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...

Inhibition of Cytohesins Protects against Genetic Models of Motor Neuron Disease

The Journal of neuroscience, 2015-06, Vol.35 (24), p.9088-9105

2015

Volltextzugriff (PDF)

Protein folding in the ER

Seminars in cell & developmental biology, 1999-10, Vol.10 (5), p.443-454

1999

Volltextzugriff (PDF)

The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains

The Journal of biological chemistry, 1992-10, Vol.267 (30), p.21303-21306

1992

Volltextzugriff (PDF)

Inhibition of Immunoglobulin Folding and Secretion by Dominant Negative BiP ATPase Mutants

Proceedings of the National Academy of Sciences - PNAS, 1996-05, Vol.93 (11), p.5269-5274

1996

Volltextzugriff (PDF)

Hsp70 and Antifibrillogenic Peptides Promote Degradation and Inhibit Intracellular Aggregation of Amyloidogenic Light Chains

The Journal of cell biology, 2001-02, Vol.152 (4), p.705-715

2001

Volltextzugriff (PDF)

OR4,23 ER chaperone GRP94 depletion in skeletal muscle reduces muscle and organismal growth through inhibition of IGF-I production

Growth hormone & IGF research, 2010, Vol.20, p.S11-S11

2010

Volltextzugriff (PDF)

Structure and biogenesis of lytic granules

Current topics in microbiology and immunology, 1995, Vol.198, p.39

1995

Volltextzugriff (PDF)

Regulation of kinesin activity by phosphorylation of kinesin-associated proteins

The Journal of biological chemistry, 1994-07, Vol.269 (29), p.19176-19182

1994

Volltextzugriff (PDF)

Inhibition of Amyloid Fiber Assembly by Both BiP and Its Target Peptide

Immunity (Cambridge, Mass.), 2000-10, Vol.13 (4), p.433-442

2000

Volltextzugriff (PDF)

Membrane Biogenesis during B Cell Differentiation: Most Endoplasmic Reticulum Proteins Are Expressed Coordinately

The Journal of cell biology, 1990-05, Vol.110 (5), p.1501-1511

1990

Volltextzugriff (PDF)

GRP94, an ER chaperone with protein and peptide binding properties

Seminars in cell & developmental biology, 1999-10, Vol.10 (5), p.495-505

1999

Volltextzugriff (PDF)

Ig light chains are secreted predominantly as monomers

The Journal of immunology (1950), 1996-10, Vol.157 (7), p.2969-2975

1996

Volltextzugriff (PDF)

The Lytic Granules of Natural Killer Cells Are Dual-Function Organelles Combining Secretory and Pre-Lysosomal Compartments

The Journal of cell biology, 1990-12, Vol.111 (6), p.2327-2340

1990

Volltextzugriff (PDF)

Rapid degradation of an unassembled immunoglobulin light chain is mediated by a serine protease and occurs in a pre-Golgi compartment

The Journal of biological chemistry, 1993-12, Vol.268 (34), p.25940-25947

1993

Volltextzugriff (PDF)

A Single Amino Acid Substitution in the Variable Region of the Light Chain Specifically Blocks Immunoglobulin Secretion

Proceedings of the National Academy of Sciences - PNAS, 1990-10, Vol.87 (20), p.8135-8139

1990

Volltextzugriff (PDF)

Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro

Journal of cell science, 1993, Vol.104 (1), p.151-162

1993

Volltextzugriff (PDF)

Identification of the N-terminal Peptide Binding Site of Glucose-regulated Protein 94

The Journal of biological chemistry, 2004-04, Vol.279 (16), p.16543-16552

2004

Volltextzugriff (PDF)

Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

Nature (London), 1994-08, Vol.370 (6488), p.373-375

1994

Volltextzugriff (PDF)

Two Proteins Targeted to the Same Lytic Granule Compartment Undergo Very Different Posttranslational Processing

Proceedings of the National Academy of Sciences - PNAS, 1989-09, Vol.86 (18), p.7128-7132

1989

Volltextzugriff (PDF)

Radicicol-sensitive Peptide Binding to the N-terminal Portion of GRP94

The Journal of biological chemistry, 2002-10, Vol.277 (43), p.40742-40750

2002

Volltextzugriff (PDF)

Cysteines in CH1 Underlie Retention of Unassembled Ig Heavy Chains

The Journal of biological chemistry, 2005-04, Vol.280 (15), p.14402-14412

2005

Volltextzugriff (PDF)

Sperm Morphogenesis in Wild-Type and Fertilization-Defective Mutants of Caenorhabditis elegans

The Journal of cell biology, 1981-10, Vol.91 (1), p.26-44

1981

Volltextzugriff (PDF)

Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones

Molecular endocrinology (Baltimore, Md.), 1999-09, Vol.13 (9), p.1435-1448

1999

Volltextzugriff (PDF)

Folding of Insulin Receptor Monomers Is Facilitated by the Molecular Chaperones Calnexin and Calreticulin and Impaired by Rapid Dimerization

The Journal of cell biology, 1998-05, Vol.141 (3), p.637-646

1998

Volltextzugriff (PDF)

Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain

Journal of molecular biology, 2001-11, Vol.313 (5), p.1021-1034

2001

Volltextzugriff (PDF)

1 – 25 von 122

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(104)
Mit Volltextzugriff
(106)

Publikationsform

Sprache

Erscheinungsjahr

n.n

Thema

Science & Technology
(73)
Life Sciences & Biomedicine
(48)
Animals
(39)
Humans
(27)
Biological And Medical Sciences
(23)
Mice
(23)
Fundamental And Applied Biological Sciences. Psychology
(17)
Physics
(15)
Exact Sciences And Technology
(14)
Female
(14)
Technology
(14)
Materials Science
(13)
Applied Sciences
(12)
Cell Line
(12)
Immunology
(12)
Male
(12)
Adult
(10)
Cell Biology
(10)
Middle Aged
(10)
Physical Sciences
(10)

15 weitere anzeigen...

Weniger anzeigen...

Menü

Weitere Dienste

Einstellungen

Inhibition of Cytohesins Protects against Genetic Models of Motor Neuron Disease

Protein folding in the ER

The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains

Inhibition of Immunoglobulin Folding and Secretion by Dominant Negative BiP ATPase Mutants

Hsp70 and Antifibrillogenic Peptides Promote Degradation and Inhibit Intracellular Aggregation of Amyloidogenic Light Chains

OR4,23 ER chaperone GRP94 depletion in skeletal muscle reduces muscle and organismal growth through inhibition of IGF-I production

Structure and biogenesis of lytic granules

Regulation of kinesin activity by phosphorylation of kinesin-associated proteins

Inhibition of Amyloid Fiber Assembly by Both BiP and Its Target Peptide

Membrane Biogenesis during B Cell Differentiation: Most Endoplasmic Reticulum Proteins Are Expressed Coordinately

GRP94, an ER chaperone with protein and peptide binding properties

Ig light chains are secreted predominantly as monomers

The Lytic Granules of Natural Killer Cells Are Dual-Function Organelles Combining Secretory and Pre-Lysosomal Compartments

Rapid degradation of an unassembled immunoglobulin light chain is mediated by a serine protease and occurs in a pre-Golgi compartment

A Single Amino Acid Substitution in the Variable Region of the Light Chain Specifically Blocks Immunoglobulin Secretion

Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro

Identification of the N-terminal Peptide Binding Site of Glucose-regulated Protein 94

Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

Two Proteins Targeted to the Same Lytic Granule Compartment Undergo Very Different Posttranslational Processing

Radicicol-sensitive Peptide Binding to the N-terminal Portion of GRP94

Cysteines in CH1 Underlie Retention of Unassembled Ig Heavy Chains

Sperm Morphogenesis in Wild-Type and Fertilization-Defective Mutants of Caenorhabditis elegans

Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones

Folding of Insulin Receptor Monomers Is Facilitated by the Molecular Chaperones Calnexin and Calreticulin and Impaired by Rapid Dimerization

Both the environment and somatic mutations govern the aggregation pathway of pathogenic immunoglobulin light chain

Suchergebnisse filtern