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"collagen helix"¿¡ ´ëÇÑ °Ë»ö °á°úÀÔ´Ï´Ù. °Ë»ö °á°ú º¸´Â µµÁß¿¡ Tab ۸¦ ´©¸£½Ã¸é °Ë»ö âÀÌ ¼±Åõ˴ϴÙ.
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¿µ¹® collagen ÇÑ±Û ¾Æ±³Áú, ÄݶóÁ¨
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  • ¿µ¹®
    ÇѱÛ
  • double helix
    ÀÌÁß³ª¼±
  • double stranded helix
    ÀÌÁß°¡´Ú³ª¼±
  • helix
    1. ³ª¼± 2. ±Ó¹ÙÄû, ÀÌ·û
  • collagen
    ¾Æ±³Áú, Äݶó°Õ
  • collagen band
    ¾Æ±³Áú¶ì
  • collagen disease
    Äݶó°Õº´
  • collagen fiber
    ¾Æ±³¼¶À¯
  • collagen graft
    ¾Æ±³ÁúÀ̽Ä
  • collagen implant
    ¾Æ±³ÁúÀ̽Ä, Äݶó°ÕÀ̽Ä
  • collagen injection
    ¾Æ±³ÁúÁÖ»ç, Äݶó°ÕÁÖ»ç
  • collagen-vascular disease
    Äݶó°ÕÇ÷°üº´, ±³¿øÇ÷°üº´
´ëÇÑÀÇÇù Çʼö ÀÇÇпë¾îÁý »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • collagen
    ¾Æ±³Áú
  • helix
    1. ³ª¼±, 2. ±ÍµÑ·¹
¿¾ ´ëÇÑÀÇÇù ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • double helix
    ÀÌÁß³ª¼±
  • double stranded helix
    ÀÌÁß²ö³ª¼±
  • helix
    ³ª¼±, ±ÍµÑ·¹
  • triple helix
    »ïÁß³ª¼±
  • collagen band
    ¾Æ±³Áú¶ì
  • collagen
    ¾Æ±³Áú
  • collagen disease
    ¾Æ±³Áúº´
  • collagen fiber
    (¢¡collagenous fiber) ¾Æ±³¼¶À¯
  • collagen graft
    ¾Æ±³ÁúÀ̽Ä
  • collagen implant
    ¾Æ±³ÁúÀ̽Ä
  • collagen injection
    ¾Æ±³ÁúÁÖ»ç
  • collagen-vascular disease
    ¾Æ±³ÁúÇ÷°üº´, ±³¿øÇ÷°üº´
  • fibrillar collagen
    ¿ø¼¶À¯¾Æ±³Áú
  • necrobiotic collagen
    »ý±«»ç¾Æ±³Áú
  • diffuse collagen disease
    ±¤¹üÀ§¾Æ±³Áúº´, ¹Ì¸¸¾Æ±³Áúº´
¿¾ ´ëÇÑÀÇÇù 2 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 1 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Fibril, collagen or elastin
    ¿ø¼¶À¯(ê«àéë«), ±³¿øÁú(Îïê«òõ) ¶Ç´Â ź·Â¼Ò(÷¥ÕôáÈ)
¿¾ ´ëÇÑÀÇÇù 3 ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • double helix
    ½Ö³ª¼±(±¸Á¶), ÀÌÁß³ª¼±.
  • double helix
    ÀÌÁß³ª¼±(ì£ñìÕ¢àÁ), ½Ö³ª¼±
  • double helix, DNA model
  • double stranded helix
    ÀÌÁ߻質»ç¼±.
  • helix
    ³ª¼±, ÀÌ·û
  • helix
    ³ª¼±.À̺ñÀÌ·û(ì¼ëÌ).
  • helix
    ±ÍµÑ·¹
  • helix, double
    ÀÌÁß³ª¼±
  • larger muscle of helix
    ´ëÀÌ·û±Ù
  • larger muscle of helix<³ª> musculus helicis major
    ´ëÀÌ·û±Ù(ÓÞì¼ëÌÐÉ).
  • muscle of helix, larger
    ´ëÀÌ·û±Ù
  • smaller muscle of helix
    ÀÛÀº±ÍµÑ·¹±Ù, ¼ÒÀÌ·û±Ù.
  • triple helix
    »ïÁß³ª¼±(ß²ñìÑÞàÁ).
  • collagen
    ±³¿øÁú(Îïê«òõ), Äݶó°Õ.
  • collagen
    ÄݶóÁ¨
´ëÇÑÇØºÎÇÐȸ ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • Collagen fiber
    ¾Æ±³¼¶À¯
    [¿¾ ¿ë¾î] ±³¿ø¼¶À¯
  • Helix
    ±ÍµÑ·¹
    [¿¾ ¿ë¾î] ÀÌ·û
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  • ¿µ¹®
    ÇѱÛ
  • collagen helix
    ÄݶóÀü ³ª¼±(Õ¢àÁ)
´ëÇÑ»ýÈ­ÇкÐÀÚ»ý¹°ÇÐȸ ¿ë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • collagen
    ÄݶóÀü
  • double helix
    ÀÌÁß ³ª¼±(ì£ñìÕ¢àÊ) (ÔÒ) Watson-Crick model
  • helix
    ³ª¼±(Õ¢àÁ)
  • 310 helix
    310 ³ª¼±(Õ¢àÁ)
  • helix-breaking amino acid
    ³ª¼±(Õ¢àÁ) ±ú±â ¾Æ¹Ì³ë»ê(ß«)
  • helix-coil transition
    ³ª¼±(Õ¢àÁ)-ÄÚÀÏ ÃµÀÌ(ôÃì¹)
  • helix-destabilizing protein
    ³ª¼± ºÒ¾ÈÁ¤È­ ´Ü¹éÁú(Õ¢àÁÝÕäÌïÒûùÓ±ÛÜòõ)
  • helix nucleation
    ³ª¼± ÇÙÇü¼º(Õ¢àÁú·û¡à÷)
  • helix winding number
    ³ª¼±(Õ¢àÁ) °¨±â¼ö(â¦)
  • interwound helix
    »ó¼±(ßÓàÁ)³ª¼±(Õ¢àÁ)
  • n-fold helix
    n-¹è¼ö ³ª¼±(ÛÃâ¦Õ¢àÁ)
  • nonpalindromic helix
    ºñȸ¹®(ÞªüÞÚ¦) ³ª¼±(Õ¢àÁ)
  • palindromic helix
    ȸ¹®³ª¼±(üÞÙþÕ¢àÁ)
  • pi helix
    ÆÄÀÌ ³ª¼±(Õ£àÊ)
  • relaxed helix
    ÀÌ¿Ï ³ª¼±(ì¬èÐÕ¢àÁ)
KI ÀÇÇпë¾î »çÀü °Ë»ö À¯»ç °Ë»ö °á°ú : 2 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
  • collagen
    ±³¿øÁú, Äݶó°Õ
  • collagen disease
    ±³¿øÁúº´
KMLE ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
bHLH basic helix-loop-helix
bHLH-ZIP basic helix-loop-helix-leucine zipper
HLH helix-loop-helix; hemophagocytic lymphohistiocytosis
HD Haab-Dimmer [syndrome]; Hajna-Damon [broth]; Hansen disease; hearing distance; heart disease; helix ...
HPA Health Care Practice Act; Health Policy Agenda for the American People; health promotion advocates; ...
KMLE ÀÚµ¿ÃßÃâ ÀÇÇоà¾î »çÀü À¯»ç °Ë»ö °á°ú : 5 ÆäÀÌÁö: 1
HLH B)-helix-loop-helix
bHLH Basic Helix-Loop-Helix
bHLH Basic region helix-loop-helix
H-T-H helix-turn-helix
HhH Helix-hairpin-Helix
°æºÏ´ë Ä¡°ú´ëÇÐ ±¸°­³»°ú ±³½Ç »çÀü À¯»ç °Ë»ö °á°ú : 13 ÆäÀÌÁö: 1
  • ¿µ¹®
    ÇѱÛ
    ¼³¸í
  • double stranded helix
    ÀÌÁß»è ³ª»ç¼±
  • helix
    ³ª¼±, ÀÌ·û, ±Ó¹ÙÄû, ±ÍµÑ·¹
    1. ÀüÀÚ¼®ÀÇ ¼±·û °°Àº ³ª¼± ±¸Á¶. 2. ÀÌÀÍÀÇ »ó¹æ ¹× ºÎ¹æ ÀÚÀ¯¿¬.
  • spine of helix
    ±ÍµÑ·¹ µ¹±â
  • calcified collagen fiber
    ¼®È¸È­ ±³¿ø ¼¶À¯
  • collagen
    ±³¿øÁú
    ÇǺÎ, °ñ, Àδë, ¿¬°ñ, ´Ù¸¥ °áÇÕ Á¶Á÷¿¡ ÀÖ´Â Èò»öÀÇ ´Ü¹éÁú ¼ººÐÀÇ ¼¶À¯. ¸ð±³¿øÁú·Î ±¸¼ºµÇ¾î ÀÖ´Ù. À̰ÍÀº ²úÀ̸é Á©¶óƾÀ¸·Î º¯ÇÑ´Ù.
  • collagen bundle
    ±³¿ø¼¶À¯¼Ó
  • collagen disease
    ±³¿ø Áúȯ, ±³¿øÁú Áúȯ, ±³¿øº´, ±³¿øÁúº´
    µ¿ÀǾî=connective tissue disorders. º´¸®Á¶Á÷ÇÐÀûÀ¸·Î Ç÷°üÀÇ °áÇÕ Á¶Á÷¿¡ ÆØÈ­³ª ±«»ç µûÀ§ÀÇ º¯È­°¡ ¹ß°ßµÇ´Â ¸ðµç ÁúȯÀ» ÀϰýÇÏ¿©, ±×µéÀÇ »óÈ£°ü·ÃÀ» º¸±â À§ÇØ 1942³â ¹Ì±¹ÀÇ O. Ŭ·½Æä·¯ µî¿¡ ÀÇÇØ¼­ Á¦ÃâµÈ Áý¾à °³³ä.
  • collagen fiber
    ±³¿ø ¼¶À¯
  • collagen fiber web
    ±³¿ø ¼¶À¯ ±×¹°
  • collagen fibrils of cementum
    ¹é¾ÇÁúÀÇ ±³¿ø¿ø¼¶À¯
    ¹é¾ÇÁú Ç¥¸éÀ» °üÅëÇÏ¿©, Ä¡¾Æ ÁöÁö¿¡ ÇÊ¿äÇÑ Ä¡ÁÖ ¼¶À¯¿Í ¿¬¼ÓµÇ¾î ÀÖ´Â ¿ø¼¶À¯.
  • collagen-vascular disease
    ±³¿øÁú-Ç÷°ü¼º Áúȯ
  • microfibril of collagen
    ¾Æ±³ ¹Ì¼¼ ¿ø¼¶À¯
  • microfibrillar collagen
    ¹Ì¼¼ ¼¶À¯¼º ÄݶóÁ¨
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
helix loop helix <molecular biology> A motif associated with transcription factors, allowing them to recognise and bind to specific DNA sequences. Two _ helices are separated by a loop.
Examples: myoblast MyoD1, c myc, Drosophila genes daughterless, hairy, twist, scute, achaete, asense. Not the same as helix turn helix.
(18 Nov 1997)
helix-loop-helix motifs A group of 20-residue peptides characterised by two alpha helices separated by a non-helical segment. These recurring supersecondary structural patterns are found in many sequence-specific DNA-binding proteins.
(12 Dec 1998)
helix turn helix <molecular biology> A motif associated with transcription factors, allowing them to bind to and recognise specific DNA sequences. Two amphipathic _ helices are separated by a short sequence with a _ sheet. One helix lies across the major groove of the DNA, while the recognition helix enters the major groove and interacts with specific bases. An example in Drosophila is the homeotic gene fushi tarazu, that binds to the sequence TCAATTAAATGA. Not the same as helix loop helix.
(18 Nov 1997)
helix-turn-helix motifs The first DNA-binding protein motif to be recognised. Helix-turn-helix motifs were originally identified in bacterial proteins but have since been found in hundreds of DNA-binding proteins from both eukaryotes and prokaryotes. They are constructed from two alpha helices connected by a short extended chain of amino acids, which constitute the "turn." the two helices are held at a fixed angle, primarily through interactions between the two helices.
(12 Dec 1998)
Mallory's collagen stain <technique> One of a number of staining methods using phosphomolybdic or phosphotungstic acid with an acid stain, such as aniline blue, or with haematoxylin for connective tissue staining.
(05 Mar 2000)
collagen <protein> The protein substance of the white fibres (collagenous fibres) of skin, tendon, bone, cartilage and all other connective tissue, composed of molecules of tropocollagen, it is converted into gelatin by boiling. Collagenous pertaining to collagen, forming or producing collagen.
Origin: Gr. Kolla = glue, gennan = to produce
(18 Nov 1997)
collagen diseases Historically, a heterogeneous group of acute and chronic diseases, including rheumatoid arthritis, systemic lupus erythematosus, progressive systemic sclerosis, dermatomyositis, etc. This classification was based on the notion that "collagen" was equivalent to "connective tissue", but with the present recognition of the different types of collagen and the aggregates derived from them as distinct entities, the term "collagen diseases" now pertains exclusively to those inherited conditions in which the primary defect is at the gene level and affects collagen biosynthesis, post-translational modification, or extracellular processing directly.
(12 Dec 1998)
collagen fibre An individual fibre that varies in diameter from less than 1 um to about 12 um and is composed of fibrils; the fibre's, which are usually arranged in bundles, undergo some branching and are of indefinite length; chemically the fibre is a glycoprotein, collagen, which yields gelatin upon boiling; they make up the principal element of irregular connective tissue, tendons, aponeuroses, and most ligaments, and occur in the matrix of cartilage and osseous tissue.
Synonym: white fibre.
(05 Mar 2000)
collagen fibrils The fibril's that comprise a collagen fibre, ranging from 20 to 200 nm and averaging about 100 nm in diameter (substantially larger in tendons), with cross-striations averaging 64 nm.
Synonym: collagen fibrils.
(05 Mar 2000)
collagen injection Correction of superficial soft tissue deformities, acne scars, or age-related skin changes by injection (implantation) of collagen; bovine collagen preparations are commonly used. Prior intradermal testing is necessary to exclude hypersensitivity.
(05 Mar 2000)
collagen telopeptidase <enzyme> Neutral metalloproteinase from porcine gingiva; removes the extra-helical extension peptides proximal to the lysyl residue at position 17
Registry number: EC 3.4.24.-
Synonym: collagen depolymerase
(26 Jun 1999)
collagen-vascular diseases A group of generalised disease's affecting connective tissue and frequently characterised by fibrinoid necrosis or vasculitis; in some collagen disease's, auto-immunization, particularly antinuclear antibodies, has been shown and circulating immune complexes are found. The term is not entirely acceptable because there is no evidence that collagen is primarily involved; "collagen" was once synonymous with "connective tissue" rather than describing a specific fibrinous protein in that tissue.
See: connective-tissue diseases.
(05 Mar 2000)
SLS collagen <protein> Abnormal packing pattern of collagen molecules formed if ATP is added to acidic collagen solutions, in which lateral aggregates of molecules are produced.
Each aggregate is 300 nm long and the molecules are all in register. If SLS aggregates are overlapped with a quarter stagger, the 67 nm banding pattern of normal fibrils is reconstituted.
(19 Jan 1998)
type I collagen The most abundant collagen, which forms large well-organised fibrils having high tensile strength.
(05 Mar 2000)
type II collagen Collagen unique to cartilage, nucleus pulposis, notochord, and vitreous body; it forms as thin highly glycosylated fibrils.
(05 Mar 2000)
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  • ¿µ¹®
    ÇѱÛ
  • collagen
    ±³¿øÁú
  • double helix
    (»ýÈ­)(¿°»öüÀÇ DNAºÐÀÚ ³»ÀÇ)ÀÌÁß ³ª¼±(±¸Á¶)
  • helix
    ³ª¼±;¼Ò¿ëµ¹ÀÌ;¼Ò¿ëµ¹ÀÌ Àå½Ä;±Ó¹ÙÄû !
ÀÌ ¾Æ·¡ ºÎÅÍ´Â °á°ú°¡ ¾ø½À´Ï´Ù.
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  • Á¦Ç°¸í
    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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    ¼ººÐ/ÇÔ·®
    ±¸ºÐ/º¸Çè±Þ¿©
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    ÇѱÛ
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    ÇѱÛ
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MeSH(Medical Subject Headings) À¯»ç °Ë»ö (http://www.nlm.nih.gov) °á°ú : 0 ÆäÀÌÁö: 1
¿ÜºÎ ¸µÅ© - Merriam-Webster's ÀÇÇлçÀü ¸ÂÃã °Ë»ö (https://www.merriam-webster.com) °á°ú: 0 ÆäÀÌÁö: 1
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