Zobrazeno 1 - 10
of 61
pro vyhledávání: '"Jonas S, Johansson"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1824:1409-1415
A monomeric four-α-helix bundle protein Aα 4 was designed as a step towards investigating the interaction of volatile general anesthetics with their putative membrane protein targets. The alpha helices, connected by glycine loops, have the sequence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b795ab2a429a3f80cc4262ae44046b1
https://doi.org/10.1016/j.bbapap.2012.06.007
https://doi.org/10.1016/j.bbapap.2012.06.007
Publikováno v:
Biophysical Journal. 96:4176-4187
We demonstrate that cyano-phenylalanine (Phe(CN)) can be utilized to probe the binding of the inhalational anesthetic halothane to an anesthetic-binding, model ion channel protein hbAP-Phe(CN). The Trp to Phe(CN) mutation alters neither the alpha-hel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::288a81c4a16210893f387adace1fbafa
https://doi.org/10.1016/j.bpj.2009.01.055
https://doi.org/10.1016/j.bpj.2009.01.055
Publikováno v:
Journal of Clinical Anesthesia. 19:218-221
This case series details successful management of life-threatening airway obstruction after carotid endarterectomy. In the first case, ventilation was restored with a Laryngeal Mask Airway. In the second case, laryngeal mask airway rescue was unsucce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5149151caa52a73e6491ffcca5b1a8bc
https://doi.org/10.1016/j.jclinane.2006.06.008
https://doi.org/10.1016/j.jclinane.2006.06.008
Autor:
Ravindernath Pidikiti, Konda S. Reddy, Jonas S. Johansson, Krishna M. G. Mallela, Tao Zhang, Mohammad Shamim
Publikováno v:
International Congress Series. 1283:155-159
A molecular understanding of volatile general anesthetic mechanisms of action will ultimately require high-resolution structural descriptions of anesthetic–protein complexes. Structural changes in proteins following anesthetic binding have been tec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01aaf7991e20d0538251394643cda138
https://doi.org/10.1016/j.ics.2005.06.099
https://doi.org/10.1016/j.ics.2005.06.099
Publikováno v:
International Congress Series. 1283:15-20
A convergence of evidence suggests the core of 4-α-helix bundles is an important structural motif of volatile anesthetic targets. However, structural detail of such sites in natural proteins remains elusive. We screened over 80 soluble proteins for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e45989d391fede0ca2b527390aebfc19
https://doi.org/10.1016/j.ics.2005.06.079
https://doi.org/10.1016/j.ics.2005.06.079
Autor:
Tao Zhang, Jonas S. Johansson
Publikováno v:
International Congress Series. 1283:219-222
Isothermal titration calorimetry has been used to characterize the binding of 10 volatile general anesthetics to the hydrophobic core of a four-α-helix bundle protein. This relatively small protein (124 residues) is able to bind a total of 10 volati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e977e2f016f54c677c9e4675891eb16c
https://doi.org/10.1016/j.ics.2005.07.050
https://doi.org/10.1016/j.ics.2005.07.050
Autor:
Ravindernath Pidikiti, Mohammad Shamim, Krishna M. G. Mallela, Konda S. Reddy, Jonas S. Johansson
Publikováno v:
Biomacromolecules. 6:1516-1523
The structural features of volatile anesthetic binding sites on proteins are being investigated with the use of a defined model system consisting of a four-R-helix bundle scaffold with a hydrophobic core. The current study describes the bacterial exp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7334b50146e9f6c670c134820744b25e
https://doi.org/10.1021/bm049226a
https://doi.org/10.1021/bm049226a
Binding of the volatile general anesthetics halothane and isoflurane to a mammalian β-barrel protein
Publikováno v:
FEBS Journal. 272:573-581
A molecular understanding of volatile anesthetic mechanisms of action will require structural descriptions of anesthetic-protein complexes. Porcine odorant binding protein is a 157 residue member of the lipocalin family that features a large beta-bar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ce9b913b32166344ebaef094ab233305
https://doi.org/10.1111/j.1742-4658.2004.04500.x
https://doi.org/10.1111/j.1742-4658.2004.04500.x
Autor:
Wenlin Wei, Baobin Kang, Ravindernath Pidikiti, Maryellen F. Eckenhoff, Jonas S. Johansson, Anna Carnini, Huafeng Wei, Roderic G. Eckenhoff, Jason M. Keller
Publikováno v:
Anesthesiology. 101:703-709
Background The majority of surgical patients receive inhaled anesthetics, principally small haloalkanes and haloethers. Long-term cognitive problems occur in the elderly subsequent to anesthesia and surgery, and previous surgery might also be a risk
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff809c0f9992bfa6b9209b206eb01a3a
https://doi.org/10.1097/00000542-200409000-00019
https://doi.org/10.1097/00000542-200409000-00019
Autor:
Gavin A. Manderson, Jonas S. Johansson
Publikováno v:
Biopolymers. 75:338-354
The general anesthetics halothane and chloroform are capable of binding to synthetic water-soluble four-alpha-helix bundles, which model the putative in vivo receptors. In this study, we investigate the binding of these anesthetics to synthetic water
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f8d7bf0d9a86d4cd62f77002692eedd
https://doi.org/10.1002/bip.20138
https://doi.org/10.1002/bip.20138