Conversion of alpha-lactalbumin to a protein inducing apoptosis - Wikidata - awgldk - TriplyDB

Conversion of alpha-lactalbumin to a protein inducing apoptosis

Conversion of alpha-lactalbumin to a protein inducing apoptosis

http://www.wikidata.org/entity/Q24681658

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Sensitization of Staphylococcus aureus to methicillin and other antibiotics in vitro and in vivo in the presence of HAMLET The bovine lactation genome: insights into the evolution of mammalian milk Bioactive Molecules Released in Food by Lactic Acid Bacteria: Encrypted Peptides and Biogenic Amines Protein receptor-independent plasma membrane remodeling by HAMLET: a tumoricidal protein-lipid complex.HAMLET binding to α-actinin facilitates tumor cell detachment Apoptosis-like death in bacteria induced by HAMLET, a human milk lipid-protein complex The human milk protein-lipid complex HAMLET sensitizes bacterial pathogens to traditional antimicrobial agents Changes in proteasome structure and function caused by HAMLET in tumor cells.Structure and stability analysis of cytotoxic complex of camel α-lactalbumin and unsaturated fatty acids produced at high temperature.HAMLET: functional properties and therapeutic potential.Low resolution solution structure of HAMLET and the importance of its alpha-domains in tumoricidal activity.HAMLET interacts with lipid membranes and perturbs their structure and integrity.Coupling Mass Spectrometry-Based "Omic" Sciences with Bioguided Processing to Unravel Milk's Hidden Bioactivities.Conserved features of cancer cells define their sensitivity to HAMLET-induced death; c-Myc and glycolysis Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.Applications of site-specific labeling to study HAMLET, a tumoricidal complex of α-lactalbumin and oleic acid.HAMLET interacts with histones and chromatin in tumor cell nuclei.Label-free liquid chromatography-tandem mass spectrometry analysis with automated phosphopeptide enrichment reveals dynamic human milk protein phosphorylation during lactation Influence of pH on the structure and oleic acid binding ability of bovine α-lactalbumin.Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state.Lactosomes: structural and compositional classification of unique nanometer-sized protein lipid particles of human milk.Mutagens in human breast lipid and milk: the search for environmental agents that initiate breast cancer.A unifying mechanism for cancer cell death through ion channel activation by HAMLET.Can misfolded proteins be beneficial? The HAMLET case.Oleic acid may be the key contributor in the BAMLET-induced erythrocyte hemolysis and tumoricidal action Bacterial programmed cell death: making sense of a paradox.Targeting Human α-Lactalbumin Gene Insertion into the Goat β-Lactoglobulin Locus by TALEN-Mediated Homologous Recombination A novel initiation mechanism of death in Streptococcus pneumoniae induced by the human milk protein-lipid complex HAMLET and activated during physiological death.Bioinspired assembly of small molecules in cell milieu.Detecting cryptic epitopes created by nanoparticles.Lipids as cofactors in protein folding: stereo-specific lipid-protein interactions are required to form HAMLET (human alpha-lactalbumin made lethal to tumor cells).Molecular mechanisms of the cytotoxicity of human α-lactalbumin made lethal to tumor cells (HAMLET) and other protein-oleic acid complexes.Lipids as tumoricidal components of human α-lactalbumin made lethal to tumor cells (HAMLET): unique and shared effects on signaling and death Overexpression of an antimicrobial peptide derived from C. elegans using an aggregation-prone protein coexpression system Protein-dependent Membrane Interaction of A Partially Disordered Protein Complex with Oleic Acid: Implications for Cancer Lipidomics.Cow's milk allergy: from allergens to new forms of diagnosis, therapy and prevention.Structure and function of human α-lactalbumin made lethal to tumor cells (HAMLET)-type complexes.Bioactivity of α-lactalbumin related to its interaction with fatty acids: a review.Alternatively folded proteins with unexpected beneficial functions.Protein-fatty acid complexes: biochemistry, biophysics and function.

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P2860

Conversion of alpha-lactalbumin to a protein inducing apoptosis

http://www.wikidata.org/entity/Q24681658

description

2000 nî lūn-bûn

@nan

2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

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2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

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2000年论文

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name

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@ast

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@en

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@nl

type

label

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@ast

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@en

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@nl

prefLabel

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@ast

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@en

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Conversion of alpha-lactalbumin to a protein inducing apoptosis

@en

P2093

A K Mossberg

http://www.w3.org/2001/XMLSchema#string

C Svanborg

http://www.w3.org/2001/XMLSchema#string

P2860

Apoptosis induced by a human milk protein

A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli

MOLMOL: a program for display and analysis of macromolecular structures

Molecular characterization of alpha-lactalbumin folding variants that induce apoptosis in tumor cells

The importance of alpha-lactalbumin in infant nutrition

NMR spectroscopy and protein folding: studies of lysozyme and alpha-lactalbumin.

The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

Out of the ER--outfitters, escorts and guides.

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scholarly article

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921781

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10.1073/PNAS.97.8.4221

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8

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97

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Anders P. Hakansson

Mattias Svensson

Sara Snogerup Linse

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2000-04-01T00:00:00Z

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12556709

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10760289

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P921

apoptotic process

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18203

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