Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Yuen Han Lam"'
Autor:
Yuen Han Lam, Paul R. Gooley, Chi L.L. Pham, Andrew Hung, Neil H. Thomson, Nevena Todorova, Sheena E. Radford, Chai Lean Teoh, Andreas Engel, Trevor A. Smith, Emma E. Lees, Irene Yarovsky, C. Lincoln, Geoffrey J. Howlett, Michael D. W. Griffin, Katrina J. Binger, Shirley A. Müller
Publikováno v:
Journal of Molecular Biology. 405:1246-1266
The self-assembly of specific proteins to form insoluble amyloid fibrils is a characteristic feature of a number of age-related and debilitating diseases. Lipid-free human apolipoprotein C-II (apoC-II) forms characteristic amyloid fibrils and is one
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c55b0fd2e4885bcbd34f150bfca1d2ef
https://doi.org/10.1016/j.jmb.2010.12.006
https://doi.org/10.1016/j.jmb.2010.12.006
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 78:858-872
The interaction with model membranes of a peptide, EqtII(1-32), corresponding to the N-terminal region of the pore-forming toxin equinatoxin II (EqtII) has been studied using solid-state NMR and molecular dynamics (MD) simulations. The distances betw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d86a8f484743fca096e00fb70dcfa53e
https://doi.org/10.1002/prot.22612
https://doi.org/10.1002/prot.22612
Publikováno v:
European Biophysics Journal. 31:383-388
Melittin is a cytolytic peptide whose biological activity is lost upon binding to a six-residue peptide, Ac-IVIFDC-NH(2), with which it forms a highly insoluble complex. As a result, the structural analysis of the interaction between the two peptides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d04a43fa1a3b5ffeb9b1c82c5ebe0e5b
https://doi.org/10.1007/s00249-002-0229-z
https://doi.org/10.1007/s00249-002-0229-z
Publikováno v:
Journal of Pharmaceutical Sciences. 91:943-951
The molecular mobility of protein in lyophilized lysozyme-sugar systems stored at different relative humidities was studied using solid-state NMR. Relaxation measurements, T(1) of high-frequency (MHz), and T(1rho), of low-frequency (kHz) motions, wer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ef947d1482bab3d85e9ea00ce55da71
https://doi.org/10.1002/jps.10089
https://doi.org/10.1002/jps.10089
Autor:
Penelope Woodberry, Bernard F. Hoskins, Frances Separovic, Brendan F. Abrahams, Richard Robson, Yuen-Han Lam
Publikováno v:
Journal of Solid State Chemistry. 156:51-56
The low-temperature crystal structure of Cd(CN) 2 ·2/3H 2 O· t -BuOH (230 K) is reported, Pbcm , a =8.694(1), b =16.908(4), c =21.157(3) A. Although the cell has approximately twice the volume of the previously reported room temperature cell the 3D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::243d785479994729ed3befbce9892339
https://doi.org/10.1006/jssc.2000.8957
https://doi.org/10.1006/jssc.2000.8957
Publikováno v:
Journal of Protein Chemistry. 19:529-534
The conformation of a melittin-inhibitor complex was studied by solution NMR, solid-state NMR, and circular dichroism. In solution, binding was studied by titrating inhibitor against melittin in dimethyl sulfoxide, methanol, aqueous buffer, and dodec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2af7814b89282dbbb109eee44bd55548
https://doi.org/10.1023/a:1026561701338
https://doi.org/10.1023/a:1026561701338
Publikováno v:
Letters in Peptide Science. 7:151-156
Amphibian skin is a rich source of peptides that are specific to pathogens and act by disrupting bacterial membranes. Three antimicrobial peptides were isolated from the skin glands of Australian tree frogs,Litoria caerulea andLitoria genimaculata. N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c2466413b85a233be63827b7ed7944c
https://doi.org/10.1007/bf02443582
https://doi.org/10.1007/bf02443582
Autor:
Andrew Routh, Yuen Han Lam, Wolfgang B. Fischer, Peter J. Judge, D. Fischer, T. Mehnert, Anthony Watts
Publikováno v:
Proteins
Vpu from HIV‐1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61a3114269d440f8cb71b204f1eb3332
http://ora.ox.ac.uk/objects/uuid:64856273-36eb-436f-a741-e8f346d9842b
http://ora.ox.ac.uk/objects/uuid:64856273-36eb-436f-a741-e8f346d9842b
Publikováno v:
Viral Membrane Proteins: Structure, Function, and Drug Design ISBN: 9780306484957
The replication of HIV-1 is strongly enhanced by a small membrane protein called virus protein U (Vpu). Vpu achieves its task by (a) interacting with CD4, the HIV-1 receptor, and (b) by amplifying particle release at the site of the plasma membrane.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bbe3bd1e2746c4be8ad35c4a73fd96c0
https://doi.org/10.1007/0-387-28146-0_14
https://doi.org/10.1007/0-387-28146-0_14
