Partial characterization of the cytoplasmic domain of human kidney band 3. (Q38293231)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7629093%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

title

Partial characterization of the cytoplasmic domain of human kidney band 3 (English)

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22 October 2019

4

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22 October 2019

author name string

C C Wang

series ordinal

1

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22 October 2019

R Moriyama

series ordinal

2

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22 October 2019

C R Lombardo

series ordinal

3

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22 October 2019

language of work or name

English

0 references

publication date

1 July 1995

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Journal of Biological Chemistry

22 October 2019

published in

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22 October 2019

volume

270

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22 October 2019

issue

30

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22 October 2019

page(s)

17892-17897

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22 October 2019

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https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Structure and function of the cytoplasmic domain of band 3: center of erythrocyte membrane-peripheral protein interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Subtypes of intercalated cells in rat kidney collecting duct defined by antibodies against erythroid band 3 and renal vacuolar H+-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

A 45-kDa protein antigenically related to band 3 is selectively expressed in kidney mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Hemichrome binding to band 3: nucleation of Heinz bodies on the erythrocyte membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Expression, purification, and characterization of the functional dimeric cytoplasmic domain of human erythrocyte band 3 in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

The complete amino acid sequence of the human erythrocyte membrane anion-transport protein deduced from the cDNA sequence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Cloning and characterization of band 3, the human erythrocyte anion-exchange protein (AE1)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Multiple tissue-specific sites of transcriptional initiation of the mouse anion antiport gene in erythroid and renal cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

Binding constants and stoichiometries of glyceraldehyde 3-phosphate dehydrogenase-tubulin complexes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.30.17892

21 January 2018

Identifiers

DOI

10.1074/JBC.270.30.17892

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7629093%20AND%20SRC:MED&resulttype=core&format=json

22 October 2019

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