BIOMAT Database Logo BIOMAT Database Logo

Immunoglobulin and amyloid fibril proteins. 1973

G G Glenner

UI MeSH Term Description Entries
D007136 Immunoglobulins Multi-subunit proteins which function in IMMUNITY. They are produced by B LYMPHOCYTES from the IMMUNOGLOBULIN GENES. They are comprised of two heavy (IMMUNOGLOBULIN HEAVY CHAINS) and two light chains (IMMUNOGLOBULIN LIGHT CHAINS) with additional ancillary polypeptide chains depending on their isoforms. The variety of isoforms include monomeric or polymeric forms, and transmembrane forms (B-CELL ANTIGEN RECEPTORS) or secreted forms (ANTIBODIES). They are divided by the amino acid sequence of their heavy chains into five classes (IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M) and various subclasses. Globulins, Immune,Immune Globulin,Immune Globulins,Immunoglobulin,Globulin, Immune
D008247 Lysosomes A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured or undergoes MEMBRANE FUSION. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed). Autolysosome,Autolysosomes,Lysosome
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010587 Phagocytosis The engulfing and degradation of microorganisms; other cells that are dead, dying, or pathogenic; and foreign particles by phagocytic cells (PHAGOCYTES). Phagocytoses
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D001797 Blood Protein Electrophoresis Electrophoresis applied to BLOOD PROTEINS. Hemoglobin Electrophoresis,Electrophoresis, Blood Protein,Electrophoresis, Hemoglobin,Protein Electrophoresis, Blood
D002942 Circular Dichroism A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

G G Glenner
Amyloid fibril proteins.
November 2002, Mechanisms of ageing and development,
G G Glenner
[Amyloid fibril proteins and their precursors].
April 1991, Nihon rinsho. Japanese journal of clinical medicine,
G G Glenner
Prediction of amyloid fibril-forming proteins.
April 2001, The Journal of biological chemistry,
G G Glenner
Amyloid fibril protein related to immunoglobulin lambda-chains.
April 1975, Journal of immunology (Baltimore, Md. : 1950),
G G Glenner
The biochemical genetics of amyloid fibril proteins.
January 1989, La Ricerca in clinica e in laboratorio,
G G Glenner
Theory of amyloid fibril nucleation from folded proteins.
July 2017, Israel journal of chemistry,
G G Glenner
A new method to classify amyloid fibril proteins.
January 1985, Acta neuropathologica,
G G Glenner
Stabilization of discordant helices in amyloid fibril-forming proteins.
May 2004, Protein science : a publication of the Protein Society,
G G Glenner
Nomenclature 2014: Amyloid fibril proteins and clinical classification of the amyloidosis.
December 2014, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis,
G G Glenner
Amyloid fibril proteins found in Papua New Guinean and other amyloidoses.
March 1978, Papua and New Guinea medical journal,
Copied contents to your clipboard!