Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Paul M. M. Weers"'
Publikováno v:
Molecular and Cellular Biochemistry. 478:173-183
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3723897a3f7770e98320750caa74c89
https://doi.org/10.1007/s11010-022-04497-y
https://doi.org/10.1007/s11010-022-04497-y
Publikováno v:
BBA advances. 1
Apolipophorin III (apoLp-III) from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::74b8aee3cbf1f54fa6dc798f0cbbb9fb
https://pubmed.ncbi.nlm.nih.gov/36267477
https://pubmed.ncbi.nlm.nih.gov/36267477
Autor:
Mark T Lek, Siobanth Cruz, Nnejiuwa U Ibe, Wendy H J Beck, John K Bielicki, Paul M M Weers, Vasanthy Narayanaswami
Publikováno v:
PLoS ONE, Vol 12, Iss 6, p e0178346 (2017)
Apolipoprotein (apo) E3 and apoAI are exchangeable apolipoproteins that play a dominant role in regulating plasma lipoprotein metabolism. ApoE3 (299 residues) is composed of an N-terminal (NT) domain bearing a 4-helix bundle and a C-terminal (CT) dom
Externí odkaz:
https://doaj.org/article/13ed6acafcff45beb0d1ed062e7adf06
Publikováno v:
Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology. 44(1)
The laboratory protocol presented here takes about 3 hours to perform and investigates protein and lipid interactions. Students first purify His6 -tagged human apolipoprotein A-I (apoA-I) with Ni-NTA affinity resin in a simple batch protocol and prep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::60c002a83153cb76574a8f01fa027be5
https://pubmed.ncbi.nlm.nih.gov/26560199
https://pubmed.ncbi.nlm.nih.gov/26560199
Publikováno v:
Journal of Lipid Research, Vol 41, Iss 3, Pp 416-423 (2000)
Apolipophorin III (apoLp-III) from Locusta mi- gratoria is an exchangeable apolipoprotein that binds re- versibly to lipoprotein surfaces. The native protein is glyco- sylated at Asn-18 and Asn-85. Variable attachment of five distinct oligosaccharide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ea16853fe3d07a58b056166eec8321d
https://doi.org/10.1016/s0022-2275(20)34480-1
https://doi.org/10.1016/s0022-2275(20)34480-1
Autor:
Kim Oikawa, Hideaki Maekawa, Vasanthy Narayanaswami, Robert O. Ryan, Ryoichi Sato, Yoshio Yamauchi, Kozo Tsuchida, Cyril M. Kay, Paul M. M. Weers
Publikováno v:
European Journal of Biochemistry. 267:728-736
Apolipophorin III (apoLp-III) from the silkmoth, Bombyx mori, has been over-expressed in Escherichia coli, purified and characterized. Far-UV CD spectroscopic analysis revealed 65% alpha-helix secondary structure. Near-UV CD spectra obtained in buffe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a0d80819f0ca4191d601efccbde05193
https://doi.org/10.1046/j.1432-1327.2000.01050.x
https://doi.org/10.1046/j.1432-1327.2000.01050.x
Autor:
Vasanthy Narayanaswami, F. P. Kooiman, Cyril M. Kay, D. J. Van Der Horst, Robert O. Ryan, Douglas G. Scraba, Jan Bogerd, Paul M. M. Weers
Publikováno v:
Biochemistry. 34:11822-11830
The structural basis for the lipid binding capability of Locusta migratoria apolipophorin III (apoLp-III) was assessed by characterizing the amino and carboxyl terminal halves of the protein. The native molecule (approximately 20 kDa) was deglycosyla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c08ddc9aedbc38d8d113d8da3eb860c
https://doi.org/10.1021/bi00037a021
https://doi.org/10.1021/bi00037a021
Publikováno v:
Biochemistry. 33:3617-3624
Apolipophorin I11 (apoLp-111) from the migratory locust, Locusta migratoria, represents the only full-length apolipoprotein whose three-dimensional structure has been solved. In the present study, spectroscopic methods have been employed to investiga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::283bb15edd09665aedb4fe1e35a3962f
https://doi.org/10.1021/bi00178a019
https://doi.org/10.1021/bi00178a019
Publikováno v:
Biochemistry. 39(23)
The effect of lipid association on the local environment of the two tryptophan residues of Locusta migratoria apolipophorin III (apoLp-III) has been studied. In the lipid-free state, Trp115 in helix 4 is buried in the hydrophobic interior of the heli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd52b979f1cf3ea6e7308aca793ee6c8
https://pubmed.ncbi.nlm.nih.gov/10841768
https://pubmed.ncbi.nlm.nih.gov/10841768
Autor:
Jianjun Wang, Paul M. M. Weers, Brian D. Sykes, Dick J. Van der Horst, Cyril M. Kay, Robert O. Ryan
Publikováno v:
Biochimica et biophysica acta. 1393(1)
Apolipophorin III (apoLp-III) from the locust Locusta migratoria is an exchangeable apolipoprotein that reversibly binds to lipoproteins. During lipid binding the protein has been proposed to undergo a major conformational change. To study the mechan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9df92564c9c2aaca41ee2cd66c804d77
https://pubmed.ncbi.nlm.nih.gov/9714761
https://pubmed.ncbi.nlm.nih.gov/9714761