Faculty Opinions recommendation of Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies.

2008 ◽  
Author(s):  
Paolo Rossi
Keyword(s):  
Ubiquitin Chain ◽  
Specific Antibodies

scholarly journals Ubiquitin Chain Editing Revealed by Polyubiquitin Linkage-Specific Antibodies

Cell ◽  
2008 ◽  
Vol 134 (4) ◽  
pp. 668-678 ◽  
Author(s):  
Kim Newton ◽  
Marissa L. Matsumoto ◽  
Ingrid E. Wertz ◽  
Donald S. Kirkpatrick ◽  
Jennie R. Lill ◽  
...  
Keyword(s):  
Ubiquitin Chain ◽  
Specific Antibodies

Ribosome Structural Organization

1974 ◽  
Vol 32 ◽  
pp. 332-333
Author(s):  
James A. Lake
Keyword(s):  
Ribosomal Proteins ◽  
Structural Organization ◽  
Three Dimensional ◽  
Small Subunit ◽  
Structural Studies ◽  
X Ray Diffraction ◽  
Specific Antibodies ◽  
X Ray ◽  
E Coli ◽  
Complete Sequences

The understanding of ribosome structure has advanced considerably in the last several years. Biochemists have characterized the constituent proteins and rRNA's of ribosomes. Complete sequences have been determined for some ribosomal proteins and specific antibodies have been prepared against all E. coli small subunit proteins. In addition, a number of naturally occuring systems of three dimensional ribosome crystals which are suitable for structural studies have been observed in eukaryotes. Although the crystals are, in general, too small for X-ray diffraction, their size is ideal for electron microscopy.

Virus-specific antibodies allow viral replication in the marginal zone, thereby promoting CD8+ T-cell priming and viral control

2016 ◽  
Vol 54 (12) ◽  
pp. 1343-1404
Author(s):  
V Duhan ◽  
V Khairnar ◽  
SK Friedrich ◽  
C Hardt ◽  
PA Lang ◽  
...  
Keyword(s):  
T Cell ◽  
Viral Replication ◽  
Marginal Zone ◽  
Cd8 T Cell ◽  
Viral Control ◽  
Specific Antibodies ◽  
T Cell Priming

Naturally Occurring IgG Autoantibodies to Platelet Cytoskeleton Tropomyosin

1996 ◽  
Vol 75 (04) ◽  
pp. 642-647 ◽  
Author(s):  
Ming Hou ◽  
Dick Stockelberg ◽  
Jack Kutti ◽  
Hans Wadenvik
Keyword(s):  
Molecular Weight ◽  
Human Platelet ◽  
Chronic Idiopathic Thrombocytopenic Purpura ◽  
Thrombocytopenic Purpura ◽  
Immunoblot Assay ◽  
Specific Antibodies ◽  
Platelet Protein ◽  
Naturally Occurring ◽  
Normal Individuals ◽  
Cytoskeleton Protein

SummaryWe have observed that naturally occurring serum antibodies generated a 30 Kd band in a platelet immunoblot assay. The target protein had the same molecular weight (30 Kd) under nonreduced and reduced electrophoretic conditions, and could be immunoblotted from either autologous or homologous platelet lysates. Also, the 30 Kd reactive autoantibodies could be totally adsorbed by platelet cytoskeletons. From these data one likely candidate for the autoantibody target was the intracellular platelet protein tropomyosin. Indeed, a commercially available monoclonal antitropomyosin antibody reacted with proteins comigrating with this 30 Kd band; affinity purified human platelet tropomyosin was bound by the antibodies that recognized the 30 Kd protein. This body of evidence conclusively demonstrated that naturally occurring serum autoantibodies reacted with the platelet cytoskeleton protein - tropomyosin. These tropomyosin specific antibodies were found in roughly the same percentage of sera from patients with chronic idiopathic thrombocytopenic purpura (ITP) as from normal individuals.

The Relation Between VIIIR:AG and VIII:C Studied with Two Antisera

1979 ◽  
Author(s):  
H. P. Muller ◽  
N. H. van Tilburg ◽  
R. M. Bertina ◽  
J. J. Veltkamp
Keyword(s):  
Molecular Weight ◽  
High Salt ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Specific Antibodies ◽  
Specific Effects ◽  
Normal Plasma ◽  
Coagulant Activity ◽  
Sterical Hindrance ◽  
Inhibitory Antibodies

FVIII was separated into low molecular weight FVIII (LMW FVIII) and high molecular weight FVIII (HMW FVIII) by gel chromatography in the presence of high salt concentration or by high salt elution of LMW FVIII from FVIII bound to anti HMW FVII-Sepharose. Specific antibodies were raised in rabbits against HMW FVIII and LMW FVIII. After removal of the contaminating anti HMW activities the rabbit anti LMW FVIII was still able to neutralize the FVIII coagulant activity of normal plasma and of IMW FVIII with canparable efficiency and it had no effect on the VIIIR:WF of FVIII in normal plasma or in HMW FVIII. Anti LMW FVIII does not bind to HMW FVIII and does not precipitate FVIII as tested by counter immunoelectrophoresis. Rabbit anti HMW FVIII precipitates FVIII in normal plasma, inhibits VIIIR:WF activity, while it has no effect on the FVIII coagulant activity of LMW FVIII. The coagulant activity of FVIII in normal plasma is slightly inhibited by anti HMW FVIII presumably by non-specific effects (sterical hindrance). It is concluded that inhibitory antibodies against VIII:C raised in rabbits recognize antigenic structures only present on LMW FVIII. Antibodies against HMW FVIII raised in rabbits appears to recognize structures only present on HMW FVIII.

Seroprevalence of specific antibodies during pregnancy and risk for early life infectious diseases

2020 ◽  
Author(s):  
M Albrecht ◽  
G Gabriel ◽  
H Jacobsen ◽  
G Hansen ◽  
H Becher ◽  
...  
Keyword(s):  
Infectious Diseases ◽  
Early Life ◽  
Specific Antibodies
Sign in / Sign up

Export Citation Format

Share Document