| human alpha-lactalbumin and human lactoferrin complexes appeared to interact with the chromatin of isolated nuclei affecting chromatin structural organization | Effect of alpha-lactalbumin and lactoferrin oleic acid complexes on chromatin structural organization.
Lebedev DV, Zabrodskaya YA, Pipich V, Kuklin AI, Ramsay E, Sokolov AV, Elizarova AY, Shaldzhyan AA, Grudinina NA, Pantina RA, Wu B, Shtam TA, Volnitskiy AV, Schmidt AE, Shvetsov AV, Vasilyev VB, Isaev-Ivanov VV, Egorov VV. | 06/27/2020 |
| Studies indicate that alpha-lactalbumin has two domains, a large alpha-helical domain and a small beta-sheet domain connected by a calcium binding loop. | Disorder in Milk Proteins: α-Lactalbumin. Part C. Peculiarities of Metal Binding.
Permyakov EA, Permyakov SE, Breydo L, Redwan EM, Almehdar HA, Uversky VN. | 02/18/2017 |
| High molecular mass complexes are formed with alpha-lactalbumin and alphaB-crystallin, preventing the amorphous aggregation of alpha-lactalbumin. | The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin.
Kulig M, Ecroyd H. | 01/26/2013 |
| analysis of macromolecular crowding on the structural stability of human alpha-lactalbumin | Effects of macromolecular crowding on the structural stability of human α-lactalbumin.
Zhang DL, Wu LJ, Chen J, Liang Y. | 11/17/2012 |
| Data show that alpha-lactalbumin and CD14 form a complex in the gut which alters degradation of CD14, suggesting a mechanism by which this key LPS receptor may remain functional in the neonatal gut. | Alpha-lactalbumin in human milk alters the proteolytic degradation of soluble CD14 by forming a complex.
Spencer WJ, Binette A, Ward TL, Davis LD, Blais DR, Harrold J, Mack DR, Altosaar I. | 11/26/2011 |
| Observational study of gene-disease association. (HuGE Navigator) | Investigation of genetic susceptibility factors for human longevity - a targeted nonsynonymous SNP study.
Flachsbart F, Franke A, Kleindorp R, Caliebe A, Blanché H, Schreiber S, Nebel A. | 12/5/2010 |
| The complexes formed by partially folded alpha-lactalbumin with oleic acid display selective apoptotic activity against tumor cells. | The oleic acid complexes of proteolytic fragments of alpha-lactalbumin display apoptotic activity.
Tolin S, De Franceschi G, Spolaore B, Frare E, Canton M, Polverino de Laureto P, Fontana A. | 02/8/2010 |
| the structural preferences of the alpha-LA molten globule at pH 7 at the level of individual residues were investigated. | The human alpha-lactalbumin molten globule: comparison of structural preferences at pH 2 and pH 7.
Rösner HI, Redfield C., Free PMC Article | 01/21/2010 |
| recombinant human alpha-LA was purified from transgenic milk and displayed physicochemical properties similar to its natural counterpart with respect to molecular weight, structure, and regulatory activity for beta-1,4-galactosyltransferase | Expression and characterization of bioactive recombinant human alpha-lactalbumin in the milk of transgenic cloned cows.
Wang J, Yang P, Tang B, Sun X, Zhang R, Guo C, Gong G, Liu Y, Li R, Zhang L, Dai Y, Li N. | 01/21/2010 |
| alpha-lactalbumin molten globule has even more native-like character than suggested by studies conducted at higher temperature | Probing the effect of temperature on the backbone dynamics of the human alpha-lactalbumin molten globule.
Ramboarina S, Redfield C. | 01/21/2010 |
| pH-dependent stability of the alpha-lactalbumin molten globule state. | pH-dependent stability of the human alpha-lactalbumin molten globule state: contrasting roles of the 6 - 120 disulfide and the beta-subdomain at low and neutral pH.
Horng JC, Demarest SJ, Raleigh DP. | 01/21/2010 |
| The electrostatic nature of the alpha-lactalbumin (LA)-histone interaction justifies use of alpha-LA as a basis for design of antitumor agents, acting through disorganization of chromatin structure due to interaction between alpha-LA and histone. | No need to be HAMLET or BAMLET to interact with histones: binding of monomeric alpha-lactalbumin to histones and basic poly-amino acids.
Permyakov SE, Pershikova IV, Khokhlova TI, Uversky VN, Permyakov EA. | 01/21/2010 |
| Results describe the reaction mechanism and formation of CIDNP (chemically induced dynamic nuclear polarization) in the photoreactions of the dye 2,2'-dipyridyl with non-native states of bovine and human alpha-lactalbumins in aqueous solution. | Time-resolved CIDNP study of non-native states of bovine and human alpha-lactalbumins.
Morozova OB, Hore PJ, Bychkova VE, Sagdeev RZ, Yurkovskaya AV. | 01/21/2010 |
| the non-cooperative denaturation of the molten globule, alpha-lactalbumin secondary structure elements are stabilized by non-specific, non-native interactions | Characterization of the denaturation of human alpha-lactalbumin in urea by molecular dynamics simulations.
Smith LJ, Jones RM, van Gunsteren WF. | 01/21/2010 |
| comparison of the structural and stability properties of the isolated alpha-helical domain of lysozyme with that of alpha-lactalbumin | Cooperative folding of the isolated alpha-helical domain of hen egg-white lysozyme.
Bai P, Peng Z. | 01/21/2010 |
| Fold and topology of alpha-lactalbumin may be formed from degenerate groups of side chains. | Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.
Mok KH, Nagashima T, Day IJ, Hore PJ, Dobson CM., Free PMC Article | 01/21/2010 |
| NMR study of the conformation of HAMLET, the folding variant of human alpha-lactalbumin, complexed to oleic acid. | Conformational analysis of HAMLET, the folding variant of human alpha-lactalbumin associated with apoptosis.
Casbarra A, Birolo L, Infusini G, Dal Piaz F, Svensson M, Pucci P, Svanborg C, Marino G., Free PMC Article | 01/21/2010 |
| Structural characterisation of the human alpha-lactalbumin molten globule at high temperature | Structural characterisation of the human alpha-lactalbumin molten globule at high temperature.
Ramboarina S, Redfield C. | 01/21/2010 |
| lipids are tissue-specific cofactors in alpha-lactalbumin protein folding | Lipids as cofactors in protein folding: stereo-specific lipid-protein interactions are required to form HAMLET (human alpha-lactalbumin made lethal to tumor cells).
Svensson M, Mossberg AK, Pettersson J, Linse S, Svanborg C., Free PMC Article | 01/21/2010 |
| a functional Ca(2+)-binding site is not required for conversion of alpha-lactalbumin to the active complex or to cause cell death | Alpha-lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human alpha-lactalbumin made lethal to tumor cells).
Svensson M, Fast J, Mossberg AK, Düringer C, Gustafsson L, Hallgren O, Brooks CL, Berliner L, Linse S, Svanborg C., Free PMC Article | 01/21/2010 |
| Local interactions as well as hydrophobic interactions formed in the molten globule state play an important role in organizing the structure in the transition state and in guiding the subsequent folding of alpha-lactalbumin. | Effects of the stabilization of the molten globule state on the folding mechanism of alpha-lactalbumin: a study of a chimera of bovine and human alpha-lactalbumin.
Mizuguchi M, Matsuura A, Nabeshima Y, Masaki K, Watanabe M, Aizawa T, Demura M, Nitta K, Mori Y, Shinoda H, Kawano K. | 01/21/2010 |
| a folding variant of alpha-lactalbumin has a role in lactating mammary gland apoptosis | Apoptotic cell death in the lactating mammary gland is enhanced by a folding variant of alpha-lactalbumin.
Baltzer A, Svanborg C, Jaggi R., Free PMC Article | 01/21/2010 |
| hydrogen exchange behavior of variants using mass spectrometry | Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry.
Last AM, Schulman BA, Robinson CV, Redfield C. | 10/3/2001 |