| D002352 |
Carrier Proteins |
Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. |
Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier |
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| D002874 |
Chromosome Mapping |
Any method used for determining the location of and relative distances between genes on a chromosome. |
Gene Mapping,Linkage Mapping,Genome Mapping,Chromosome Mappings,Gene Mappings,Genome Mappings,Linkage Mappings,Mapping, Chromosome,Mapping, Gene,Mapping, Genome,Mapping, Linkage,Mappings, Chromosome,Mappings, Gene,Mappings, Genome,Mappings, Linkage |
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| D002896 |
Chromosomes, Human, Pair 6 |
A specific pair GROUP C CHROMSOMES of the human chromosome classification. |
Chromosome 6 |
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| D006360 |
Heat-Shock Proteins |
Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions. |
Stress Protein,Stress Proteins,Heat-Shock Protein,Heat Shock Protein,Heat Shock Proteins,Protein, Stress |
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| D006801 |
Humans |
Members of the species Homo sapiens. |
Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man |
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| D000075102 |
Organic Cation Transporter 2 |
Organic cation transporter consisting of twelve transmembrane domains and expressed primarily in the kidney. It transports a wide range of metabolites, drugs, and neurotransmitters from the blood to the KIDNEY TUBULES, including DOPAMINE; SEROTONIN; CHOLINE; and CISPLATIN. |
OCT2 Protein,SLC22A2 Protein,Solute Carrier Family 22 Member 2 |
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| D016133 |
Polymerase Chain Reaction |
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships. |
Anchored PCR,Inverse PCR,Nested PCR,PCR,Anchored Polymerase Chain Reaction,Inverse Polymerase Chain Reaction,Nested Polymerase Chain Reaction,PCR, Anchored,PCR, Inverse,PCR, Nested,Polymerase Chain Reactions,Reaction, Polymerase Chain,Reactions, Polymerase Chain |
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| D056404 |
Chaperonin Containing TCP-1 |
A group II chaperonin found in eukaryotic CYTOSOL. It is comprised of eight subunits with each subunit encoded by a separate gene. This chaperonin is named after one of its subunits which is a T-COMPLEX REGION-encoded polypeptide. |
CCT delta Subunit,Chaperonin CCT,Chaperonin CCT, alpha Subunit,Chaperonin CCT, beta Subunit,Chaperonin CCT, delta Subunit,Chaperonin CCT, epsilon Subunit,Chaperonin CCT, eta Subunit,Chaperonin CCT, gamma Subunit,Chaperonin CCT, theta Subunit,Chaperonin CCT, zeta1 Subunit,Chaperonin CCT, zeta2 Subunit,Chaperonin Containing TCP1, Subunit 1,Chaperonin Containing TCP1, Subunit 2,Chaperonin Containing TCP1, Subunit 3,Chaperonin Containing TCP1, Subunit 4,Chaperonin Containing TCP1, Subunit 5,Chaperonin Containing TCP1, Subunit 6A,Chaperonin Containing TCP1, Subunit 6B,Chaperonin Containing TCP1, Subunit 7,Chaperonin Containing TCP1, Subunit 8,Chaperonin Containing t-Complex Polypeptide,Chaperonin-Containing T-Complex Polypeptide 1,Cytosolic Chaperonin,Cytosolic Molecular Chaperone CCT,Testis Complex Polypeptide 1,t-Complex Polypeptide 1,t-Complex Protein 1,Chaperonin Containing T Complex Polypeptide 1,Chaperonin Containing TCP 1,Chaperonin Containing t Complex Polypeptide,Chaperonin, Cytosolic,t Complex Polypeptide 1,t Complex Protein 1 |
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| D018832 |
Molecular Chaperones |
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures. |
Chaperones, Molecular,Chaperone, Molecular,Molecular Chaperone |
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| D018833 |
Chaperonins |
A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins utilize the energy of ATP hydrolysis to enhance the efficiency of PROTEIN FOLDING reactions and thereby help proteins reach their functional conformation. The family of chaperonins is split into GROUP I CHAPERONINS, and GROUP II CHAPERONINS, with each group having its own repertoire of protein subunits and subcellular preferences. |
Chaperonin,Chaperonin Complex,Chaperonin Complexes,Chaperonin Family,Chaperonin Protein Complex,Complex, Chaperonin |
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