Results 41 to 50 of about 42,931 (245)

C1q-targeted inhibition of the classical complement pathway prevents injury in a novel mouse model of acute motor axonal neuropathy [PDF]

open access: yes, 2016
Introduction Guillain-Barré syndrome (GBS) is an autoimmune disease that results in acute paralysis through inflammatory attack on peripheral nerves, and currently has limited, non-specific treatment options.
Barrie, Jennifer A.   +8 more
core   +2 more sources

Interaction between complement subcomponent C1q and bacterial lipopolysaccharides [PDF]

open access: yesBiochemical Journal, 1989
The heptose-less mutant of Escherichia coli, D31m4, bound complement subcomponent C1q and its collagen-like fragments (C1qCLF) with Ka values of 1.4 x 10(8) and 2.0 x 10(8) M-1 respectively. This binding was suppressed by chemical modification of C1q and C1qCLF using diethyl pyrocarbonate (DEPC).
A, Zohair   +3 more
openaire   +2 more sources

Complement C1q activates tumor suppressor WWOX to induce apoptosis in prostate cancer cells. [PDF]

open access: yesPLoS ONE, 2009
BACKGROUND:Tissue exudates contain low levels of serum complement proteins, and their regulatory effects on prostate cancer progression are largely unknown.
Qunying Hong   +10 more
doaj   +1 more source

Human C1q Induces Apoptosis in an Ovarian Cancer Cell Line via Tumor Necrosis Factor [PDF]

open access: yes, 2016
Copyright: © 2016 Kaur, Sultan, Murugaiah, Pathan, Alhamlan, Karteris and Kishore. Human C1q is the first recognition subcomponent of the complement classical pathway that plays a vital role in the clearance of immune complexes, pathogens and apoptotic ...
Alhamlan, F   +6 more
core   +1 more source

C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions

open access: yesFrontiers in Immunology, 2017
Complement C1 is the defining component of the classical pathway. Within the C1qC1r2C1s2 complex, C1q functions as a molecular scaffold for C1r2C1s2 and C1q binding to its ligands activates these two serine proteases.
Jinhua Lu, Uday Kishore
doaj   +1 more source

Complement activation and protein adsorption by carbon nanotubes [PDF]

open access: yes, 2006
As a first step to validate the use of carbon nanotubes as novel vaccine or drug delivery devices, their interaction with a part of the human immune system, complement, has been explored.
Flahaut, Emmanuel   +5 more
core   +2 more sources

Paths reunited: initiation of the classical and lectin pathways of complement activation [PDF]

open access: yes, 2010
Understanding the structural organisation and mode of action of the initiating complex of the classical pathway of complement activation (C1) has been a central goal in complement biology since its isolation almost 50 years ago.
Keeble, Anthony H.   +4 more
core   +1 more source

Complement C1q expression in Erythema nodosum leprosum

open access: yesPLOS Neglected Tropical Diseases, 2018
Complement C1q is a soluble protein capable of initiating components of the classical pathway in host defence system. In earlier qualitative studies, C1q has been implicated in the pathogenesis of Erythema Nodosum Leprosum (ENL). However, little is known about the role of this complement in ENL reaction.
Edessa Negera   +5 more
openaire   +4 more sources

Complement Component C1q and Anti‐C1q Antibodies in Theory and in Clinical Practice [PDF]

open access: yesScandinavian Journal of Immunology, 2008
AbstractThe complement system is a major part of the innate immunity. The first component of the classical pathway of complement activation, C1q, plays a crucial role in the clearance of immune complexes and apoptotic bodies from the organism. Autoantibodies against C1q (anti‐C1q) have been found in a number of autoimmune and infectious diseases.
E, Potlukova, P, Kralikova
openaire   +2 more sources

A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system [PDF]

open access: yes, 2008
The M protein of Streptococcus equi subsp. equi known as fibrinogen-binding protein (FgBP) is a cell wall-associated protein with antiphagocytic activity that binds IgG. Recombinant versions of the seven equine IgG subclasses were used to investigate the
Abi-Rached   +49 more
core   +4 more sources

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