vimentin

Vimentin
	PDB rendering based on 1gk4.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1GK4, 1GK6, 1GK7, 3G1E, 3KLT, 3S4R, 3SSU, 3SWK, 3TRT, 3UF1, 4MCY, 4MCZ, 4MD0, 4MD5, 4MDI, 4MDJ
Identifiers
Symbols	VIM ; CTRCT30; HEL113
External IDs	OMIM: 193060 MGI: 98932 HomoloGene: 2538 GeneCards: VIM Gene
Gene ontology
Molecular function	• glycoprotein binding; • double-stranded RNA binding; • structural constituent of cytoskeleton; • structural constituent of eye lens; • protein binding; • protein C-terminus binding; • identical protein binding; • scaffold protein binding; • keratin filament binding;
Cellular component	• cytoplasm; • peroxisome; • cytosol; • cytoskeleton; • intermediate filament; • plasma membrane; • focal adhesion; • cell leading edge; • neuron projection; • intermediate filament cytoskeleton; • extracellular exosome;
Biological process	• apoptotic process; • cellular component disassembly involved in execution phase of apoptosis; • movement of cell or subcellular component; • positive regulation of gene expression; • negative regulation of neuron projection development; • programmed cell death; • astrocyte development; • viral process; • muscle filament sliding; • intermediate filament organization; • Bergmann glial cell differentiation; • SMAD protein signal transduction; • lens fiber cell development;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	v; t; e;

ビメンチン

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/07/23 14:18:45」(JST)

wiki en

[Wiki en表示]

Immunofluorescence staining pattern of vimentin antibodies. Produced by incubating vimentin primary antibodies and FITC labelled secondary antibodies with HEp-20-10 cells.

Vimentin is a protein that in humans is encoded by the VIM gene.

Vimentin is a type III intermediate filament (IF) protein that is expressed in mesenchymal cells. IF proteins are found in all metazoan cells^[1] as well as bacteria.^[2] IF, along with tubulin-based microtubules and actin-based microfilaments, comprise the cytoskeleton. All IF proteins are expressed in a highly developmentally-regulated fashion; vimentin is the major cytoskeletal component of mesenchymal cells. Because of this, vimentin is often used as a marker of mesenchymally-derived cells or cells undergoing an epithelial-to-mesenchymal transition (EMT) during both normal development and metastatic progression.

Structure

A vimentin monomer, like all other intermediate filaments, has a central α-helical domain, capped on each end by non-helical amino (head) and carboxyl (tail) domains.^[3] Two monomers are likely co-translationally expressed in a way that facilitates their formation of a coiled-coil dimer, which is the basic subunit of vimentin assembly.^[4]

The α-helical sequences contain a pattern of hydrophobic amino acids that contribute to forming a "hydrophobic seal" on the surface of the helix.^[3] In addition, there is a periodic distribution of acidic and basic amino acids that seems to play an important role in stabilizing coiled-coil dimers.^[3] The spacing of the charged residues is optimal for ionic salt bridges, which allows for the stabilization of the α-helix structure. While this type of stabilization is intuitive for intrachain interactions, rather than interchain interactions, scientists have proposed that perhaps the switch from intrachain salt bridges formed by acidic and basic residues to the interchain ionic associations contributes to the assembly of the filament.^[3]

Function

Vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally.^[5]

The dynamic nature of vimentin is important when offering flexibility to the cell. Scientists found that vimentin provided cells with a resilience absent from the microtubule or actin filament networks, when under mechanical stress in vivo. Therefore, in general, it is accepted that vimentin is the cytoskeletal component responsible for maintaining cell integrity. (It was found that cells without vimentin are extremely delicate when disturbed with a micropuncture).^[6] Transgenic mice that lack vimentin appeared normal and did not show functional differences.^[7] It is possible that the microtubule network may have compensated for the absence of the intermediate network. This result supports an intimate interactions between microtubules and vimentin. Moreover, when microtubule depolymerizers were present, vimentin reorganization occurred, once again implying a relationship between the two systems.^[6] On the other hand, wounded mice that lack the vimentin gene heal slower than their wild type counterparts. ^[8]

In essence, vimentin is responsible for maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. Vimentin has been shown to eliminate toxic proteins in JUNQ and IPOD inclusion bodies in asymmetric division of mammalian cell lines.^[9]

Also, vimentin is found to control the transport of low-density lipoprotein, LDL, -derived cholesterol from a lysosome to the site of esterification.^[10] With the blocking of transport of LDL-derived cholesterol inside the cell, cells were found to store a much lower percentage of the lipoprotein than normal cells with vimentin. This dependence seems to be the first process of a biochemical function in any cell that depends on a cellular intermediate filament network. This type of dependence has ramifications on the adrenal cells, which rely on cholesteryl esters derived from LDL.^[10]

Clinical significance

It has been used as a sarcoma tumor marker to identify mesenchyme.^[11]^[12]

Methylation of the vimentin gene has been established as a biomarker of colon cancer and this is being utilized in the development of fecal tests for colon cancer. Statistically significant levels of vimentin gene methylation have also been observed in certain upper gastrointestinal pathologies such as Barrett's esophagus, esophageal adenocarcinoma, and intestinal type gastric cancer.^[13] High levels of DNA methylation in the promotor region have also been associated with markedly decreased survival in hormone positive breast cancers.^[14]

See also Anti-citrullinated protein antibody for its use in diagnosis of rheumatoid arthritis.

Interactions

Vimentin has been shown to interact with:

DSP ^[15]
MEN1 ^[16]
MYST2 ^[17]^[18]
PLEC ^[19]^[20]
PKN1 ^[21]
SPTAN1 ^[20]
UPP1 ^[22]
YWHAZ ^[23]

The 3' UTR of Vimentin mRNA has been found to bind a 46kDa protein.^[24]

References

^ Eriksson JE, Dechat T, Grin B, Helfand B, Mendez M, Pallari HM, Goldman RD (2009). "Introducing intermediate filaments: from discovery to disease". J Clin Invest 119 (7): 1763–71. doi:10.1172/JCI38339. PMC 2701876. PMID 19587451.
^ Cabeen MT, Jacobs-Wagner C (2010). "The bacterial cytoskeleton". Annu Rev Genet 44: 365–92. doi:10.1146/annurev-genet-102108-134845. PMID 21047262.
^ ^a ^b ^c ^d Fuchs E., Weber K. (1994). "Intermediate filaments: structure, dynamics, function, and disease". Annu Rev Biochem 63: pp. 345–82. doi:10.1146/annurev.bi.63.070194.002021. PMID 7979242.
^ Chang L, Shav-Tal Y, Trcek T, Singer RH, Goldman RD. (2006). "Assembling an intermediate filament network by dynamic cotranslation". J Cell Biol 172 (5): 747–58. doi:10.1083/jcb.200511033. PMC 2063706. PMID 16505169.
^ Katsumoto T., Mitsushima A., Kurimura T. (1990). "The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction". Biol Cell 68 (2): pp. 139–46. doi:10.1016/0248-4900(90)90299-I. PMID 2192768.
^ ^a ^b Goldman RD, Khuon S, Chou YH, Opal P, Steinert PM (August 1996). "The function of intermediate filaments in cell shape and cytoskeletal integrity". J. Cell Biol. 134 (4): 971–83. doi:10.1083/jcb.134.4.971. PMC 2120965. PMID 8769421.
^ Golucci-Guyon E, Portier M-M, Dunia I, Paulin D, Pournin S, Babinet C (1994). "Mice lacking vimentin develop and reproduce without an obvious phenotype.". Cell 79 (4): 679–94. doi:10.1016/0092-8674(94)90553-3. PMID 7954832.
^ Eckes B, Colucci-Guyon E, Smola H, Nodder S, Babinet C, Krieg T, Martin P (2000). "Impaired wound healing in embryonic and adult mice lacking vimentin.". Journal of cell science 113: 2455––62. PMID 10852824.
^ Ogrodnik M, Salmonowicz H, Brown R, Turkowska J, Sredniawa W, Pattabiraman S, Amen T, Abraham AC, Eichler N, Lyakhovetsky R, Kaganovich D (2014). "Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin". Proceedings of the National Academy of Sciences of the United States of America 111 (22): 8049–54. doi:10.1073/pnas.1324035111. PMC 4050583. PMID 24843142.
^ ^a ^b Sarria AJ, Panini SR, Evans RM (September 1992). "A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells". J. Biol. Chem. 267 (27): 19455–63. PMID 1527066.
^ Leader M, Collins M, Patel J, Henry K (January 1987). "Vimentin: an evaluation of its role as a tumour marker". Histopathology 11 (1): 63–72. doi:10.1111/j.1365-2559.1987.tb02609.x. PMID 2435649.
^ "Immunohistochemistry from the Washington Animal Disease Diagnostic laboratory (WADDL)of the College of Veterinary Medicine, Washington State University". Retrieved 2009-03-14.
^ Moinova, Helen (April 2012). "Aberrant Vimentin Methylation is Characteristic of Upper GI Pathologies". Cancer Epidemiology Biomarkers Prev 21 (4): 594–600. doi:10.1158/1055-9965.epi-11-1060.
^ Ulirsch, Jacob (January 2013). "Vimentin DNA methylation predicts survival in breast cancer". Breast Cancer Research and Treatment 137 (2): 383–96. doi:10.1007/s10549-012-2353-5. PMID 23239149.
^ Meng JJ, Bornslaeger EA, Green KJ, Steinert PM, Ip W (1997). "Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments". J. Biol. Chem. 272 (34): 21495–503. doi:10.1074/jbc.272.34.21495. PMID 9261168.
^ Lopez-Egido J, Cunningham J, Berg M, Oberg K, Bongcam-Rudloff E, Gobl A (2002). "Menin's interaction with glial fibrillary acidic protein and vimentin suggests a role for the intermediate filament network in regulating menin activity". Exp. Cell Res. 278 (2): 175–83. doi:10.1006/excr.2002.5575. PMID 12169273.
^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
^ Herrmann H, Wiche G (1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin". J. Biol. Chem. 262 (3): 1320–5. PMID 3027087.
^ ^a ^b Brown MJ, Hallam JA, Liu Y, Yamada KM, Shaw S (2001). "Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin". J. Immunol. 167 (2): 641–5. doi:10.4049/jimmunol.167.2.641. PMID 11441066.
^ Matsuzawa K, Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y, Amano M, Kaibuchi K, Matsuura Y, Azuma I, Inagaki M (1997). "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. 234 (3): 621–5. doi:10.1006/bbrc.1997.6669. PMID 9175763.
^ Russell RL, Cao D, Zhang D, Handschumacher RE, Pizzorno G (2001). "Uridine phosphorylase association with vimentin. Intracellular distribution and localization". J. Biol. Chem. 276 (16): 13302–7. doi:10.1074/jbc.M008512200. PMID 11278417.
^ Tzivion G, Luo ZJ, Avruch J (2000). "Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo". J. Biol. Chem. 275 (38): 29772–8. doi:10.1074/jbc.M001207200. PMID 10887173.
^ Zehner ZE, Shepherd RK, Gabryszuk J, Fu TF, Al-Ali M, Holmes WM (August 1997). "RNA-protein interactions within the 3 ' untranslated region of vimentin mRNA". Nucleic Acids Res. 25 (16): 3362–70. doi:10.1093/nar/25.16.3362. PMC 146884. PMID 9241253.

External links

Vimentin Images

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. 原発不明の低分化癌 poorly differentiated cancer from an unknown primary site
2. 原発不明の腺癌 adenocarcinoma of unknown primary site
3. 異型線維黄色腫 atypical fibroxanthoma
4. 臨床的に有用な生物学的マーカーによる関節リウマチの診断および転帰評価 clinically useful biologic markers in the diagnosis and assessment of outcome in rheumatoid arthritis
5. 研究用生物学的マーカーによる関節リウマチの診断および評価ま investigational biologic markers in the diagnosis and assessment of rheumatoid arthritis

English Journal

Sex and age differences in brain-derived neurotrophic factor and vimentin in the zebra finch song system: Relationships to newly generated cells.

Tang YP1, Wade J2.
The Journal of comparative neurology.J Comp Neurol.2016 Apr 1;524(5):1081-96. doi: 10.1002/cne.23893. Epub 2015 Oct 15.
The neural song circuit is enhanced in male compared with female zebra finches due to differential rates of incorporation and survival of cells between the sexes. Two double-label immunohistochemical experiments were conducted to increase the understanding of relationships between newly generated ce
PMID 26355496

Identification of candidate synovial membrane biomarkers after Achyranthes aspera treatment for rheumatoid arthritis.

Zheng W1, Lu X2, Fu Z1, Zhang L1, Li X1, Xu X1, Ren Y1, Lu Y1, Fu H1, Tian J3.
Biochimica et biophysica acta.Biochim Biophys Acta.2016 Mar;1864(3):308-16. doi: 10.1016/j.bbapap.2015.12.010. Epub 2015 Dec 24.
Rheumatoid arthritis (RA) is a systemic autoimmune disease whose main symptom is a heightened inflammatory response in synovial tissues. To verify the anti-arthritic activities of Achyranthes aspera and its possible therapy-related factors on the pathogenesis of RA, the saponins in A. aspera root we
PMID 26724776

Cytokeratin-positive interstitial reticulum cell tumor: recognition of a potential "in situ" pattern.

Bösmüller H1, Klenske J2, Bonzheim I3, Scharpf M3, Rieger N3, Quintanilla-Fend L3, Fend F3.
Human pathology.Hum Pathol.2016 Mar;49:15-21. doi: 10.1016/j.humpath.2015.10.001. Epub 2015 Oct 26.
Cytokeratin-positive interstitial reticulum cell (CIRC) tumor is a very rare accessory cell neoplasm of lymphoid organs derived from fibroblastic reticulum cells, which originate from mesenchymal stem cells. We describe the histologic, immunophenotypical, and molecular features of a CIRC tumor in a
PMID 26826404

Japanese Journal

Microvascularization on Collared Peccary Placenta : a Microvascular Cast Study in Late Pregnancy

Santos Tatiana Carlesso,Oliveira Moacir Franco,Dantzer Vibeke [他]
Zoological science 29(7), 437-443, 2012-07
NAID 40019342090

臓器別専門外来でのReview of systems聴取の重要性が示唆されたAmelanotic melanomaの1剖検例

石井彰,菅原斉,渡辺珠美,松本充也,松林洋志,出光俊郎,兵頭隆史,山田茂樹,川上正舒
自治医科大学紀要 34, 129-134, 2012-03-01
… 皮下結節組織の免疫染色でvimentin 陽性,melanoma-associated antigen (HMB45) 陽性,S100蛋白陽性,epithelial membrane antigen陰性,cytokeratin(CAM5.2)陰性,CD30陰性であったことからAmelanotic melanomaと診断。 …
NAID 110008922666

Related Pictures

[Eriksson-1] Eriksson JE, Dechat T, Grin B, Helfand B, Mendez M, Pallari HM, Goldman RD (2009). "Introducing intermediate filaments: from discovery to disease". J Clin Invest 119 (7): 1763–71. doi:10.1172/JCI38339. PMC 2701876. PMID 19587451.

[Cabeen-2] Cabeen MT, Jacobs-Wagner C (2010). "The bacterial cytoskeleton". Annu Rev Genet 44: 365–92. doi:10.1146/annurev-genet-102108-134845. PMID 21047262.

[fuchs-3] Fuchs E., Weber K. (1994). "Intermediate filaments: structure, dynamics, function, and disease". Annu Rev Biochem 63: pp. 345–82. doi:10.1146/annurev.bi.63.070194.002021. PMID 7979242.

[chang-4] Chang L, Shav-Tal Y, Trcek T, Singer RH, Goldman RD. (2006). "Assembling an intermediate filament network by dynamic cotranslation". J Cell Biol 172 (5): 747–58. doi:10.1083/jcb.200511033. PMC 2063706. PMID 16505169.

[katsumoto-5] Katsumoto T., Mitsushima A., Kurimura T. (1990). "The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction". Biol Cell 68 (2): pp. 139–46. doi:10.1016/0248-4900(90)90299-I. PMID 2192768.

[goldman-6] Goldman RD, Khuon S, Chou YH, Opal P, Steinert PM (August 1996). "The function of intermediate filaments in cell shape and cytoskeletal integrity". J. Cell Biol. 134 (4): 971–83. doi:10.1083/jcb.134.4.971. PMC 2120965. PMID 8769421.

[Golucci-Guyon-7] Golucci-Guyon E, Portier M-M, Dunia I, Paulin D, Pournin S, Babinet C (1994). "Mice lacking vimentin develop and reproduce without an obvious phenotype.". Cell 79 (4): 679–94. doi:10.1016/0092-8674(94)90553-3. PMID 7954832.

[Eckes2000-8] Eckes B, Colucci-Guyon E, Smola H, Nodder S, Babinet C, Krieg T, Martin P (2000). "Impaired wound healing in embryonic and adult mice lacking vimentin.". Journal of cell science 113: 2455––62. PMID 10852824.

[pmid24843142-9] Ogrodnik M, Salmonowicz H, Brown R, Turkowska J, Sredniawa W, Pattabiraman S, Amen T, Abraham AC, Eichler N, Lyakhovetsky R, Kaganovich D (2014). "Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin". Proceedings of the National Academy of Sciences of the United States of America 111 (22): 8049–54. doi:10.1073/pnas.1324035111. PMC 4050583. PMID 24843142.

[sarria-10] Sarria AJ, Panini SR, Evans RM (September 1992). "A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells". J. Biol. Chem. 267 (27): 19455–63. PMID 1527066.

[pmid2435649-11] Leader M, Collins M, Patel J, Henry K (January 1987). "Vimentin: an evaluation of its role as a tumour marker". Histopathology 11 (1): 63–72. doi:10.1111/j.1365-2559.1987.tb02609.x. PMID 2435649.

[urlImmunohistochemistry_from_the_Washington_Animal_Disease_Diagnostic_laboratory_.28WADDL.29of_the_College_of_Veterinary_Medicine.2C_Washington_State_University-12] "Immunohistochemistry from the Washington Animal Disease Diagnostic laboratory (WADDL)of the College of Veterinary Medicine, Washington State University". Retrieved 2009-03-14.

[13] Moinova, Helen (April 2012). "Aberrant Vimentin Methylation is Characteristic of Upper GI Pathologies". Cancer Epidemiology Biomarkers Prev 21 (4): 594–600. doi:10.1158/1055-9965.epi-11-1060.

[14] Ulirsch, Jacob (January 2013). "Vimentin DNA methylation predicts survival in breast cancer". Breast Cancer Research and Treatment 137 (2): 383–96. doi:10.1007/s10549-012-2353-5. PMID 23239149.

[pmid9261168-15] Meng JJ, Bornslaeger EA, Green KJ, Steinert PM, Ip W (1997). "Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments". J. Biol. Chem. 272 (34): 21495–503. doi:10.1074/jbc.272.34.21495. PMID 9261168.

[pmid12169273-16] Lopez-Egido J, Cunningham J, Berg M, Oberg K, Bongcam-Rudloff E, Gobl A (2002). "Menin's interaction with glial fibrillary acidic protein and vimentin suggests a role for the intermediate filament network in regulating menin activity". Exp. Cell Res. 278 (2): 175–83. doi:10.1006/excr.2002.5575. PMID 12169273.

[pmid16189514-17] Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

[pmid16169070-18] Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.

[pmid3027087-19] Herrmann H, Wiche G (1987). "Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin". J. Biol. Chem. 262 (3): 1320–5. PMID 3027087.

[pmid11441066-20] Brown MJ, Hallam JA, Liu Y, Yamada KM, Shaw S (2001). "Cutting edge: integration of human T lymphocyte cytoskeleton by the cytolinker plectin". J. Immunol. 167 (2): 641–5. doi:10.4049/jimmunol.167.2.641. PMID 11441066.

[pmid9175763-21] Matsuzawa K, Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y, Amano M, Kaibuchi K, Matsuura Y, Azuma I, Inagaki M (1997). "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. 234 (3): 621–5. doi:10.1006/bbrc.1997.6669. PMID 9175763.

[pmid11278417-22] Russell RL, Cao D, Zhang D, Handschumacher RE, Pizzorno G (2001). "Uridine phosphorylase association with vimentin. Intracellular distribution and localization". J. Biol. Chem. 276 (16): 13302–7. doi:10.1074/jbc.M008512200. PMID 11278417.

[pmid10887173-23] Tzivion G, Luo ZJ, Avruch J (2000). "Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo". J. Biol. Chem. 275 (38): 29772–8. doi:10.1074/jbc.M001207200. PMID 10887173.

[pmid9241253-24] Zehner ZE, Shepherd RK, Gabryszuk J, Fu TF, Al-Ali M, Holmes WM (August 1997). "RNA-protein interactions within the 3 ' untranslated region of vimentin mRNA". Nucleic Acids Res. 25 (16): 3362–70. doi:10.1093/nar/25.16.3362. PMC 146884. PMID 9241253.

匿名

検索

案内

案内