関: lamin type A

WordNet

the 1st letter of the Roman alphabet (同)a
the blood group whose red cells carry the A antigen (同)type_A, group A

PrepTutorEJDIC

answer / ampere
…‘を'打つ,たたく,なぐる / 打つ,たたく,なぐる
すばやくずらかる
arsenicの化学記号

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/02/08 16:11:09」(JST)

wiki en

Lamin A/C also known as LMNA is a protein that in humans is encoded by the LMNA gene.^[1]^[2] Lamin A/C belongs to the lamin family of proteins.

Function

Biogenesis of lamin A in normal cells and the failure to generate mature lamin A in Hutchinson-Gilford progeria syndrome.

In the setting of ZMPSTE24 deficiency, the final step of lamin processing does not occur, resulting in an accumulation of farnesyl-prelamin A. In Hutchinson-Gilford progeria syndrome, a 50-amino acid deletion in prelamin A (amino acids 607–656) removes the site for the second endoproteolytic cleavage. Consequently, no mature lamin A is formed, and a farnesylated mutant prelamin A (progerin) accumulates in cells.^[3] The nuclear lamina consist of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. Vertebrate lamins consist of two types, A and B. Through alternate splicing, this gene encodes three type A lamin isoforms.^[4]

Early in mitosis, maturation promoting factor (abbreviated MPF, also called mitosis-promoting factor or M-phase-promoting factor) phosphorylates specific serine residues in all three nuclear lamins, causing depolymerization of the lamin intermediate filaments. The phosphorylated lamin B dimers remain associated with the nuclear membrane via their isoprenyl anchor. Lamin A is targeted to the nuclear membrane by an isoprenyl group but it is cleaved shortly after arriving at the membrane. It stays associated with the membrane through protein-protein interactions of itself and other membrane associated proteins, such as LAP1. Depolymerization of the nuclear lamins leads to disintegration of the nuclear envelope. Transfection experiments demonstrate that phosphorylation of human lamin A is required for lamin depolymerization, and thus for disassembly of the nuclear envelope, which normally occurs early in mitosis.

Clinical significance

Wild type (left) and mutated (right) form of lamin A (LMNA, PDB: 1IFR). Normally, arginine 527 (blue) forms salt bridge with glutamate 537 (magenta), but R527L substitution results in braking this interaction (leucine is too short to reach glutamate). Models are presented in surface (upper) and in cartoon representation (down).^[5]

Mutations in the LMNA gene are associated with several diseases, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, restrictive dermopathy and Hutchinson-Gilford progeria syndrome. A truncated version of lamin A, commonly known as progerin, causes Hutchinson-Gilford progeria syndrome.^[6]^[7] To date over 1,400 SNPs are known [3]. They can manifest in changes on mRNA, splicing or protein (e.g. Arg471Cys,^[8] Arg482Gln,^[9] Arg527Leu,^[10] Arg527Cys,^[11] Ala529Val ^[12] ) level.

Interactions

LMNA has been shown to interact with:

ALOX12^[13]
EMD^[14]^[15]^[16]^[17]
NARF^[18]
SREBF1^[19]
TMPO^[20]^[21]
ZNF239^[22]
SIRT1^[23]

References

^ Kamat AK, Rocchi M, Smith DI, Miller OJ (March 1993). "Lamin A/C gene and a related sequence map to human chromosomes 1q12.1-q23 and 10". Somat. Cell Mol. Genet. 19 (2): 203–8. doi:10.1007/BF01233534. PMID 8511676.
^ Wydner KL, McNeil JA, Lin F, Worman HJ, Lawrence JB (March 1996). "Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization". Genomics 32 (3): 474–8. doi:10.1006/geno.1996.0146. PMID 8838815.
^ Coutinho HD, Falcão-Silva VS, Gonçalves GF, da Nóbrega RB (2009). "Molecular ageing in progeroid syndromes: Hutchinson-Gilford progeria syndrome as a model". Immun Ageing 6: 4. doi:10.1186/1742-4933-6-4. PMC 2674425. PMID 19379495.
^ "Entrez Gene: LMNA lamin A/C".
^ Al-Haggar M, Madej-Pilarczyk A, Kozlowski L, Bujnicki JM, Yahia S, Abdel-Hadi D, Shams A, Ahmad N, Hamed S, Puzianowska-Kuznicka M (2012). "A novel homozygous p.Arg527Leu LMNA mutation in two unrelated Egyptian families causes overlapping mandibuloacral dysplasia and progeria syndrome". Eur J Hum Genet. 20 (11): 1134–40. doi:10.1038/ejhg.2012.77. PMC 3476705. PMID 22549407.
^ Capell BC, Collins FS (December 2006). "Human laminopathies: nuclei gone genetically awry". Nat. Rev. Genet. 7 (12): 940–52. doi:10.1038/nrg1906. PMID 17139325.
^ Rankin J, Ellard S (October 2006). "The laminopathies: a clinical review". Clin. Genet. 70 (4): 261–74. doi:10.1111/j.1399-0004.2006.00677.x. PMID 16965317.
^ Zirn B, Kress W, Grimm T, Berthold LD, Neubauer B, Kuchelmeister K, Müller U, Hahn A (2008). "Association of homozygous LMNA mutation R471C with new phenotype: mandibuloacral dysplasia, progeria, and rigid spine muscular dystrophy". Am J Med Genet A 146A (8): 1049–1054. doi:10.1002/ajmg.a.32259. PMID 18348272.
^ Cao H, Hegele RA (2002). "Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy". Hum. Molec. Genet. 9 (1): 109–12. doi:10.1093/hmg/9.1.109. PMID 10587585.
^ Al-Haggar M, Madej-Pilarczyk A, Kozlowski L, Bujnicki JM, Yahia S, Abdel-Hadi D, Shams A, Ahmad N, Hamed S, Puzianowska-Kuznicka M (2012). "A novel homozygous p.Arg527Leu LMNA mutation in two unrelated Egyptian families causes overlapping mandibuloacral dysplasia and progeria syndrome". Eur J Hum Genet. 20 (11): 1134–40. doi:10.1038/ejhg.2012.77. PMC 3476705. PMID 22549407.
^ Agarwal AK, Kazachkova I, Ten S, Garg A (2008). "Severe mandibuloacral dysplasia-associated lipodystrophy and progeria in a young girl with a novel homozygous Arg527Cys LMNA mutation". J Clin Endocrinol Metab 93 (12): 4617–4623. doi:10.1210/jc.2008-0123. PMC 2626450. PMID 18796515.
^ Garg A, Cogulu O, Ozkinay F, Onay H, Agarwal AK (2005). "A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia". J. Clin. Endocrinol. Metab. 90 (9): 5259–64. doi:10.1210/jc.2004-2560. PMID 15998779.
^ Tang K, Finley RL, Nie D, Honn KV (March 2000). "Identification of 12-lipoxygenase interaction with cellular proteins by yeast two-hybrid screening". Biochemistry 39 (12): 3185–91. doi:10.1021/bi992664v. PMID 10727209.
^ Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I, Stamm S, Wilson KL, Morris GE (June 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". Eur. J. Biochem. 270 (11): 2459–66. doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701.
^ Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L, Squarzoni S, Maraldi NM (April 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochem. Biophys. Res. Commun. 303 (3): 764–70. doi:10.1016/S0006-291X(03)00415-7. PMID 12670476.
^ Sakaki M, Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K, Ishiura S (February 2001). "Interaction between emerin and nuclear lamins". J. Biochem. 129 (2): 321–7. doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.
^ Clements L, Manilal S, Love DR, Morris GE (January 2000). "Direct interaction between emerin and lamin A". Biochem. Biophys. Res. Commun. 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. PMID 10673356.
^ Barton RM, Worman HJ (October 1999). "Prenylated prelamin A interacts with Narf, a novel nuclear protein". J. Biol. Chem. 274 (42): 30008–18. doi:10.1074/jbc.274.42.30008. PMID 10514485.
^ Lloyd DJ, Trembath RC, Shackleton S (April 2002). "A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies". Hum. Mol. Genet. 11 (7): 769–77. doi:10.1093/hmg/11.7.769. PMID 11929849.
^ Markiewicz E, Dechat T, Foisner R, Quinlan RA, Hutchison CJ (December 2002). "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein". Mol. Biol. Cell 13 (12): 4401–13. doi:10.1091/mbc.E02-07-0450. PMC 138642. PMID 12475961.
^ Dechat T, Korbei B, Vaughan OA, Vlcek S, Hutchison CJ, Foisner R (October 2000). "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins". J. Cell. Sci. 113 (19): 3473–84. PMID 10984438.
^ Dreuillet C, Tillit J, Kress M, Ernoult-Lange M (November 2002). "In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C". Nucleic Acids Res. 30 (21): 4634–42. doi:10.1093/nar/gkf587. PMC 135794. PMID 12409453.
^ Liu B, Ghosh S, Yang X, Zheng H, Liu X, Wang Z, Jin G, Zheng B, Kennedy BK, Suh Y, Kaeberlein M, Tryggvason K, Zhou Z (2012). "Resveratrol Rescues SIRT1-Dependent Adult Stem Cell Decline and Alleviates Progeroid Features in Laminopathy-Based Progeria". Cell Metabolism 16 (6): 738–750. doi:10.1016/j.cmet.2012.11.007. PMID 23217256.

External links

Online 'Mendelian Inheritance in Man' (OMIM) Cardiomyopathy, Dilated, 1A; CMD1A -115200
Online 'Mendelian Inheritance in Man' (OMIM) LAMIN A/C; LMNA -150330
LMNA protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
LOVD mutation database: LMNA
GeneCards for LMNA

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 拡張型心筋症の遺伝学 genetics of dilated cardiomyopathy
2. エメリー‐ドレフェス型筋ジストロフィー emery dreifuss muscular dystrophy
3. 脂肪異栄養症症候群 lipodystrophic syndromes
4. 心疾患関連する遺伝性症候群 inherited syndromes associated with cardiac disease
5. 肢帯型筋ジストロフィー limb girdle muscular dystrophy

English Journal

Bilateral stenosis of carotid siphon in Hutchinson-Gilford progeria syndrome.

Narazaki R, Makimura M, Sanefuji M, Fukamachi S, Akiyoshi H, So H, Yamamura K, Doisaki S, Kojima S, Ihara K, Hara T, Ohga S.SourceDivision of Pediatrics, Tagawa Municipal Hospital, Fukuoka, Japan; Department of Pediatrics, Graduate School of Medical Sciences, Kyushu University, Fukuoka, Japan.
Brain & development.Brain Dev.2013 Aug;35(7):690-3. doi: 10.1016/j.braindev.2012.10.008. Epub 2012 Nov 8.
Hutchinson-Gilford progeria syndrome (HGPS) is a rare premature aging disease, caused by a de novo mutation of lamin-A gene, LMNA G608G. Accumulation of abnormal lamin-A (progerin) compromises nuclear membrane integrity and results in the accelerated senescence. Affected patients show a typical feat
PMID 23141186

Human Ng2+ adipose stem cells loaded in vivo on a new crosslinked hyaluronic acid-Lys scaffold fabricate a skeletal muscle tissue.

Desiderio V, De Francesco F, Schiraldi C, De Rosa A, La Gatta A, Paino F, d'Aquino R, Ferraro GA, Tirino V, Papaccio G.SourceDipartimento di Medicina Sperimentale, Sezione di Istologia ed Embriologia Medica, Tissue Engineering and Regenerative (TERM), Seconda Università degli Studi di Napoli, Napoli, Italy.
Journal of cellular physiology.J Cell Physiol.2013 Aug;228(8):1762-73. doi: 10.1002/jcp.24336.
Mesenchymal stem cell (MSC) therapy holds promise for treating diseases and tissue repair. Regeneration of skeletal muscle tissue that is lost during pathological muscle degeneration or after injuries is sustained by the production of new myofibers. Human Adipose stem cells (ASCs) have been reported
PMID 23359523

Japanese Journal

A new c.1621 C>G, p.R541G lamin A/C mutation in a family with DCM and regional wall motion abnormalities (akinesis/dyskinesis): genotype-phenotype correlation

Malek Lukasz A.,Labib Sarah,Mazurkiewicz Lukasz [他]
Journal of human genetics 56(1), 83-86, 2011-01
NAID 40017436400

2．家族性ペースメーカー植込み症例における遺伝的背景の検討 : ―心臓Na+チャネル病，Lamin A/C遺伝子関連心筋症―

牧山武,静田聡,赤尾昌治,木村剛,堀江稔
心電図 30(3), 200-208, 2010
… 子解析の結果，33例中17例（51.5％）に心臓Na+チャネル遺伝子（SCN5A），またはLamin A/C遺伝子（LMNA）異常を同定した〔SCN5A異常8/33例（24.2％），LMNA異常9/33例（27.2％）〕．SCN5A異常を検出した8例中5例には，ほかの心臓Na+チャネル病の合併（Brugada症候群4例，QT延長症候群1例）を認めた．一方，LMNAは核膜の裏打ち蛋白であるLamin A，Cをコードし，その遺伝子異常により拡張型心筋症，心臓伝導障害，致死 …
NAID 130000432005

Related Pictures

★リンクテーブル★

リンク元	「カスパーゼ」「ラミンA」
関連記事	「A」「Ad」

「カスパーゼ」

Lamin A/C
	PDB rendering based on 1ifr.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1IFR, 1IVT, 1X8Y, 2XV5, 2YPT, 3GEF, 3V4Q, 3V4W, 3V5B
Identifiers
Symbols	LMNA ; CDCD1; CDDC; CMD1A; CMT2B1; EMD2; FPL; FPLD; FPLD2; HGPS; IDC; LDP1; LFP; LGMD1B; LMN1; LMNC; LMNL1; PRO1
External IDs	OMIM: 150330 MGI: 96794 HomoloGene: 41321 ChEMBL: 1293235 GeneCards: LMNA Gene
Gene ontology
Molecular function	• structural molecule activity; • protein binding;
Cellular component	• nucleus; • nuclear envelope; • lamin filament; • nuclear lamina; • nucleoplasm; • cytoplasm; • cytosol; • intermediate filament; • nuclear matrix; • nuclear speck; • nuclear membrane; • perinuclear region of cytoplasm;
Biological process	• mitotic cell cycle; • apoptotic process; • cellular component disassembly involved in execution phase of apoptosis; • mitotic nuclear envelope disassembly; • mitotic nuclear envelope reassembly; • spermatogenesis; • muscle organ development; • programmed cell death; • regulation of cell migration; • establishment or maintenance of microtubule cytoskeleton polarity; • endoplasmic reticulum unfolded protein response; • protein localization to nucleus; • sterol regulatory element binding protein import into nucleus; • IRE1-mediated unfolded protein response; • cellular protein metabolic process; • ventricular cardiac muscle cell development; • cellular response to hypoxia; • negative regulation of release of cytochrome c from mitochondria; • positive regulation of cell aging; • regulation of protein localization to nucleus; • negative regulation of extrinsic apoptotic signaling pathway;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;

　　[★]

英: caspase
同: ICEファミリープロテアーゼ ICE family protease

ヒトICEプロテアーゼスーパーファミリー

Family	Caspase	Other Name	Recognition	Target (Truncation site)
caspase-1	caspase-1	ICE	WEHD	pro IL-1β (FEAD/G, YVHD/A), procaspase-3, procaspase-4
	caspase-4	ICErel-II, TX, ICH-2
	caspase-5	ICErel-III, TY
caspase-2	caspase-2	ICH-1	DEHD	PARP (DEVD/G)
caspase-2	caspase-9	ICE-LAP6, Mch6	LEHD	PARP, procaspase-3
caspase-3	caspase-3	CPP32, Yama	DEVD	PARP, SREBP (DEPD/S), U1snRNP (DGPD/G), lamin B, D4-GDI (DELD/S), DNA-PK (DEVD/N), DFF (DETD/S, DAVD/T), actin (ELPD/G) ?, PKCδ (DMQD/N) ?]]
	caspase-7	Mch3, ICE-LAP3, CMH-1	DEVD	PARP, procaspase-6
	caspase-6	Mch2	VEHD	lamin A (VEID/N)]]
	caspase-8	FLICE, MACH, Mch5	LETD	procaspase-3, Bid
	caspase-10	Mch4	LEXD
	caspase-11	Ich3

「ラミンA」

　　[★]

英: lamin A、lamin type A

「A」

　　[★]

「Ad」

　　[★]

アデノウイルス

関: adenoviral、adenovirus

[pmid8511676-1] Kamat AK, Rocchi M, Smith DI, Miller OJ (March 1993). "Lamin A/C gene and a related sequence map to human chromosomes 1q12.1-q23 and 10". Somat. Cell Mol. Genet. 19 (2): 203–8. doi:10.1007/BF01233534. PMID 8511676.

[pmid8838815-2] Wydner KL, McNeil JA, Lin F, Worman HJ, Lawrence JB (March 1996). "Chromosomal assignment of human nuclear envelope protein genes LMNA, LMNB1, and LBR by fluorescence in situ hybridization". Genomics 32 (3): 474–8. doi:10.1006/geno.1996.0146. PMID 8838815.

[pmid19379495-3] Coutinho HD, Falcão-Silva VS, Gonçalves GF, da Nóbrega RB (2009). "Molecular ageing in progeroid syndromes: Hutchinson-Gilford progeria syndrome as a model". Immun Ageing 6: 4. doi:10.1186/1742-4933-6-4. PMC 2674425. PMID 19379495.

[4] "Entrez Gene: LMNA lamin A/C".

[5] Al-Haggar M, Madej-Pilarczyk A, Kozlowski L, Bujnicki JM, Yahia S, Abdel-Hadi D, Shams A, Ahmad N, Hamed S, Puzianowska-Kuznicka M (2012). "A novel homozygous p.Arg527Leu LMNA mutation in two unrelated Egyptian families causes overlapping mandibuloacral dysplasia and progeria syndrome". Eur J Hum Genet. 20 (11): 1134–40. doi:10.1038/ejhg.2012.77. PMC 3476705. PMID 22549407.

[pmid17139325-6] Capell BC, Collins FS (December 2006). "Human laminopathies: nuclei gone genetically awry". Nat. Rev. Genet. 7 (12): 940–52. doi:10.1038/nrg1906. PMID 17139325.

[pmid16965317-7] Rankin J, Ellard S (October 2006). "The laminopathies: a clinical review". Clin. Genet. 70 (4): 261–74. doi:10.1111/j.1399-0004.2006.00677.x. PMID 16965317.

[8] Zirn B, Kress W, Grimm T, Berthold LD, Neubauer B, Kuchelmeister K, Müller U, Hahn A (2008). "Association of homozygous LMNA mutation R471C with new phenotype: mandibuloacral dysplasia, progeria, and rigid spine muscular dystrophy". Am J Med Genet A 146A (8): 1049–1054. doi:10.1002/ajmg.a.32259. PMID 18348272.

[9] Cao H, Hegele RA (2002). "Nuclear lamin A/C R482Q mutation in Canadian kindreds with Dunnigan-type familial partial lipodystrophy". Hum. Molec. Genet. 9 (1): 109–12. doi:10.1093/hmg/9.1.109. PMID 10587585.

[10] Al-Haggar M, Madej-Pilarczyk A, Kozlowski L, Bujnicki JM, Yahia S, Abdel-Hadi D, Shams A, Ahmad N, Hamed S, Puzianowska-Kuznicka M (2012). "A novel homozygous p.Arg527Leu LMNA mutation in two unrelated Egyptian families causes overlapping mandibuloacral dysplasia and progeria syndrome". Eur J Hum Genet. 20 (11): 1134–40. doi:10.1038/ejhg.2012.77. PMC 3476705. PMID 22549407.

[11] Agarwal AK, Kazachkova I, Ten S, Garg A (2008). "Severe mandibuloacral dysplasia-associated lipodystrophy and progeria in a young girl with a novel homozygous Arg527Cys LMNA mutation". J Clin Endocrinol Metab 93 (12): 4617–4623. doi:10.1210/jc.2008-0123. PMC 2626450. PMID 18796515.

[12] Garg A, Cogulu O, Ozkinay F, Onay H, Agarwal AK (2005). "A novel homozygous Ala529Val LMNA mutation in Turkish patients with mandibuloacral dysplasia". J. Clin. Endocrinol. Metab. 90 (9): 5259–64. doi:10.1210/jc.2004-2560. PMID 15998779.

[pmid10727209-13] Tang K, Finley RL, Nie D, Honn KV (March 2000). "Identification of 12-lipoxygenase interaction with cellular proteins by yeast two-hybrid screening". Biochemistry 39 (12): 3185–91. doi:10.1021/bi992664v. PMID 10727209.

[pmid12755701-14] Wilkinson FL, Holaska JM, Zhang Z, Sharma A, Manilal S, Holt I, Stamm S, Wilson KL, Morris GE (June 2003). "Emerin interacts in vitro with the splicing-associated factor, YT521-B". Eur. J. Biochem. 270 (11): 2459–66. doi:10.1046/j.1432-1033.2003.03617.x. PMID 12755701.

[pmid12670476-15] Lattanzi G, Cenni V, Marmiroli S, Capanni C, Mattioli E, Merlini L, Squarzoni S, Maraldi NM (April 2003). "Association of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblasts". Biochem. Biophys. Res. Commun. 303 (3): 764–70. doi:10.1016/S0006-291X(03)00415-7. PMID 12670476.

[pmid11173535-16] Sakaki M, Koike H, Takahashi N, Sasagawa N, Tomioka S, Arahata K, Ishiura S (February 2001). "Interaction between emerin and nuclear lamins". J. Biochem. 129 (2): 321–7. doi:10.1093/oxfordjournals.jbchem.a002860. PMID 11173535.

[pmid10673356-17] Clements L, Manilal S, Love DR, Morris GE (January 2000). "Direct interaction between emerin and lamin A". Biochem. Biophys. Res. Commun. 267 (3): 709–14. doi:10.1006/bbrc.1999.2023. PMID 10673356.

[pmid10514485-18] Barton RM, Worman HJ (October 1999). "Prenylated prelamin A interacts with Narf, a novel nuclear protein". J. Biol. Chem. 274 (42): 30008–18. doi:10.1074/jbc.274.42.30008. PMID 10514485.

[pmid11929849-19] Lloyd DJ, Trembath RC, Shackleton S (April 2002). "A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies". Hum. Mol. Genet. 11 (7): 769–77. doi:10.1093/hmg/11.7.769. PMID 11929849.

[pmid12475961-20] Markiewicz E, Dechat T, Foisner R, Quinlan RA, Hutchison CJ (December 2002). "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein". Mol. Biol. Cell 13 (12): 4401–13. doi:10.1091/mbc.E02-07-0450. PMC 138642. PMID 12475961.

[pmid10984438-21] Dechat T, Korbei B, Vaughan OA, Vlcek S, Hutchison CJ, Foisner R (October 2000). "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins". J. Cell. Sci. 113 (19): 3473–84. PMID 10984438.

[pmid12409453-22] Dreuillet C, Tillit J, Kress M, Ernoult-Lange M (November 2002). "In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C". Nucleic Acids Res. 30 (21): 4634–42. doi:10.1093/nar/gkf587. PMC 135794. PMID 12409453.

[pmid23217256-23] Liu B, Ghosh S, Yang X, Zheng H, Liu X, Wang Z, Jin G, Zheng B, Kennedy BK, Suh Y, Kaeberlein M, Tryggvason K, Zhou Z (2012). "Resveratrol Rescues SIRT1-Dependent Adult Stem Cell Decline and Alleviates Progeroid Features in Laminopathy-Based Progeria". Cell Metabolism 16 (6): 738–750. doi:10.1016/j.cmet.2012.11.007. PMID 23217256.

匿名

検索

案内

案内

lamin A