KIF5B

KIF5B

Kinesin family member 5B, also known as KIF5B, is a human gene.cite web | title = Entrez Gene: KIF5B kinesin family member 5B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3799| accessdate = ]

PBB_Summary
section_title =
summary_text =

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Navone F, Niclas J, Hom-Booher N, "et al." |title=Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells. |journal=J. Cell Biol. |volume=117 |issue= 6 |pages= 1263–75 |year= 1992 |pmid= 1607388 |doi=
*cite journal | author=Niclas J, Navone F, Hom-Booher N, Vale RD |title=Cloning and localization of a conventional kinesin motor expressed exclusively in neurons. |journal=Neuron |volume=12 |issue= 5 |pages= 1059–72 |year= 1994 |pmid= 7514426 |doi=
*cite journal | author=Kull FJ, Sablin EP, Lau R, "et al." |title=Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. |journal=Nature |volume=380 |issue= 6574 |pages= 550–5 |year= 1996 |pmid= 8606779 |doi= 10.1038/380550a0
*cite journal | author=Rahman A, Friedman DS, Goldstein LS |title=Two kinesin light chain genes in mice. Identification and characterization of the encoded proteins. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15395–403 |year= 1998 |pmid= 9624122 |doi=
*cite journal | author=Tanaka Y, Kanai Y, Okada Y, "et al." |title=Targeted disruption of mouse conventional kinesin heavy chain, kif5B, results in abnormal perinuclear clustering of mitochondria. |journal=Cell |volume=93 |issue= 7 |pages= 1147–58 |year= 1998 |pmid= 9657148 |doi=
*cite journal | author=Rahman A, Kamal A, Roberts EA, Goldstein LS |title=Defective kinesin heavy chain behavior in mouse kinesin light chain mutants. |journal=J. Cell Biol. |volume=146 |issue= 6 |pages= 1277–88 |year= 1999 |pmid= 10491391 |doi=
*cite journal | author=Ong LL, Lim AP, Er CP, "et al." |title=Kinectin-kinesin binding domains and their effects on organelle motility. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32854–60 |year= 2000 |pmid= 10913441 |doi= 10.1074/jbc.M005650200
*cite journal | author=Kanai Y, Okada Y, Tanaka Y, "et al." |title=KIF5C, a novel neuronal kinesin enriched in motor neurons. |journal=J. Neurosci. |volume=20 |issue= 17 |pages= 6374–84 |year= 2000 |pmid= 10964943 |doi=
*cite journal | author=Setou M, Seog DH, Tanaka Y, "et al." |title=Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites. |journal=Nature |volume=417 |issue= 6884 |pages= 83–7 |year= 2002 |pmid= 11986669 |doi= 10.1038/nature743
*cite journal | author=Hakimi MA, Speicher DW, Shiekhattar R |title=The motor protein kinesin-1 links neurofibromin and merlin in a common cellular pathway of neurofibromatosis. |journal=J. Biol. Chem. |volume=277 |issue= 40 |pages= 36909–12 |year= 2002 |pmid= 12191989 |doi= 10.1074/jbc.C200434200
*cite journal | author=Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL |title=The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23. |journal=Biochemistry |volume=41 |issue= 50 |pages= 14906–15 |year= 2003 |pmid= 12475239 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Macioce P, Gambara G, Bernassola M, "et al." |title=Beta-dystrobrevin interacts directly with kinesin heavy chain in brain. |journal=J. Cell. Sci. |volume=116 |issue= Pt 23 |pages= 4847–56 |year= 2004 |pmid= 14600269 |doi= 10.1242/jcs.00805
*cite journal | author=Deloukas P, Earthrowl ME, Grafham DV, "et al." |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375–81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462
*cite journal | author=Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL |title=The ribosome receptor, p180, interacts with kinesin heavy chain, KIF5B. |journal=Biochem. Biophys. Res. Commun. |volume=319 |issue= 3 |pages= 987–92 |year= 2004 |pmid= 15184079 |doi= 10.1016/j.bbrc.2004.05.069
*cite journal | author=Jin J, Smith FD, Stark C, "et al." |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051
*cite journal | author=Su Q, Cai Q, Gerwin C, "et al." |title=Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons. |journal=Nat. Cell Biol. |volume=6 |issue= 10 |pages= 941–53 |year= 2004 |pmid= 15459722 |doi= 10.1038/ncb1169
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Brickley K, Smith MJ, Beck M, Stephenson FA |title=GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins: association in vivo and in vitro with kinesin. |journal=J. Biol. Chem. |volume=280 |issue= 15 |pages= 14723–32 |year= 2005 |pmid= 15644324 |doi= 10.1074/jbc.M409095200
*cite journal | author=Benzinger A, Muster N, Koch HB, "et al." |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. |journal=Mol. Cell Proteomics |volume=4 |issue= 6 |pages= 785–95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Нужна курсовая?

Look at other dictionaries:

  • RANBP2 — RAN binding protein 2 PDB rendering based on 1rrp …   Wikipedia

  • Kinesin — Animation of kinesin walking on a microtubule The kinesin dimer attaches to, and mo …   Wikipedia

  • Microtubule — Space filling model of a microtubule segment derived from cryo electron microscopy. The protofilaments are seen running along the axis of the segment. The microtubule (+) end is towards the top of the image.[1] Microtubules are a component of the …   Wikipedia

  • Keratin — Not to be confused with kerogen, carotene, chitin, or creatine. Microscopy of keratin filaments inside cells. Keratin refers to a family of fibrous structural proteins. Keratin is the key structural material making up the outer layer of human… …   Wikipedia

  • Cytoskeleton — The eukaryotic cytoskeleton. Actin filaments are shown in red, microtubules in green, and the nuclei are in blue. The cytoskeleton (also CSK) is a cellular scaffolding or skeleton contained within a cell s cytoplasm and is made out of protein.… …   Wikipedia

  • Microfilament — Actin cytoskeleton of mouse embryo fibroblasts, stained with Fluorescein isothiocyanate phalloidin Microfilaments ( or actin filaments) are the thinnest filaments of the cytoskeleton, a structure found in the cytoplasm of all eukaryotic cells.… …   Wikipedia

  • Actin — G Actin (PDB code: 1j6z). ADP and the divalent cation are highlighted …   Wikipedia

  • Myosin — Part of the myosin II structure. Atoms in the heavy chain are colored red on the left hand side, and atoms in the light chains are colored orange and yellow. Myosins comprise a family of ATP dependent motor proteins and are best known for their… …   Wikipedia

  • Lamin — Nuclear lamins, also known as Class V intermediate filaments, are fibrous proteins providing structural function and transcriptional regulation in the cell nucleus. Nuclear lamins interact with membrane associated proteins to form the nuclear… …   Wikipedia

  • MreB — Procaryotic MreB (PDB code: 1jce) in cartoon representation. The fold of the protein is similar to its eukaryotic counterpart actin. MreB is a protein found in bacteria that has been identified as a homologue of actin, as indicated by… …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”