| ¿µ¹® | gene | ÇÑ±Û | À¯ÀüÀÚ |
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| ¿µ¹® | gene therapy | ÇÑ±Û | À¯ÀüÀÚ¿ä¹ý |
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| ¼³¸í | À¯Àüº´À» Ä¡·áÇÒ ¸ñÀûÀ¸·Î, Á¤»óÀûÀ¸·Î ±â´ÉÇÏ´Â ´ÜÀÏÀ¯ÀüÀÚ È¤Àº º¹¼öÀ¯ÀüÀÚ¸¦ ¾î¶² ±â¿ø¿¡¼ ¾ò¾î³»¾î »ý¼¼Æ÷¿¡ µµÀÔÇÏ´Â °Í. À¯Àü¹°ÁúÀº À¯ÀüÀÚ»ðÀÔ Á¶ÀÛ¿¡ ÀÇÇØ ¼ö¿ë¼¼Æ÷¿¡·Î µµÀԵȴÙ. Áï, À¯ÀüÀÚ¸¦ ³¢¿ö ³ÖÀº »õ·Î¿î ¼¼Æ÷¸¦ »ç¿ëÇÏ´Â Ä¡·á·Î¼ 1980³â ¹Ì±¹ÀÇ ÇÐÀÚ°¡ ÁöÁßÇØºóÇ÷ȯÀÚ¿¡°Ô °ÇàÇÏ¿© ºñÆÇÀ» ¹Þ¾ÒÁö¸¸, ¹Ì±¹ ±¹¸³º¸°Ç¿¬±¸¼Ò´Â 1990³â 9¿ù ¾Æµ¥³ë½Å µ¥¾Æ¹Ì³ª¾ÆÁ¦(adenosine deaminase, ADA) °áÇÌÁõ ȯÀÚÀÇ ¸²ÇÁ±¸¿¡ ADA À¯ÀüÀÚ¸¦ ³¢¿ö ³Ö´Â Ä¡·á¸¦ ½ÃÀÛÇÑ ÀÌ·¡ ÇöÀç´Â ¾ÏÀ» Æ÷ÇÔÇÑ ¸¹Àº Áúº´µéÀ» Ä¡·áÇÏ´Â ¸ñÀûÀ¸·Î ¾²ÀδÙ. |
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| Bmod | behavior modification |
|---|---|
| CM | California mastitis [test]; calmodulin; capreomycin; carboxymethyl; cardiac murmur; cardiac muscle; ... |
| CMS | children's medical services; Christian Medical Society; chronic myelodysplastic syndrome; chromosome... |
| EBM | electrophysiologic behavior modification; epidermal basement membrane; evidence-based medicine; expr... |
| ICD-9-CM | International Classification of Diseases-ninth revision-Clinical Modification |
| DMF | Dose modification factors |
|---|---|
| ICD9CM | International Classification of Diseases 9th Revision Clinical Modification |
| ICD-9 CM | International Classification of Diseases, Ninth Revision, Clinical Modification |
| MDRD | Modification of Diet in Renal Disease |
| R-M | Restriction and modification |
| modification | 1. A nonhereditary change in an organism; e.g., one that is acquired from its own activity or environment. 2. A chemical or structural alteration in a molecule. Behaviour modification, the systematic use of principles of conditioning and learning, especially operant or instrumental conditioning, to teach certain skills or to extinguish undesirable behaviours, attitudes, or phobias. Chemical modification, alteration in the structure of a molecule, typically a macromolecule such as a protein, by chemical means; often, the covalent addition by some reagent. Covalent modification, alteration in the structure of a macromolecule by enzymatic means, resulting in a change in the properties of that macromolecule; frequently, this type of modification is physiologically relevant. (05 Mar 2000) |
|---|---|
| modification enzyme | <enzyme, molecular biology> An enzyme that introduces minor bases into DNA or RNA or that alters bases already incorporated. Serves to alter the sequence so that restriction enzymes will not damage the strand. (18 Nov 1997) |
| post-translational modification | The enzymatic processing of a polypeptide chain after translation from messenger RNA and after peptide bond formation has occurred. Examples include glycosylation, acylation, limited proteolysis, phosphorylation, isoprenylation. (10 Oct 1997) |
| ScrFI modification methylase | <enzyme> From lactococcus lactis subsp. Cremoris uc503; recognises sequence ccngg and forms m(5)ccngg; see also DNA modification methylase dsav and DNA modification methylase ssoii Registry number: EC 2.1.1.- Synonym: scrfi methylase (26 Jun 1999) |
| host restriction-modification | A bacterial system where the bacterium is able to destroy invading DNA from a bacteriophage (virus which infects bacteria) while at the same time preventing the destruction of their own DNA. The phage DNA is cleaved by a restriction enzyme made by the bacterium, the bacterial DNA is modified (usually with methylation) so that the enzyme will not destroy it. (09 Oct 1997) |
| Stirling's modification of Gram's stain | <technique> A stable aniline-crystal violet stain. (05 Mar 2000) |
| DNA modification | <molecular biology> A variety of chemical changes made to a DNA molecule just after it has been replicated. An example is DNA methylation. (09 Oct 1997) |
| DNA modification methylases | <enzyme> Enzymes that are part of the restriction-modification systems. They are responsible for producing a species-characteristic methylation pattern, on either adenine or cytosine residues, in a specific short base sequence in the host cell's own DNA. This methylated sequence will occur many times in the hosT-cell DNA and remain intact for the lifetime of the cell. Any DNA from another species which gains entry into a living cell and lacks the characteristic methylation pattern will be recognised by the restriction endonucleases of similar specificity and destroyed by cleavage. most have been studied in bacterial systems, but a few have been found in eukaryotic organisms. Registry number: EC 2.1.1.- (12 Dec 1998) |
| DNA restriction-modification enzymes | Systems consisting of two enzymes, a modification methylase and a restriction endonuclease. They are closely related in their specificity and protect the DNA of a given bacterial species. The methylase adds methyl groups to adenine or cytosine residues in the same target sequence that constitutes the restriction enzyme binding site. The methylation renders the target site resistant to restriction, thereby protecting DNA against cleavage. (12 Dec 1998) |
| allelic gene | See: allele, dominance of traits. (05 Mar 2000) |
| antibiotic resistance gene | Genes in a microorganism which confer resistance to antibiotics, for example by coding for enzymes which destroy it, by coding for surface proteins which prevent it from entering the microorganism, or by being a mutant form of the antibiotic's target so that it can ignore it. (09 Oct 1997) |
| autosomal gene | A gene located on any chromosome other than the sex chromosomes (X or Y). (05 Mar 2000) |
| bicoid gene | A group of genes which are important to the proper development of the head and thorax in the embryo of the fruit fly Drosophila melanogaster. (09 Oct 1997) |
| BRCA1 breast cancer susceptibility gene | This mutated (changed) version of the BRCA1 gene makes a person susceptible to developing breast cancer. (12 Dec 1998) |
| calcitonin gene-related peptide | <protein> A second product transcribed from the calcitonin gene. Calcitonin gene related peptide is found in a number of tissues including nervous tissue. It is a vasodilator that may participate in the cutaneous triple response. It is a neuropeptide of 37 amino acids with structural homology to salmon calcitonin. Co-localises with substance P in neurons. It occurs as a result of alternative processing of mRNA from the calcitonin gene. The neuropeptide is widely distributed in neural tissue of the brain, gut, perivascular nerves, and other tissue. The peptide produces multiple biological effects and has both circulatory and neurotransmitter modes of action. In particular, it is a potent endogenous vasodilator. Intracerebral administration leads to a rise in noradrenergic sympathetic outflow, a rise in blood pressure and a fall in gastric secretion. Acronym: CGRP (05 May 2002) |
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