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Chaperone (protein)

Index Chaperone (protein)

In molecular biology, molecular chaperones are proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures. [1]

72 relations: Adenosine diphosphate, Adenosine triphosphate, AHSA1, Anfinsen's dogma, Apoptosis, Bacteria, Bacterial adhesin, Binding immunoglobulin protein, Biological membrane, Calnexin, Calreticulin, Chaperome, Chaperone DnaJ, Chaperonin, Chemical chaperone, Co-chaperone, Cytosol, DNA, Endoplasmic reticulum, ERP29, Escherichia coli, Eukaryote, Fungal prion, Gene expression, Glucose-regulated protein, Green fluorescent protein, GroEL, GroES, Heat shock protein, Heat shock protein 47, Hereditary inclusion body myopathy, Histone, Hop (protein), HSF1, Hsp33, HSP60, Hsp70, Hsp90, HSP90B1, Hydrophobe, Immunophilins, In vitro, In vivo, Macromolecular crowding, Matrix (biology), Mitochondrion, Molecular biology, Molecular Microbiology (journal), Nanometre, Nucleoplasmin, ..., Nucleosome, PDIA3, Peptide, Pharmacological chaperone, Prion, Proteasome, Protein, Protein aggregation, Protein dimer, Protein disulfide-isomerase, Protein domain, Protein dynamics, Protein folding, Protein precursor, Protein targeting, Proteolysis, R. John Ellis, Ron Laskey, Saccharomyces cerevisiae, Serine protease, Steric effects, Translocon. Expand index (22 more) »

Adenosine diphosphate

Adenosine diphosphate (ADP), also known as adenosine pyrophosphate (APP), is an important organic compound in metabolism and is essential to the flow of energy in living cells.

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Adenosine triphosphate

Adenosine triphosphate (ATP) is a complex organic chemical that participates in many processes.

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AHSA1

Activator of 90 kDa heat shock protein ATPase homolog 1 is an enzyme that in humans is encoded by the AHSA1 gene.

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Anfinsen's dogma

Anfinsen's dogma (also known as the thermodynamic hypothesis) is a postulate in molecular biology that states that, at least for a small globular protein in its standard physiological environment, the native structure is determined only by the protein's amino acid sequence.

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Apoptosis

Apoptosis (from Ancient Greek ἀπόπτωσις "falling off") is a process of programmed cell death that occurs in multicellular organisms.

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Bacteria

Bacteria (common noun bacteria, singular bacterium) is a type of biological cell.

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Bacterial adhesin

Adhesins are cell-surface components or appendages of bacteria that facilitate adhesion or adherence to other cells or to surfaces, usually the host they are infecting or living in.

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Binding immunoglobulin protein

Binding immunoglobulin protein (BiP) also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 (HSPA5) is a protein that in humans is encoded by the HSPA5 gene.

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Biological membrane

A biological membrane or biomembrane is an enclosing or separating membrane that acts as a selectively permeable barrier within living things.

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Calnexin

Calnexin (CNX) is a integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER).

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Calreticulin

Calreticulin also known as calregulin, CRP55, CaBP3, calsequestrin-like protein, and endoplasmic reticulum resident protein 60 (ERp60) is a protein that in humans is encoded by the CALR gene.

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Chaperome

Chaperome refers to the ensemble of all cellular molecular chaperone and co-chaperone proteins that assist protein folding of misfolded proteins or folding intermediates in order to ensure native protein folding and function, to antagonize aggregation-related proteotoxicity and ensuing protein loss-of-function or protein misfolding-diseases such as the neurodegenerative diseases Alzheimer's, Huntington's or Parkinson's disease, as well as to safeguard cellular proteostasis and proteome balance.

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Chaperone DnaJ

In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kD), is a molecular chaperone protein.

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Chaperonin

Chaperonins are proteins that provide favourable conditions for the correct folding of other proteins, thus preventing aggregation.

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Chemical chaperone

Chemical chaperones are a class of small molecules that function to enhance the folding and/or stability of proteins.

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Co-chaperone

Co-chaperones are proteins that assist chaperones in protein folding and other functions.

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Cytosol

The cytosol, also known as intracellular fluid (ICF) or cytoplasmic matrix, is the liquid found inside cells.

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DNA

Deoxyribonucleic acid (DNA) is a thread-like chain of nucleotides carrying the genetic instructions used in the growth, development, functioning and reproduction of all known living organisms and many viruses.

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Endoplasmic reticulum

The endoplasmic reticulum (ER) is a type of organelle found in eukaryotic cells that forms an interconnected network of flattened, membrane-enclosed sacs or tube-like structures known as cisternae.

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ERP29

Endoplasmic reticulum protein 29 (ERp29) is a chaperone protein that in humans is encoded by the ERP29 gene.

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Escherichia coli

Escherichia coli (also known as E. coli) is a Gram-negative, facultatively anaerobic, rod-shaped, coliform bacterium of the genus Escherichia that is commonly found in the lower intestine of warm-blooded organisms (endotherms).

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Eukaryote

Eukaryotes are organisms whose cells have a nucleus enclosed within membranes, unlike Prokaryotes (Bacteria and other Archaea).

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Fungal prion

A fungal prion is a prion that infects fungal hosts.

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Gene expression

Gene expression is the process by which information from a gene is used in the synthesis of a functional gene product.

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Glucose-regulated protein

Glucose-regulated protein is a protein in the endoplasmic reticulum in the cell.

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Green fluorescent protein

The green fluorescent protein (GFP) is a protein composed of 238 amino acid residues (26.9 kDa) that exhibits bright green fluorescence when exposed to light in the blue to ultraviolet range.

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GroEL

GroEL belongs to the chaperonin family of molecular chaperones, and is found in a large number of bacteria.

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GroES

Heat shock 10 kDa protein 1 (Hsp10) also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF) is a protein that in humans is encoded by the HSPE1 gene.

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Heat shock protein

Heat shock proteins (HSP) are a family of proteins that are produced by cells in response to exposure to stressful conditions.

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Heat shock protein 47

Heat shock protein 47, also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen.

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Hereditary inclusion body myopathy

Hereditary inclusion body myopathies (HIBM) are a heterogeneous group of very rare genetic disorders which have different symptoms.

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Histone

In biology, histones are highly alkaline proteins found in eukaryotic cell nuclei that package and order the DNA into structural units called nucleosomes.

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Hop (protein)

Hop, occasionally written HOP, is an abbreviation for Hsp70-Hsp90 Organizing Protein.

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HSF1

Heat shock factor 1 (HSF1) is a protein that in humans is encoded by the HSF1 gene.

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Hsp33

Hsp33 protein is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation.

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HSP60

Heat shock proteins are generally responsible for preventing damage to proteins in response to high levels of heat.

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Hsp70

The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins.

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Hsp90

Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in protein degradation.

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HSP90B1

Heat shock protein 90kDa beta member 1 (HSP90B1), known also as endoplasmin, gp96, grp94, or ERp99, is a chaperone protein that in humans is encoded by the HSP90B1 gene.

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Hydrophobe

In chemistry, hydrophobicity is the physical property of a molecule (known as a hydrophobe) that is seemingly repelled from a mass of water.

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Immunophilins

In molecular biology, immunophilins are endogenous cytosolic peptidyl-prolyl isomerases (PPI) that catalyze the interconversion between the cis and trans isomers of peptide bonds containing the amino acid proline (Pro).

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In vitro

In vitro (meaning: in the glass) studies are performed with microorganisms, cells, or biological molecules outside their normal biological context.

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In vivo

Studies that are in vivo (Latin for "within the living"; often not italicized in English) are those in which the effects of various biological entities are tested on whole, living organisms or cells, usually animals, including humans, and plants, as opposed to a tissue extract or dead organism.

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Macromolecular crowding

The phenomenon of macromolecular crowding alters the properties of molecules in a solution when high concentrations of macromolecules such as proteins are present.

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Matrix (biology)

In biology, matrix (plural: matrices) is the material (or tissue) in animal or plant cells, in which more specialized structures are embedded, and a specific part of the mitochondrion.

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Mitochondrion

The mitochondrion (plural mitochondria) is a double-membrane-bound organelle found in most eukaryotic organisms.

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Molecular biology

Molecular biology is a branch of biology which concerns the molecular basis of biological activity between biomolecules in the various systems of a cell, including the interactions between DNA, RNA, proteins and their biosynthesis, as well as the regulation of these interactions.

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Molecular Microbiology (journal)

Molecular Microbiology is a bimonthly peer-reviewed scientific journal covering all aspects of molecular microbiology.

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Nanometre

The nanometre (International spelling as used by the International Bureau of Weights and Measures; SI symbol: nm) or nanometer (American spelling) is a unit of length in the metric system, equal to one billionth (short scale) of a metre (m).

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Nucleoplasmin

Nucleoplasmin, the first identified molecular chaperone is a thermostable acidic protein with a pentameric structure.

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Nucleosome

A nucleosome is a basic unit of DNA packaging in eukaryotes, consisting of a segment of DNA wound in sequence around eight histone protein cores.

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PDIA3

Protein disulfide-isomerase A3 (PDIA3), also known as glucose-regulated protein, 58-kD (GRP58), is an isomerase enzyme.

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Peptide

Peptides (from Gr.: πεπτός, peptós "digested"; derived from πέσσειν, péssein "to digest") are short chains of amino acid monomers linked by peptide (amide) bonds.

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Pharmacological chaperone

A pharmacological chaperone (or pharmacoperone, from "protein chaperone") is a small molecule that enters cells and serves as a molecular scaffolding in order to cause otherwise-misfolded mutant proteins to fold and route correctly within the cell.

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Prion

Prions are misfolded proteins that are associated with several fatal neurodegenerative diseases in animals and humans.

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Proteasome

Proteasomes are protein complexes which degrade unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds.

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Protein

Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues.

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Protein aggregation

Protein aggregation is a biological phenomenon in which mis-folded proteins aggregate (i.e., accumulate and clump together) either intra- or extracellularly.

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Protein dimer

In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound.

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Protein disulfide-isomerase

Protein disulfide isomerase, or PDI, is an enzyme in the endoplasmic reticulum (ER) in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold.

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Protein domain

A protein domain is a conserved part of a given protein sequence and (tertiary) structure that can evolve, function, and exist independently of the rest of the protein chain.

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Protein dynamics

Proteins are generally thought to adopt unique structures determined by their amino acid sequences, as outlined by Anfinsen's dogma.

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Protein folding

Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.

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Protein precursor

A protein precursor, also called a pro-protein or pro-peptide, is an inactive protein (or peptide) that can be turned into an active form by post-translational modification, such as breaking off a piece of the molecule or adding on another molecule.

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Protein targeting

Protein targeting or protein sorting is the biological mechanism by which proteins are transported to the appropriate destinations in the cell or outside it.

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Proteolysis

Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids.

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R. John Ellis

Reginald John Ellis (born 12 February 1935) is a British scientist.

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Ron Laskey

Ronald Alfred Laskey CBE FRS (born 26 January 1945) is a British cell biologist and cancer researcher.

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Saccharomyces cerevisiae

Saccharomyces cerevisiae is a species of yeast.

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Serine protease

Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the (enzyme's) active site.

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Steric effects

Steric effects are nonbonding interactions that influence the shape (conformation) and reactivity of ions and molecules.

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Translocon

The translocon (commonly known as a translocator or translocation channel) is a complex of proteins associated with the translocation of polypeptides across membranes.

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References

[1] https://en.wikipedia.org/wiki/Chaperone_(protein)

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