- RAVER1
for PTB hnRNPI and microfilament attachment proteins. journal J. Cell Biol. volume 155 issue ... more details
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- Palladin
of Human Palladin, a Microfilament associated Protein journal Mol. Biol. Cell volume 12 issue ... Palladin, a Microfilament associated Protein journal Mol. Biol. Cell volume 12 issue 10 pages 3060 ... of Human Palladin, a Microfilament associated Protein journal Mol. Biol. Cell volume ... more details
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- GAS2L1
Orphan date February 2009 PBB geneid 10634 GAS2 like protein 1 is a protein that in humans is encoded by the GAS2L1 gene . ref name pmid8975699 cite journal author Zucman Rossi J, Legoix P, Thomas G title Identification of new members of the Gas2 and Ras families in the 22q12 chromosome region journal Genomics volume 38 issue 3 pages 247 54 year 1997 month Mar pmid 8975699 pmc doi 10.1006 geno.1996.0625 ref ref name pmid12584248 cite journal author Goriounov D, Leung CL, Liem RK title Protein products of human Gas2 related genes on chromosomes 17 and 22 hGAR17 and hGAR22 associate with both microfilaments and microtubules journal J Cell Sci volume 116 issue Pt 6 pages 1045 58 year 2003 month Feb pmid 12584248 pmc doi 10.1242 jcs.00272 ref ref name pmid1607387 cite journal author Brancolini C, Bottega S, Schneider C title Gas2, a growth arrest specific protein, is a component of the microfilament network system journal J Cell Biol volume 117 issue 6 pages 1251 61 year 1992 month Jul pmid 1607387 pmc 2289493 doi 10.1083 jcb.117.6.1251 ref ref name entrez cite web title Entrez Gene GAS2L1 growth arrest specific 2 like 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 10634 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text The protein encoded by this gene, a member of the GAS2 family, is similar in sequence to the mouse protein Gas2, an actin associated protein expressed at high levels in growth arrested cells. Expression of the mouse Gas2 gene is negatively regulated by serum and growth factors. Three transcript variants encoding two different isoforms have been found for this gene. ref name entrez cite web title Entrez Gene GAS2L1 growth arrest specific 2 like 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 10634 accessdate ref References reflist Further reading refbegin 2 PBB Fu ... more details
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- Intermediate filament
File Intermediate filament.svg thumb right 300px Structure of intermediate filament Infobox protein family Symbol IF tail Name Intermediate filament tail domain image PDB 1ifr EBI.jpg width caption structure of lamin a c globular domain Pfam PF00932 Pfam clan InterPro IPR001322 SMART PROSITE PDOC00198 MEROPS SCOP 1ivt TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol Filament Name Intermediate filament protein image PDB 1gk4 EBI.jpg width caption human vimentin coil 2b fragment cys2 Pfam PF00038 Pfam clan InterPro IPR016044 SMART PROSITE PDOC00198 MEROPS SCOP 1gk7 TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol Filament head Name Intermediate filament head DNA binding region image width caption Pfam PF04732 Pfam clan InterPro IPR006821 SMART PROSITE MEROPS SCOP 1gk7 TCDB OPM family OPM protein CAZy CDD Intermediate filaments IFs are a family of related protein s that share common structural and sequence features. Intermediate filaments have an average diameter of 10 nanometer s, which is between that of 7 nm actin microfilament s , and that of 25 nm microtubule s, although they were initially designated intermediate because their average diameter is between those of narrower microfilament s actin and wider myosin filaments. ref cite pmid 5664223 cite pmid 17551517 ref Most types of intermediate filaments are cytoplasm ic, but one type, the Type V Nuclear Lamins lamins , are nuclear. Structure The domain structure of IF molecules is conserved. Each protein has a non alpha helical globular domain at the N and C termini, which surrounds the alpha helical rod domain. The basic building block for IFs is a parallel and in register protein dimer dimer . The dimer is formed through the interaction of the rod domain to form a coiled coil . ref name Qin2009 cite pmid 19806221 ref Cytoplasmic IF assemble into non polar unit length filaments ULF , which then assemble into longer structures. Part of the assembly process includes a co ... more details
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- List of MeSH codes (D05)
D05.750.078.687 Lignin lignin MeshNumber D05.750.078.730 Microfilament Proteins microfilament ... more details
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- Ezrin
P, Suila H, Carp n O year 2001 month October title Characterization of human palladin, a microfilament ... membrane microfilament linker, signals cell survival through the phosphatidylinositol 3 kinase Akt ... more details
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- Actinin alpha 4
I, et al. title Raver1, a dual compartment protein, is a ligand for PTB hnRNPI and microfilament ... more details
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- PFN2
B M, Walter U year 1995 month Apr. title The proline rich focal adhesion and microfilament protein ... cite journal author Reinhard M, Giehl K, Abel K, et al. title The proline rich focal adhesion and microfilament ... more details
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- Morphogenesis
, laminin, or other ECM components, and intracellularly to microfilament binding proteins ACTN1 ... more details
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- Villin
to support the microfilament s of the microvilli of the brush border. However, knockout mice appear ... more details
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- Caldesmon
author Adam L title Regulation of microfilament reorganization and invasiveness of breast cancer cells ... more details
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- Preprophase
site for the cell plate . It consists of microtubules and microfilament s actin and persists into prophase ... more details
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- Espin (protein)
PBB geneid 83715 Espin , also known as autosomal recessive deafness type 36 protein or ectoplasmic specialization protein , is a protein that in humans is encoded by the ESPN gene . ref name entrez cite web title Entrez Gene espin url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 83715 accessdate ref Espin is a microfilament binding protein. Function Espin is a multifunctional actin bundling protein. It plays a major role in regulating the organization, dimensions, dynamics, and signaling capacities of the actin filament rich, microvillus type specializations that mediate sensory transduction in various mechanosensory and chemosensory cells. ref name entrez Clinical significance Mutations in this gene are associated with autosomal recessive neurosensory deafness, autosomal dominant sensorineural deafness without vestibular involvement, and Nonsyndromic deafness DFNB36 . ref name entrez References reflist Further reading refbegin 2 cite journal author Naz S title Mutations of ESPN cause autosomal recessive deafness and vestibular dysfunction journal J. Med. Genet. volume 41 issue 8 pages 591 5 year 2004 pmid 15286153 doi 10.1136 jmg.2004.018523 author separator , author2 Griffith AJ author3 Riazuddin S display authors 3 last4 Hampton first4 LL last5 Battey Jr first5 JF last6 Khan first6 SN last7 Riazuddin first7 S last8 Wilcox first8 ER last9 Friedman first9 TB pmc 1735855 cite journal author Boulouiz R title A novel mutation in the Espin gene causes autosomal recessive nonsyndromic hearing loss but no apparent vestibular dysfunction in a Moroccan family journal Am. J. Med. Genet. A volume 146A issue 23 pages 3086 9 year 2008 pmid 18973245 doi 10.1002 ajmg.a.32525 author separator , author2 Li Y author3 Soualhine H display authors 3 last4 Abidi first4 Omar last5 Chafik first5 Abdelaziz last6 N rnberg first6 Gudrun last7 Becker first7 Christian last8 N rnberg first8 Peter last9 Kubisch first9 Christian cite journal author Cosetti M tit ... more details
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- Index of biochemistry articles
microevolution microfilament microfilament protein Microsatellite genetics microsatellite microscope ... more details
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- Amoeboid
Image live Ammonia tepida.jpg thumb Foraminifera n Ammonia tepida Amoeboids are unicellular single celled life forms characterized by an irregular shape. ref cite web url http www.memidex.com amoeboid title amoeboid work Memidex WordNet Dictionary Thesaurus accessdate 2010 12 02 ref Amoeboid and am ba are often used interchangeably even by biologists, ref cite journal author Eric Bapteste, Henner Brinkmann, Jennifer A. Lee, Dorothy V. Moore, Christoph W. Sensen, Paul Gordon, Laure Durufl , Terry Gaasterland, Philippe Lopez, Mikl s M ller & Herv Philippe title The analysis of 100 genes supports the grouping of three highly divergent amoebae Dictyostelium, Entamoeba, and Mastigamoeba journal Proceedings of the National Academy of Sciences year 2001 volume 99 issue 3 pages 1414 1419 url http www.pnas.org content 99 3 1414.full.pdf doi 10.1073 pnas.032662799 pmid 11830664 pmc 122205 ref and especially refer to a creature moving by using pseudopod ia. Most references to amoebas or amoebae are to amoeboids in general rather than to the specific genus Amoeba . The genus Amoeba and amoeboids in general both derive their names from the ancient Greek word for change. Structure Amoeboids Amoeboid movement move using pseudopodia , which are bulges of cytoplasm . Amoebas breathe using their entire cell membrane that is constantly immersed in water. Excess water can cross into the cytosol . Amoebas have a contractile vacuole to expel excess water. Food sources vary in amoeboids. They may consume bacteria or other protist s. Some are detritivore s and eat dead organic material. They extend a pair of pseudopodia around food. They fuse to make a food vacuole which then fuses with a lysosome to add digestive chemicals. Undigested food is expelled at the cell membrane. Amoebas use pseudopodia to move and feed. They are powered by flexible microfilament s near the membrane. Microfilaments are at least 50 of the cytoskeleton . The other parts are more stiff and are composed of intermed ... more details
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- Cytoskeleton
strand. They also act as tracks for the movement of myosin molecules that attach to the microfilament ... more details
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- Membrane protein
Image 2r9r opm.gif thumb 300px Crystal structure of Potassium channel KvAP. Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots. A membrane protein is a protein molecule that is attached to, or associated with the membrane biology membrane of a cell biology cell or an organelle . More than half of all proteins interact with membranes. Function Biological membrane s consist of a phospholipid lipid bilayer bilayer and a variety of proteins that accomplish vital biological functions. Protein Structural proteins Structural protein s are attached to microfilament s in the cytoskeleton which ensures stability of the cell. Cell adhesion molecule s allow cells to identify each other and interact. Such proteins are involved in immune response , for example. Membrane enzymes produce a variety of substances essential for cell function. Membrane receptor proteins serve as connection between the cell s Cytoplasm internal and Extracellular space external environments. Membrane transport protein Transport protein s play an important role in the maintenance of concentrations of ion s. These transport proteins come in two forms carrier protein s and channel protein s. Cell membranes are the biological membranes that separate the interior of all cells from the outside environment Main categories Membrane proteins can be divided into several categories ref name Karp2009 cite book author Gerald Karp title Cell and Molecular Biology Concepts and Experiments url http books.google.com books?id arRGYE0GxRQC&pg PA128 accessdate 13 November 2010 year 2009 publisher John Wiley and Sons isbn 978 0 470 48337 4 pages 128 ref Integral membrane proteins which are permanently bound to the lipid bilayer Peripheral membrane proteins that are temporarily associated with lipid bilayer or with integral membrane proteins Lipid anchored protein s bound to lipid bilayer bound through lipidation lipidated amino acid residues In addition, pore forming toxin s and many an ... more details
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- Index of biology articles
microfilament Microsatellite genetics microsatellite microscope microtubules Miller Urey experiment ... more details
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- Protein structure
Refimprove date March 2009 In molecular biology protein structure describes the various levels of organization of protein molecules. Proteins are an important class of biological macromolecules present in all organism s. Proteins are polymers of amino acid s. Classified by their physical size, proteins are nanoparticle s definition 1 100 nm . Each protein polymer also known as a polypeptide consists of a sequence formed from 20 possible L amino acids, also referred to as residues. For chains under 40 residues the term peptide is frequently used instead of protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations, driven by a number of non covalent interactions such as hydrogen bonding , ionic interaction s, Van Der Waals forces , and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three dimensional structure. This is the topic of the scientific field of structural biology , which employs techniques such as X ray crystallography , protein NMR NMR spectroscopy , and dual polarisation interferometry to determine the structure of proteins. Protein structures range in size from tens to several thousand residues ref name Brocchieri2005 Cite journal author Brocchieri L, Karlin S title Protein length in eukaryotic and prokaryotic proteomes date 2005 06 10 volume 33 issue 10 pages 3390 3400 doi 10.1093 nar gki615 pmid 15951512 journal Nucleic Acids Research pmc 1150220 ref Very large aggregates can be formed from protein subunit s for example, many thousand actin molecules assemble into a microfilament . A protein may undergo reversible structural changes in performing its biological function. The alternative structures of the same protein are referred to as different Conformational isomerism conformation s, and transitions between them are called conformational change s. Levels of protein structure File Main protein structure level ... more details
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- Glucokinase regulatory protein
GKRP shuttles between the nucleus and the cytoplasm. It may be attached to the microfilament cytoskeleton ... more details
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- Walter C. Dornez
long microfilament razor wires, which he controls as if they were extensions of his own body. The wires ... more details
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- Boogiepop Returns: VS Imaginator Part 1
him at this, but a microfilament wire saves him at the last second. The girl had been none other ... more details
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- Boogiepop Returns: VS Imaginator Part 2
moment is saved by a microfilament wire. Accompanied by the Die Meistersinger von N rnberg , Boogiepop ... more details
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- Talin protein
at the termini of microfilament bundles in cultured chicken cells journal Cell volume 18 issue ... more details
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- RHOB
al. title The HIV 1 vpr protein induces anoikis resistance by modulating cell adhesion process and microfilament ... more details
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