Spectrin binding and the control of membrane protein mobility
Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer a...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1978 |
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| Umfang: |
4 Ill. ; 1 Tab. 9 |
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| Reproduktion: |
Wiley InterScience Backfile Collection 1832-2000 |
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| Übergeordnetes Werk: |
in: Journal of Supramolecular Structure - New York, N.Y. : Alan R. Liss, Inc, 8(1978) vom: Apr., Seite 455-463 |
| Übergeordnetes Werk: |
volume:8 ; year:1978 ; month:04 ; pages:455-463 ; extent:9 |
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| 520 | |a Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. | ||
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| 700 | 1 | |a Branton, Daniel |4 oth | |
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(DE-627)NLEJ159895588 DE-627 ger DE-627 rakwb eng Spectrin binding and the control of membrane protein mobility 1978 4 Ill. 1 Tab. 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. Wiley InterScience Backfile Collection 1832-2000 Goodman, Steven R. oth Branton, Daniel oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 8(1978) vom: Apr., Seite 455-463 (DE-627)NLEJ159070716 0091-7419 nnns volume:8 year:1978 month:04 pages:455-463 extent:9 http://dx.doi.org/10.1002/jss.400080408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 8 1978 4 455-463 9 |
| spelling |
(DE-627)NLEJ159895588 DE-627 ger DE-627 rakwb eng Spectrin binding and the control of membrane protein mobility 1978 4 Ill. 1 Tab. 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. Wiley InterScience Backfile Collection 1832-2000 Goodman, Steven R. oth Branton, Daniel oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 8(1978) vom: Apr., Seite 455-463 (DE-627)NLEJ159070716 0091-7419 nnns volume:8 year:1978 month:04 pages:455-463 extent:9 http://dx.doi.org/10.1002/jss.400080408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 8 1978 4 455-463 9 |
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(DE-627)NLEJ159895588 DE-627 ger DE-627 rakwb eng Spectrin binding and the control of membrane protein mobility 1978 4 Ill. 1 Tab. 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. Wiley InterScience Backfile Collection 1832-2000 Goodman, Steven R. oth Branton, Daniel oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 8(1978) vom: Apr., Seite 455-463 (DE-627)NLEJ159070716 0091-7419 nnns volume:8 year:1978 month:04 pages:455-463 extent:9 http://dx.doi.org/10.1002/jss.400080408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 8 1978 4 455-463 9 |
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(DE-627)NLEJ159895588 DE-627 ger DE-627 rakwb eng Spectrin binding and the control of membrane protein mobility 1978 4 Ill. 1 Tab. 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. Wiley InterScience Backfile Collection 1832-2000 Goodman, Steven R. oth Branton, Daniel oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 8(1978) vom: Apr., Seite 455-463 (DE-627)NLEJ159070716 0091-7419 nnns volume:8 year:1978 month:04 pages:455-463 extent:9 http://dx.doi.org/10.1002/jss.400080408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 8 1978 4 455-463 9 |
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(DE-627)NLEJ159895588 DE-627 ger DE-627 rakwb eng Spectrin binding and the control of membrane protein mobility 1978 4 Ill. 1 Tab. 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. Wiley InterScience Backfile Collection 1832-2000 Goodman, Steven R. oth Branton, Daniel oth in Journal of Supramolecular Structure New York, N.Y. : Alan R. Liss, Inc 8(1978) vom: Apr., Seite 455-463 (DE-627)NLEJ159070716 0091-7419 nnns volume:8 year:1978 month:04 pages:455-463 extent:9 http://dx.doi.org/10.1002/jss.400080408 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 8 1978 4 455-463 9 |
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Spectrin binding and the control of membrane protein mobility |
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Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. |
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Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. |
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Transmembrane proteins of the human erythrocyte show restricted in-plane mobility. Many of the restrictions on mobility are attributable to the molecules of spectrin which are located on the protoplasmic surface of the erythrocyte membrane. These molecules are elongate, form end-to-end heterodimer associations, and bind selectively to protein (or proteins) accessible on inside-out, but not right-side out, membrane vesicles. |
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Spectrin binding and the control of membrane protein mobility |
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