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alpha-Lactalbumin
Known as:
alpha Lactalbumin
, Lysozyme-Like Protein 7
, Lactalbumin alpha
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Alpha-lactalbumin (142 aa, ~16 kDa) is encoded by the human LALBA gene. This protein plays a role in the regulation of lactose synthesis.
National Institutes of Health
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Related topics
Related topics
9 relations
Carbohydrate Metabolism
Genes, Regulator
Homo sapiens
LALBA gene
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Broader (1)
Lactalbumin
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
1998
Highly Cited
1998
A specific hydrophobic core in the alpha-lactalbumin molten globule.
L. Wu
,
P. S. Kim
Journal of Molecular Biology
1998
Corpus ID: 26096822
Molten globules are partially structured protein folding intermediates that adopt a native-like overall backbone topology in the…
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Highly Cited
1994
Highly Cited
1994
Molecular basis of cooperativity in protein folding. V. Thermodynamic and structural conditions for the stabilization of compact denatured states
D. Xie
,
E. Freire
Proteins: Structure, Function, and Bioinformatics
1994
Corpus ID: 21518376
The heat‐denatured state of proteins has been usually assumed to be a fully hydrated random coil. It is now evident that under…
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Highly Cited
1992
Highly Cited
1992
Molecular basis of co-operativity in protein folding. III. Structural identification of cooperative folding units and folding intermediates.
K. Murphy
,
V. Bhakuni
,
D. Xie
,
E. Freire
Journal of Molecular Biology
1992
Corpus ID: 37212128
Highly Cited
1991
Highly Cited
1991
Hydrophobic clustering in nonnative states of a protein: Interpretation of chemical shifts in NMR spectra of denatured states of lysozyme
P. Evans
,
Karen D. Topping
,
D. Woolfson
,
C. Dobson
Proteins: Structure, Function, and Bioinformatics
1991
Corpus ID: 13592410
Chemical shifts of resonances of specific protons in the 1H NMR spectrum of thermally denatured hen lysozyme have been determined…
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Highly Cited
1991
Highly Cited
1991
Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-alpha-lactalbumin.
D. Xie
,
V. Bhakuni
,
E. Freire
Biochemistry
1991
Corpus ID: 26047777
High-sensitivity differential scanning calorimetry has been used to characterize the energetics of the molten globule state of…
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Highly Cited
1990
Highly Cited
1990
Surface shear viscometry as a probe of protein-protein interactions in mixed milk protein films adsorbed at the oil-water interface.
E. Dickinson
,
Susan E. Rolfe
,
D. Dalgleish
International Journal of Biological…
1990
Corpus ID: 10935330
Highly Cited
1986
Highly Cited
1986
Thermal behavior of proteins in high-performance hydrophobic-interaction chromatography. On-line spectroscopic and chromatographic characterization.
Shiaw‐lin Wu
,
K. Benedek
,
Barry L. Karger
Journal of Chromatography A
1986
Corpus ID: 23078988
Highly Cited
1986
Highly Cited
1986
Allergen‐Specific IgE Antibodies against Antigenic Components in Cow Milk and Milk Substitutes
B. Gjesing
,
O. Østerballe
,
B. Schwartz
,
U. Wahn
,
H. Løwenstein
Allergy. European Journal of Allergy and Clinical…
1986
Corpus ID: 45993521
Crossed radioimmunoelectrophoresis (CRIE) was used to study the presence of scrum IgE against antigenic components of Cow milk in…
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Highly Cited
1982
Highly Cited
1982
Metal ion binding to alpha-lactalbumin species.
K. Murakami
,
P. J. Andree
,
L. Berliner
Biochemistry
1982
Corpus ID: 33265756
A strong cation (calcium) binding site has been demonstrated to exist in several alpha-lactalbumin species; bovine, goat, human…
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Highly Cited
1975
Highly Cited
1975
Cross-linking of the components of lactose synthetase with dimethylpimelimidate.
K. Brew
,
J. H. Shaper
,
K. Olsen
,
I. Trayer
,
R. Hill
Journal of Biological Chemistry
1975
Corpus ID: 32443439
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