV-2 for their ability to form virus-like particles (VLPs) from human cells to form a competent system for BSL-2 studies of SARS-CoV-2. Herein, we provide methods and resources of producing, purifying, fluorescently and APEX2-labeling of SARS-CoV-2 VLPs for the evaluation of mechanisms of viral budding and entry as well as assessment of drug inhibitors under BSL-2 conditions.
    Schlagwörter covid19
    Sprache Englisch
    Erscheinungsdatum 2020-10-01
    Verlag Cold Spring Harbor Laboratory
    Dokumenttyp Artikel ; Online
    DOI 10.1101/2020.09.30.320903
    Datenquelle COVID19

    Volltext online

    Kategorien

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

  9. Artikel ; Online: Structural analysis of lecithin:cholesterol acyltransferase bound to high density lipoprotein particles.

    Manthei, Kelly A / Patra, Dhabaleswar / Wilson, Christopher J / Fawaz, Maria V / Piersimoni, Lolita / Shenkar, Jenny Capua / Yuan, Wenmin / Andrews, Philip C / Engen, John R / Schwendeman, Anna / Ohi, Melanie D / Tesmer, John J G

    Communications biology

    2020  Band 3, Heft 1, Seite(n) 28

    Abstract: Lecithin:cholesterol acyltransferase (LCAT) catalyzes a critical step of reverse cholesterol transport by esterifying cholesterol in high density lipoprotein (HDL) particles. LCAT is activated by apolipoprotein A-I (ApoA-I), which forms a double belt ... ...

    Abstract Lecithin:cholesterol acyltransferase (LCAT) catalyzes a critical step of reverse cholesterol transport by esterifying cholesterol in high density lipoprotein (HDL) particles. LCAT is activated by apolipoprotein A-I (ApoA-I), which forms a double belt around HDL, however the manner in which LCAT engages its lipidic substrates and ApoA-I in HDL is poorly understood. Here, we used negative stain electron microscopy, crosslinking, and hydrogen-deuterium exchange studies to refine the molecular details of the LCAT-HDL complex. Our data are consistent with LCAT preferentially binding to the edge of discoidal HDL near the boundary between helix 5 and 6 of ApoA-I in a manner that creates a path from the lipid bilayer to the active site of LCAT. Our results provide not only an explanation why LCAT activity diminishes as HDL particles mature, but also direct support for the anti-parallel double belt model of HDL, with LCAT binding preferentially to the helix 4/6 region.
    Mesh-Begriff(e) Binding Sites ; Catalytic Domain ; Lipoproteins, HDL/chemistry ; Lysine/chemistry ; Lysine/metabolism ; Mass Spectrometry ; Models, Molecular ; Multiprotein Complexes/chemistry ; Multiprotein Complexes/metabolism ; Multiprotein Complexes/ultrastructure ; Phosphatidylcholine-Sterol O-Acyltransferase/chemistry ; Phosphatidylcholine-Sterol O-Acyltransferase/metabolism ; Protein Binding ; Protein Conformation ; Recombinant Proteins ; Structure-Activity Relationship
    Chemische Substanzen Lipoproteins, HDL ; Multiprotein Complexes ; Recombinant Proteins ; Phosphatidylcholine-Sterol O-Acyltransferase (EC 2.3.1.43) ; Lysine (K3Z4F929H6)
    Sprache Englisch
    Erscheinungsdatum 2020-01-15
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 2399-3642
    ISSN (online) 2399-3642
    DOI 10.1038/s42003-019-0749-z
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

  10. Artikel ; Online: Cloning, expression, purification, crystallization and preliminary X-ray studies of the mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis.

    Patra, Dhabaleswar / Sharma, Alok / Chandran, Divya / Vijayan, Mamannamana

    Acta crystallographica. Section F, Structural biology and crystallization communications

    2011  Band 67, Heft Pt 5, Seite(n) 596–599

    Abstract: The mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis has been cloned, expressed, purified and crystallized and the crystals have been characterized using X-ray diffraction. The Matthews coefficient suggests the possibility of two ... ...

    Abstract The mannose-binding lectin domain of MSMEG_3662 from Mycobacterium smegmatis has been cloned, expressed, purified and crystallized and the crystals have been characterized using X-ray diffraction. The Matthews coefficient suggests the possibility of two lectin domains in the triclinic cell. The amino-acid sequence of the domain indicates structural similarity to well characterized β-prism II fold lectins.
    Mesh-Begriff(e) Binding Sites ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; Mannose-Binding Lectin/chemistry ; Mannose-Binding Lectin/genetics ; Mannose-Binding Lectin/isolation & purification ; Mycobacterium smegmatis/chemistry
    Chemische Substanzen Mannose-Binding Lectin
    Sprache Englisch
    Erscheinungsdatum 2011-04-28
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1744-3091
    ISSN (online) 1744-3091
    DOI 10.1107/S1744309111009547
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

Zum Seitenanfang