Results 151 to 160 of about 24,729 (207)

Sample-sparing multiplexed antibody Fc biomarker discovery using a reconfigurable integrated microfluidic platform.

open access: yesLab Chip
Zhang H   +10 more
europepmc   +1 more source

Exploring distinct modes of inter-spike cross-linking for enhanced neutralization by SARS-CoV-2 antibodies. [PDF]

open access: yesNat Commun
Nan X   +25 more
europepmc   +1 more source

A platform for the rapid screening of equine immunoglobins F (ab)2 derived from single equine memory B cells able to cross-neutralize to influenza virus. [PDF]

open access: yesEmerg Microbes Infect
Lin Y   +11 more
europepmc   +1 more source

<i>UANanoDock</i>: A Web-Based <i>UnitedAtom</i> Multiscale Nanodocking Tool for Predicting Protein Adsorption onto Nanoparticles. [PDF]

open access: yesJ Chem Inf Model
Subbotina J   +7 more
europepmc   +1 more source

A kinetic model of antigen-dependent IgG oligomerization and complement binding

open access: yes
Strasser J   +7 more
europepmc   +1 more source

Crystallographic Data for the Fab Fragment of a Human Myeloma Immunoglobulin

open access: closedNature, 1968
COMPARISONS of the physical properties and chemical structure of myeloma proteins with those of other immunoglobulins and antibodies have indicated that myeloma proteins are abnormal only in their relative homogeneity; they seem to be typical representatives of the immunoglobulin class to which they belong. In addition, antibody activity has been shown
H. P. AVEY   +3 more
openalex   +5 more sources

An easy and simple separation method for Fc and Fab fragments from chicken immunoglobulin Y (IgY)

open access: closedJournal of Chromatography B, 2020
Antigen-binding (Fab) and crystallizable (Fc) fragments are the active components of yolk immunoglobulin (IgY), which have been widely used in the pharmaceutical field. However, the common purification methods for the Fab and Fc fragments use combinations of multi-columns are complex and time-consuming.
Xin Zhou   +3 more
openalex   +4 more sources

Use of molecular replacement in the solution of an immunoglobulin Fab fragment structure [PDF]

open access: possibleActa Crystallographica Section B Structural Science, 1991
Molecular-replacement efficiency depends highly on structural and sequence homologies between available models and the molecule in the crystal being studied. The structure of the Fab fragment of an antibody specific for an influenza virus hemagglutinin was determined by molecular replacement and the Fv and the CH1:CL parts were localized separately ...
Y. Mauguen   +3 more
openaire   +2 more sources

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