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Results 1-6 of 6 (Search time: 0.002 seconds).
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Issue Date
Title
Author(s)
2001
The molecular chaperone, α-crystallin, inhibits amyloid formation by apolipoprotein C-II
Hatters, D.
;
Lindner, R.
;
Carver, J.
;
Howlett, G.
2000
Caerin 4.1, an antibiotic peptide from the Australian Tree Frog, Litoria caerulea. The N.M.R.-derived solution structure
Chia, C.
;
Carver, J.
;
Lindner, R.
;
Bowie, J.
;
Wong, H.
;
Lie, W.
2000
Mouse Hsp25, a small heat-shock protein. The role of its C-terminal extension in oligomerization and chaperone action
Lindner, R.
;
Carver, J.
;
Ehrnsperger, M.
;
Buchner, J.
;
Esposito, G.
;
Behlke, J.
;
Lutsch, G.
;
Kotlyarov, A.
;
Gaestel, M.
2010
The quaternary organization and dynamics of the molecular chaperone HSP26 are thermally regulated
Benesch, J.
;
Aquilina, J.
;
Baldwin, A.
;
Rekas, A.
;
Stengel, F.
;
Lindner, R.
;
Basha, E.
;
Devlin, G.
;
Horwitz, J.
;
Vierling, E.
;
Carver, J.
;
Robinson, C.
2000
The small heat-shock chaperone protein, -crystallin, does not recognise stable molten globule states of cytosolic proteins
Treweek, T.
;
Lindner, R.
;
Mariani, M.
;
Carver, J.
2005
Casein proteins as molecular chaperones
Morgan, P.
;
Treweek, T.
;
Lindner, R.
;
Price, W.
;
Carver, J.
Discover
Author
2
Treweek, T.
1
Aquilina, J.
1
Baldwin, A.
1
Basha, E.
1
Behlke, J.
1
Benesch, J.
1
Bowie, J.
1
Buchner, J.
1
Chia, C.
1
Devlin, G.
.
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Subject
1
Chaperone protein
1
Chromatography, Gel
1
Glycation
1
Heat-Shock Proteins
1
Light
1
Molten globule state
1
Nuclear Magnetic Resonance, Biomo...
1
Protein Structure, Quaternary
1
Saccharomyces cerevisiae Proteins
1
Scattering, Radiation
.
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Date issued
1
2010
1
2005
1
2001
3
2000