UB Paderborn / Katalog / Suche / in CDI

Sortiert nach

Einfacher Volltextzugriff von (fast) überall

Installieren Sie die LibKey Nomad-Browsererweiterung und erhalten Sie von vielen Webseiten einfachen Zugriff auf lizenzierte Volltexte oder Open Access Publikationen. Mehr erfahren...

A path to improved pharmaceutical productivity

Nature reviews. Drug discovery, 2003-09, Vol.2 (9), p.751-753

Cohen, Carl M

2003

Volltextzugriff (PDF)

Pharmacologic Treatment of Type 2 Diabetes in the U.S., Sweden, and Israel

Diabetes care, 2022-12, Vol.45 (12), p.2926-2934

2022

Volltextzugriff (PDF)

Mild spherocytosis and altered red cell ion transport in protein 4.2–null mice

The Journal of clinical investigation, 1999-06, Vol.103 (11), p.1527-1537

1999

Volltextzugriff (PDF)

Guanine nucleotide-dependent translocation of RhoA from cytosol to high affinity membrane binding sites in human erythrocytes

Biochemical journal, 1998-03, Vol.330 ( Pt 3) (3), p.1391-1398

1998

Volltextzugriff (PDF)

The molecular organization of the red cell membrane skeleton

Seminars in hematology, 1983-07, Vol.20 (3), p.141-158

Cohen, C M

1983

Volltextzugriff (PDF)

Human erythrocyte membrane protein band 4.2 (pallidin)

Seminars in hematology, 1993-04, Vol.30 (2), p.119-137

1993

Volltextzugriff (PDF)

Phorbol 12-myristate 13-acetate-stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors : possible role of protein kinase M

Biochemical journal, 1993-12, Vol.296 (3), p.675-683

1993

Volltextzugriff (PDF)

Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3

The Journal of biological chemistry, 1988-07, Vol.263 (21), p.10212-10218

1988

Volltextzugriff (PDF)

Interaction of cytoskeletal proteins on the human erythrocyte membrane

Cell, 1981-04, Vol.24 (1), p.24-32

1981

Volltextzugriff (PDF)

The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene

Nature genetics, 1992-09, Vol.2 (1), p.80-83

1992

Volltextzugriff (PDF)

Organization of the Gene for Human Erythrocyte Membrane Protein 4.2: Structural Similarities with the Gene for the a Subunit of Factor XIII

Proceedings of the National Academy of Sciences - PNAS, 1991-06, Vol.88 (11), p.4840-4844

1991

Volltextzugriff (PDF)

Control of band 3 lateral and rotational mobility by band 4.2 in intact erythrocytes: release of band 3 oligomers from low-affinity binding sites

Biophysical journal, 1996-03, Vol.70 (3), p.1534-1542

1996

Volltextzugriff (PDF)

Complete Amino Acid Sequence and Homologies of Human Erythrocyte Membrane Protein Band 4.2

Proceedings of the National Academy of Sciences - PNAS, 1990-01, Vol.87 (2), p.613-617

1990

Volltextzugriff (PDF)

Specific loss of protein kinase activities in senescent erythrocytes

Blood, 1996-08, Vol.88 (4), p.1479-1487

1996

Volltextzugriff (PDF)

Absence of high-affinity band 4.1 binding sites from membranes of glycophorin C- and D-deficient (Leach phenotype) erythrocytes

Blood, 1994-02, Vol.83 (4), p.1102-1108

1994

Volltextzugriff (PDF)

Modulation of red cell band 4.1 function by cAMP-dependent kinase and protein kinase C phosphorylation

The Journal of biological chemistry, 1988-02, Vol.263 (5), p.2209-2216

1988

Volltextzugriff (PDF)

Questions from a scientific audience: How do I get started?

Nature biotechnology, 1998-06, Vol.16 (6), p.522-524

1998

Volltextzugriff (PDF)

Developmental biology's impact on drug development

Nature biotechnology, 1998-07, Vol.16 (7), p.628-631

1998

Volltextzugriff (PDF)

Maturation of murine erythroleukemia cells committed to differentiation requires protein kinase C

The Journal of biological chemistry, 1992-08, Vol.267 (22), p.15326-15333

1992

Volltextzugriff (PDF)

Purification and properties of human erythrocyte band 4.2. Association with the cytoplasmic domain of band 3

The Journal of biological chemistry, 1986-04, Vol.261 (12), p.5536-5543

1986

Volltextzugriff (PDF)

cDNA Sequence, Gene Sequence, and Properties of Murine Pallidin (Band 4.2), the Protein Implicated in the Murine pallid Mutation

Genomics (San Diego, Calif.), 1994-06, Vol.21 (3), p.478-485

1994

Volltextzugriff (PDF)

Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated

The Journal of biological chemistry, 1992-03, Vol.267 (8), p.5680-5685

1992

Volltextzugriff (PDF)

Human Erythrocyte Dematin and Protein 4.2 (Pallidin) Are ATP Binding Proteins

Biochemistry (Easton), 1996-03, Vol.35 (9), p.3001-3006

1996

Volltextzugriff (PDF)

Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C

The Journal of biological chemistry, 1990-02, Vol.265 (5), p.2556-2562

1990

Volltextzugriff (PDF)

Role of N-myristylation in targeting of band 4.2 (pallidin) in nonerythroid cells

Experimental cell research, 1996-12, Vol.229 (2), p.421-431

1996

Volltextzugriff (PDF)

1 – 25 von 599

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(534)
Mit Volltextzugriff
(493)

Publikationsform

Sprache

Englisch
(599)

Erscheinungsjahr

n.n

Thema

Science & Technology
(527)
Life Sciences & Biomedicine
(437)
Humans
(345)
Biological And Medical Sciences
(224)
Female
(189)
Male
(171)
Medical Sciences
(161)
Adult
(127)
Middle Aged
(101)
Animals
(94)
Fundamental And Applied Biological Sciences. Psychology
(73)
Aged
(65)
Biochemistry & Molecular Biology
(55)
Physical Sciences
(55)
Neurosciences & Neurology
(47)
Adolescent
(43)
Cardiovascular System & Cardiology
(38)
Technology
(38)
Immunology
(37)
Neurosciences
(36)

15 weitere anzeigen...

Weniger anzeigen...

Neu hinzugefügt

... seit 7 Tagen
(1)
... seit 30 Tagen
(2)

Menü

Weitere Dienste

Einstellungen

A path to improved pharmaceutical productivity

Pharmacologic Treatment of Type 2 Diabetes in the U.S., Sweden, and Israel

Mild spherocytosis and altered red cell ion transport in protein 4.2–null mice

Guanine nucleotide-dependent translocation of RhoA from cytosol to high affinity membrane binding sites in human erythrocytes

The molecular organization of the red cell membrane skeleton

Human erythrocyte membrane protein band 4.2 (pallidin)

Phorbol 12-myristate 13-acetate-stimulated phosphorylation of erythrocyte membrane skeletal proteins is blocked by calpain inhibitors : possible role of protein kinase M

Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3

Interaction of cytoskeletal proteins on the human erythrocyte membrane

The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene

Organization of the Gene for Human Erythrocyte Membrane Protein 4.2: Structural Similarities with the Gene for the a Subunit of Factor XIII

Control of band 3 lateral and rotational mobility by band 4.2 in intact erythrocytes: release of band 3 oligomers from low-affinity binding sites

Complete Amino Acid Sequence and Homologies of Human Erythrocyte Membrane Protein Band 4.2

Specific loss of protein kinase activities in senescent erythrocytes

Absence of high-affinity band 4.1 binding sites from membranes of glycophorin C- and D-deficient (Leach phenotype) erythrocytes

Modulation of red cell band 4.1 function by cAMP-dependent kinase and protein kinase C phosphorylation

Questions from a scientific audience: How do I get started?

Developmental biology's impact on drug development

Maturation of murine erythroleukemia cells committed to differentiation requires protein kinase C

Purification and properties of human erythrocyte band 4.2. Association with the cytoplasmic domain of band 3

cDNA Sequence, Gene Sequence, and Properties of Murine Pallidin (Band 4.2), the Protein Implicated in the Murine pallid Mutation

Human erythrocyte protein 4.2, a high copy number membrane protein, is N-myristylated

Human Erythrocyte Dematin and Protein 4.2 (Pallidin) Are ATP Binding Proteins

Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C

Role of N-myristylation in targeting of band 4.2 (pallidin) in nonerythroid cells

Suchergebnisse filtern