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English
Fluorescence studies of spectrin and its subunits
scientific article published on 01 January 1994
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scholarly article
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
title
Fluorescence studies of spectrin and its subunits
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
author name string
Subbarao NK
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
MacDonald RC
series ordinal
2
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
language of work or name
English
0 references
publication date
1 January 1994
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
published in
Cytoskeleton
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
volume
29
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
issue
1
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
page(s)
72-81
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
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Structural analysis of homologous repeated domains in alpha-actinin and spectrin
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7 January 2021
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Hydrodynamic characterization of the heterodimer of spectrin
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Fluorescence quenching studies with proteins
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A hydrophobic quencher of protein fluorescence: 2,2,2-trichloroethanol
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Human spectrin. I. A classical light scattering study
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Membrane skeleton-bilayer interaction is not the major determinant of membrane phospholipid asymmetry in human erythrocytes.
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Fluorescence quenching studies of bovine growth hormone in several conformational states
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Binding of hydrophobic ligands to spectrin
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Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites
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Structural study of spectrin from human erythrocyte membranes
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Heat-induced alterations in monkey erythrocyte membrane phospholipid organization and skeletal protein structure and interactions.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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On the structure of erythrocyte spectrin in partially expanded membrane skeletons
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An electro-optic study of human erythrocyte spectrin dimers. The presence of calcium ions does not alter spectrin flexibility
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Preparation of red-cell-membrane cytoskeletal constituents and characterisation of protein 4.1.
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6-(p-Toluidinyl)naphthalene-2-sulfonic acid as a fluorescent probe of yeast hexokinase: conformational states induced by sugar and nucleotide ligands
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Ultrastructure of the intact skeleton of the human erythrocyte membrane
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Interaction of spectrin with phospholipids. Quenching of spectrin intrinsic fluorescence by phospholipid suspensions
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Erythrocyte spectrin is comprised of many homologous triple helical segments
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Human spectrin. VI. A viscometric study
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Human erythrocyte spectrin dimer intrinsic viscosity: temperature dependence and implications for the molecular basis of the erythrocyte membrane free energy.
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Band 4.1 enhances spectrin binding to phosphatidylserine vesicles
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Secondary structure prediction for the spectrin 106-amino acid segment, and a proposed model for tertiary structure
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Exposure of hydrophobic domains of clathrin in its membrane fusion-inducible pH region
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Identifiers
DOI
10.1002/CM.970290107
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
PubMed ID
7820859
1 reference
stated in
Europe PubMed Central
PubMed ID
7820859
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7820859%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 October 2019
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