Protein Transport
Biological Transport
Golgi Apparatus
Biological Transport, Active
Membrane Transport Proteins
Brefeldin A
Endoplasmic Reticulum
Vesicular Transport Proteins
Membrane Proteins
Intracellular Membranes
Carrier Proteins
Axonal Transport
Cathepsin A
Transport Vesicles
Molecular Sequence Data
Coatomer Protein
Amino Acid Sequence
Ion Transport
Saccharomyces cerevisiae Proteins
Saccharomyces cerevisiae
Vacuoles
Cell Membrane
Peas
trans-Golgi Network
Protein Sorting Signals
rab2 GTP-Binding Protein
Mutation
rab GTP-Binding Proteins
Cell Compartmentation
Models, Biological
COP-Coated Vesicles
Chloroplast Proteins
Monosaccharide Transport Proteins
Thylakoids
beta-Fructofuranosidase
Recombinant Fusion Proteins
Chloroplasts
Coated Vesicles
Proteins
Endosomes
Protein Processing, Post-Translational
Coat Protein Complex I
Electron Transport
Endoplasmic Reticulum, Rough
Cytoplasm
Organelles
rab1 GTP-Binding Proteins
Hydrogen-Ion Concentration
Microscopy, Electron
Protein Binding
ADP-Ribosylation Factors
Carboxypeptidases
Plant Proteins
Adenosine Triphosphatases
Sodium
Nuclear Pore Complex Proteins
Adenosine Triphosphate
Cloning, Molecular
Escherichia coli
Sequence Homology, Amino Acid
Green Fluorescent Proteins
Endocytosis
Base Sequence
ADP-Ribosylation Factor 1
Molecular Chaperones
Active Transport, Cell Nucleus
Temperature
Masoprocol
ran GTP-Binding Protein
Melanotrophs
Protein Structure, Tertiary
Viral Envelope Proteins
Glycosylation
Cytosol
Cricetinae
Subcellular Fractions
Microsomes
Clinical Chemistry Tests
Cells, Cultured
GTP-Binding Proteins
Cell Nucleus
Monensin
Microscopy, Fluorescence
Anion Transport Proteins
Dogs
Luminescent Proteins
Cation Transport Proteins
Yeasts
Microscopy, Immunoelectron
Qa-SNARE Proteins
Diffusion
Microtubules
N-Ethylmaleimide-Sensitive Proteins
Genetic Complementation Test
Adaptor Proteins, Vesicular Transport
HeLa Cells
Glucose
Cell Fractionation
Proton-Motive Force
Protein Synthesis Inhibitors
Sequence Alignment
Amino Acid Transport Systems
Guanine Nucleotide Exchange Factors
CHO Cells
Nuclear Envelope
Mitochondria
Guanosine Triphosphate
Transfection
Models, Molecular
Monomeric GTP-Binding Proteins
Lysosomes
Protein Conformation
Plasmids
Nocodazole
Receptors, Peptide
Mitochondrial Membrane Transport Proteins
Cell-Free System
Albumins
Symporters
Binding Sites
Adaptor Protein Complex 1
Vesicular stomatitis Indiana virus
RNA, Messenger
Cell Polarity
Peptides
Arabidopsis
Phospholipid Transfer Proteins
SNARE Proteins
3-O-Methylglucose
Mutagenesis, Site-Directed
Ovum Transport
ATP-Binding Cassette Transporters
Signal Recognition Particle
Membrane Fusion
Plants
Macromolecular Substances
Clathrin
DNA, Complementary
Fluorescent Antibody Technique
Amino Acid Transport Systems, Basic
Microtubule-Associated Proteins
Microscopy, Confocal
Signal Transduction
Potassium
Arabidopsis Proteins
Nuclear Proteins
DNA Primers
RNA Transport
Amino Acid Transport Systems, Neutral
Blotting, Western
Organic Cation Transport Proteins
Cricetulus
Proton-Translocating ATPases
Two-Hybrid System Techniques
Electrophoresis, Polyacrylamide Gel
Microinjections
Liver
Plant Leaves
Amino Acids
Heat-Shock Proteins
Phenotype
Glucose Transport Proteins, Facilitative
Exocytosis
HSP70 Heat-Shock Proteins
Epithelial Cells
Aminoisobutyric Acids
Mutagenesis
COS Cells
Protein Biosynthesis
Photosynthetic Reaction Center Complex Proteins
Cell Membrane Permeability
Gene Deletion
Anions
Membrane Transport Modulators
Glycoproteins
A novel in vivo assay for the analysis of protein-protein interaction. (1/21932)
The Ras Recruitment System (RRS) is a method for identification and isolation of protein-protein interaction. The method is based on translocation of cytoplasmic mammalian Ras protein to the inner leaflet of the plasma membrane through protein-protein interaction. The system is studied in a temperature-sensitive yeast strain where the yeast Ras guanyl nucleotide exchange factor is inactive at 36 degrees C. Protein-protein interaction results in cell growth at the restrictive temperature. We developed a gene reporter assay for the analysis of protein-protein interaction in mammalian cells. Ras activation in mammalian cells induces the mitogen-activated kinase cascade (MAPK), which can be monitored using Ras-dependent reporter genes. This greatly extends the usefulness of the system and provides a novel assay for protein-protein interaction in mammalian cells. (+info)Decisive structural determinants for the interaction of proline derivatives with the intestinal H+/peptide symporter. (2/21932)
To elucidate the decisive structural factors relevant for dipeptide-carrier interaction, the affinity of short amide and imide derivatives for the intestinal H+/peptide symporter (PEPT1) was investigated by measuring their ability to inhibit Gly-Sar transport in Caco-2 cells. Dipeptides with proline or alanine in the C-terminal position displayed affinity constants (Ki) of 0.15-1.2 mM and 0.08-9.5 mM, respectively. There was no clear relationship between hydrophobicity, size or ionization status of the N-terminal amino acid and the affinity of the dipeptides. However, analyzing the individual peptide bond conformations of Xaa-Pro dipeptides, a striking correlation between the cis/trans ratios (trans contents 24-70%) and the affinity constants was observed. After correcting the Ki values for the incompetent cis isomers, the Ki corr values of most dipeptides were in a small range of 0.1-0.16 mM. This result revealed the decisive role of peptide bond conformation even for a transport protein that is quite promiscuous in substrate translocation. When measuring affinity constants of Xaa-Pro and Xaa-Sar dipeptides, the cis/trans ratios cannot be ignored. Lower affinities of Lys-Pro, Arg-Pro and Pro-Pro indicate that additional molecular factors affect their binding at PEPT1. The Ki values obtained for the corresponding Xaa-Ala dipeptides support this conclusion. Potential substrates or inhibitors of peptide transport were found among Xaa-piperidides and Xaa-thiazolidides. Dipeptides with N-terminal proline displayed a very diverse affinity profile. However, in contrast to current knowledge, several Pro-Xaa dipeptides such as Pro-Leu, Pro-Tyr and Pro-Pro are recognized by PEPT1 with appreciable affinities. Binding seems mainly determined by the hydrophobicity of the C-terminal amino acid and the rigidity of the structure. (+info)Involvement of proline-rich tyrosine kinase 2 in platelet activation: tyrosine phosphorylation mostly dependent on alphaIIbbeta3 integrin and protein kinase C, translocation to the cytoskeleton and association with Shc through Grb2. (3/21932)
Proline-rich tyrosine kinase 2 (Pyk2) (also known as RAFTK, CAKbeta or CADTK) has been identified as a member of the focal adhesion kinase (FAK) family of protein-tyrosine kinases and it has been suggested that the mode of Pyk2 activation is distinct from that of FAK. In the present study we investigated the mode of Pyk2 activation in human platelets. When platelets were stimulated with thrombin, Pyk2, as well as FAK, was markedly tyrosine-phosphorylated, in a manner mostly dependent on alphaIIbbeta3 integrin-mediated aggregation. The residual Pyk2 tyrosine phosphorylation observed in the absence of platelet aggregation was completely abolished by pretreatment with BAPTA/AM [bis-(o-aminophenoxy)ethane-N,N,N',N'-tetra-acetic acid acetoxymethyl ester]. The Pyk2 phosphorylation was inhibited by protein kinase C (PKC) inhibitors at concentrations that inhibited platelet aggregation. In contrast, direct activation of PKC with the active phorbol ester PMA induced the tyrosine phosphorylation of Pyk2 and FAK but only when platelets were fully aggregated with the exogenous addition of fibrinogen (the ligand for alphaIIbbeta3 integrin). Furthermore, PMA-induced Pyk2 (and FAK) tyrosine phosphorylation was also observed when platelets adhered to immobilized fibrinogen. The activation of the von Willebrand factor (vWF)--glycoprotein Ib pathway with botrocetin together with vWF failed to induce Pyk2 (and FAK) tyrosine phosphorylation. Most Pyk2 and FAK was present in the cytosol and membrane skeleton fractions in unstimulated platelets. When platelets were stimulated with thrombin, both Pyk2 and FAK were translocated to the cytoskeleton in an aggregation-dependent manner. In immunoprecipitation studies, Pyk2, as well as FAK, seemed to associate with Shc through Grb2. With the use of glutathione S-transferase fusion proteins containing Shc-SH2, Grb2-SH2, and Grb2 N-terminal and C-terminal SH3 domains, it was implied that the proline-rich region of Pyk2 (and FAK) binds to the N-terminal SH3 domain of Grb2 and that the phosphotyrosine residue of Shc binds to the SH2 domain of Grb2. Although Pyk2 and FAK have been reported to be differentially regulated in many cell types, our results suggest that, in human platelets, the mode of Pyk2 activation is mostly similar to that of FAK, in terms of alphaIIbbeta3 integrin-dependent and PKC-dependent tyrosine phosphorylation. Furthermore, Pyk2, as well as FAK, might have one or more important roles in post-aggregation tyrosine phosphorylation events, in association with the cytoskeleton and through interaction with adapter proteins including Grb2 and Shc. (+info)Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes. (4/21932)
Aut7p, a protein recently implicated in autophagic events in the yeast Saccharomyces cerevisiae, exhibits significant homology to a mammalian protein, p16, herein termed GATE-16 (Golgi-associated ATPase Enhancer of 16 kDa), a novel intra-Golgi transport factor. Here we provide evidence for the involvement of Aut7p in different membrane trafficking processes. Aut7p largely substitutes for the activity of GATE-16 in mammalian intra-Golgi transport in vitro. In vivo, AUT7 interacts genetically with endoplasmic reticulum to Golgi SNAREs, specifically with BET1 and SEC22. Aut7p interacts physically with the following two v-SNAREs: Bet1p, which is involved in endoplasmic reticulum to Golgi vesicular transport, and Nyv1p, implicated in vacuolar inheritance. We suggest that, in addition to its role in autophagocytosis, Aut7p has pleiotropic effects and participates in at least two membrane traffic events. (+info)Targeting motifs and functional parameters governing the assembly of connexins into gap junctions. (5/21932)
To study the assembly of gap junctions, connexin--green-fluorescent-protein (Cx--GFP) chimeras were expressed in COS-7 and HeLa cells. Cx26-- and Cx32--GFP were targeted to gap junctions where they formed functional channels that transferred Lucifer Yellow. A series of Cx32--GFP chimeras, truncated from the C-terminal cytoplasmic tail, were studied to identify amino acid sequences governing targeting from intracellular assembly sites to the gap junction. Extensive truncation of Cx32 resulted in failure to integrate into membranes. Truncation of Cx32 to residue 207, corresponding to removal of most of the 78 amino acids on the cytoplasmic C-terminal tail, led to arrest in the endoplasmic reticulum and incomplete oligomerization. However, truncation to amino acid 219 did not impair Cx oligomerization and connexon hemichannels were targeted to the plasma membrane. It was concluded that a crucial gap-junction targeting sequence resides between amino acid residues 207 and 219 on the cytoplasmic C-terminal tail of Cx32. Studies of a Cx32E208K mutation identified this as one of the key amino acids dictating targeting to the gap junction, although oligomerization of this site-specific mutation into hexameric hemichannels was relatively unimpaired. The studies show that expression of these Cx--GFP constructs in mammalian cells allowed an analysis of amino acid residues involved in gap-junction assembly. (+info)Identification of mammalian TOM22 as a subunit of the preprotein translocase of the mitochondrial outer membrane. (6/21932)
A mitochondrial outer membrane protein of approximately 22 kDa (1C9-2) was purified from Vero cells assessing immunoreactivity with a monoclonal antibody, and the cDNA was cloned based on the partial amino acid sequence of the trypsin-digested fragments. 1C9-2 had 19-20% sequence identity to fungal Tom22, a component of the preprotein translocase of the outer membrane (the TOM complex) with receptor and organizer functions. Despite such a low sequence identity, both shared a remarkable structural similarity in the hydrophobicity profile, membrane topology in the Ncyt-Cin orientation through a transmembrane domain in the middle of the molecule, and the abundant acidic amino acid residues in the N-terminal domain. The antibodies against 1C9-2 inhibited the import of a matrix-targeted preprotein into isolated mitochondria. Blue native polyacrylamide gel electrophoresis of digitonin-solubilized outer membranes revealed that 1C9-2 is firmly associated with TOM40 in the approximately 400-kDa complex, with a size and composition similar to those of the fungal TOM core complex. Furthermore, 1C9-2 complemented the defects of growth and mitochondrial protein import in Deltatom22 yeast cells. Taken together, these results demonstrate that 1C9-2 is a functional homologue of fungal Tom22 and functions as a component of the TOM complex. (+info)Inhibition of NFkappaB by methyl chlorogenate from Eriobotrya japonica. (7/21932)
Methylchlorogenic acid (MC) is one of the main components in the leaves of Eriobotrya japonica. We previously reported that MC is the most potent antioxidant among several components of Eriobotrya japonica, and its antioxidant activity is stronger than that of chlorogenic acid. Antioxidants are expected to inhibit redox-sensitive NFkappaB activation since NFkappaB is readily influenced by cellular oxidative state. Based on these findings, in vivo experiments with MC were conducted to determine its ability to downregulate the NFkappaB activation in mouse liver. Results clearly showed that MC is a potent suppressor of BHP-induced NFkappaB activation. We observed a significant reduction by MC on BHP-induced translocation of p65 subunit of NFkappaB. This may be due to formation of p50/p65 heterodimer, which is mainly inducible NFkappaB. MC slightly blocked the BHP-induced IkappaB alpha degradation. There is a possibility of IkappaB alpha resynthesis via activated NFkappaB during a 5 h waiting period following BHP injection. The present results suggest that MC may inhibit NFkappaB activation, exhibiting its ability to downregulate the NFkappaB-dependent gene expression. Thus, it can be expected that MC may have potential for therapeutic intervention on various NFkappaB-dependent pathological conditions such as inflammatory or possibly mutagenic processes. (+info)Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G2 cell cycle arrest. (8/21932)
Human immunodeficiency virus (HIV) Vpr contributes to nuclear import of the viral pre-integration complex and induces G(2) cell cycle arrest. We describe the production of synthetic Vpr that permitted the first studies on the structure and folding of the full-length protein. Vpr is unstructured at neutral pH, whereas under acidic conditions or upon addition of trifluorethanol it adopts alpha-helical structures. Vpr forms dimers in aqueous trifluorethanol, whereas oligomers exist in pure water. (1)H NMR spectroscopy allows the signal assignment of N- and C-terminal amino acid residues; however, the central section of the molecule is obscured by self-association. These findings suggest that the in vivo folding of Vpr may require structure-stabilizing interacting factors such as previously described interacting cellular and viral proteins or nucleic acids. In biological studies we found that Vpr is efficiently taken up from the extracellular medium by cells in a process that occurs independent of other HIV-1 proteins and appears to be independent of cellular receptors. Following cellular uptake, Vpr is efficiently imported into the nucleus of transduced cells. Extracellular addition of Vpr induces G(2) cell cycle arrest in dividing cells. Together, these findings raise the possibility that circulating forms of Vpr observed in HIV-infected patients may exert biological effects on a broad range of host target cells. (+info)Examples of inborn errors of renal tubular transport include:
1. Cystinuria: This is a disorder that affects the reabsorption of cystine, an amino acid, in the renal tubules. It can lead to the formation of cystine stones in the kidneys.
2. Lowe syndrome: This is a rare genetic disorder that affects the transport of sodium and potassium ions across the renal tubules. It can cause a range of symptoms, including delayed development, intellectual disability, and seizures.
3. Glycine encephalopathy: This is a rare genetic disorder that affects the transport of glycine, an amino acid, across the renal tubules. It can cause a range of symptoms, including muscle weakness, developmental delays, and seizures.
4. Hartnup disease: This is a rare genetic disorder that affects the transport of tryptophan, an amino acid, across the renal tubules. It can cause a range of symptoms, including diarrhea, weight loss, and skin lesions.
5. Maple syrup urine disease: This is a rare genetic disorder that affects the transport of branched-chain amino acids (leucine, isoleucine, and valine) across the renal tubules. It can cause a range of symptoms, including seizures, developmental delays, and kidney damage.
Inborn errors of renal tubular transport can be diagnosed through a combination of clinical evaluation, laboratory tests, and genetic analysis. Treatment depends on the specific disorder and may include dietary modifications, medications, and dialysis. Early detection and treatment can help manage symptoms and prevent complications.
Transport protein
Vesicular transport protein
Membrane transport protein
Organic cation transport protein
Tricarboxylate transport protein, mitochondrial
Vesicular transport adaptor protein
Chloroplast protein-transporting ATPase
Mitochondrial membrane transport protein
Band 3 anion transport protein
Intraflagellar transport protein 46 homolog
Sodium-dependent phosphate transport protein 2A
Sodium-dependent phosphate transport protein 1
Sodium-dependent phosphate transport protein 2C
FadL outer membrane protein transport family
Sodium-dependent phosphate transport protein 2B
Long-chain fatty acid transport protein 4
Long-chain fatty acid transport protein 1
Fatty acid transport proteins
Sodium-glucose transport proteins
Neutral and basic amino acid transport protein rBAT
Transport by multiple-motor proteins
Kinesin-like protein KIF3A
Anion exchange protein 3
Iron-binding proteins
Maltose-binding protein
Transmembrane protein
Peptidoglycolipid addressing protein
Protein targeting
Dystrophin-associated protein complex
Death-associated protein 6
Sulfide
7α-Thioprogesterone
MAPK8IP3
Choriogenesis
GANC
Snowflake (gorilla)
Auxin binding protein
Haleem
Halobacterium salinarum
Metabolism
Genomic imprinting
Phosphate-transporting ATPase
Very long-chain acyl-CoA synthetase
List of pastoral visits of Pope Francis
Bacillus virus phi29
Velpatasvir
Anterograde tracing
Voltage-gated ion channel
PTBP1
SLC27A6
Selenoprotein P
Nucleoporin 85
Jebsen & Jessen (SEA)
Food desert
Tetratricopeptide repeat protein 39B
Caspase 10
Sodium-potassium pump
Mitochondrial DNA
Zinc deficiency
Phospholipid transport protein function at organelle contact sites
Laser-Driven Protein Transport Reveals Epigenetic Dynamics
PA-07-137: Protein Interactions Governing Membrane Transport in Pulmonary Health and Disease (R01)
copper transport protein ATOX1 [Mus musculus] - Protein - NCBI
PA-06-076: Protein Interactions Governing Membrane Transport in Pulmonary Health and Disease (R01)
Transport of the pathogenic prion protein through soils - PubMed
ATP6AP1L ATPase H+ transporting accessory protein 1 like (pseudogene) [Homo sapiens (human)] - Gene - NCBI
protein transport 完整報導 - Engadget 中文版
talks.cam : TICed off with protein transport into Plasmodium apicoplasts
e.hormone | Actions : Delivery :: Transport Proteins
Comprehensive Survey of Intracellular Transport System-Related Proteins in Complete Genomes and Draft Genomes
Towards functional assignment of Plasmodium membrane transport proteins: an experimental genetics study on four diverse proteins
Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection | eLife
Ion transport through chemically induced pores in protein-free phospholipid membranes - Lancaster EPrints
Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3.
The most abundant proteins in blood plasma are A globulins B transport proteins | Course Hero
Multidrug Resistance-Associated Protein 4 (MRP4/ABCC4) Controls Efflux Transport of Hesperetin Sulfates in Sulfotransferase 1A3...
KAKEN - Research Projects | Analysis of parasitophorous vacuole membrane protein in hemoglobin transport and metabolism of...
Drug binding to human fatty acid binding proteins: a mechanism of cellular transport for poorly water soluble drugs -...
The pseudorabies virus protein, pUL56, enhances virus dissemination and virulence but is dispensable for axonal transport<...
Evidence for a role of the polysaccharide capsule transport proteins in pertussis pathogenesis | ScholarBank@NUS
Cells use bubblelike structures (vesicles, yellow) to transport proteins and fats
The choroid plexus epithelium is the site of the organic anion transport protein in the brain<...
Planteome: Term Details for 'misfolded protein transport' (GO:0070843)
Water Structure-Dependent Charge Transport in Proteins - Digital Collections - National Library of Medicine
IJMS | Free Full-Text | Dynamics, a Powerful Component of Current and Future in Silico Approaches for Protein Design and...
Cytoplasm4
- In other words, the researchers found that the proteins traveled into the cytoplasm after photoactivation. (genengnews.com)
- We have recently shown that drugs bind to fatty acid binding proteins which are abundant in the cytoplasm of these cells, and which physiologically play a role in the absorption and transport of endogenous lipophilic molecules such as fatty acids. (monash.edu)
- TANGO1 proteins sometimes spread across various cell organelles and the cytoplasm. (bioengineer.org)
- The asymmetrical distribution of Ran-GTP and Ran-GDP drives cargo transport between the nucleus and cytoplasm through karyopherins, a family of nuclear transport carrier proteins that bind to Ran-GTP. (nih.gov)
Water soluble1
- To get around, the hormones attach to water soluble proteins that shuttle them in the blood's aqueous environment. (tulane.edu)
Peptides1
- Binding of viral nuclear localization signal peptides to importin-α nuclear transport protein. (bvsalud.org)
Fatty2
- Other hormone transport proteins are relatively non-selective, transporting almost any lipophilic molecule that enters the bloodstream, including steroid and thyroid hormones, plant-derived flavonoids, retinoids (vitamin A), fatty acids, and antibiotics. (tulane.edu)
- The studies described in this application will examine the relationship between drug binding affinity for fatty acid binding protein and drug permeability across the absorptive epithelial cell in an attempt to better understand the mechanisms of drug absorption and transport. (monash.edu)
Abundant1
- As the most abundant plasma protein, albumin's blood concentration often far exceeds even the flavonoids that flood the bloodstream after fruits and vegetables are eaten. (tulane.edu)
ATPase2
- Predicted to be part of plasma membrane proton-transporting V-type ATPase complex. (nih.gov)
- We selected one conserved MTP called FT2, which was previously shown to transport folate, a P-type ATPase that is specific for P. falciparum as well as two essential MTPs, CRT and ATP4. (hu-berlin.de)
Biological2
- Szent-Gyorgyi's theory of cancer was based on his idea that the electron transport (charge transfer) essential to biological energy processes occurred via the structural proteins in cells. (nih.gov)
- A membrane transport protein (or simply transporter ) is a membrane protein [ 1 ] involved in the movement of ions , small molecules , or macromolecules , such as another protein across a biological membrane . (en-academic.com)
Amino2
- The optogenetic technique involves the use of a three-part light switch, a construct comprising the photosensitive AsLOV2 protein, a short amino acid sequence that acts as a kind of shipping label, and a fluorescent protein. (genengnews.com)
- Made up of more than 1,000 amino acids, these proteins are very large indeed. (bioengineer.org)
Lipid3
- Thus, MCS provide an ideal location at which lipid transfer proteins (LTPs) can achieve the efficient transfer of individual classes of lipids from the ER to other organelles via non-vesicular transport. (nih.gov)
- When the TANGO1 protein detects a maturating collagen, it supports the formation of a tunnel-like lipid connection that transports the collagen from its place of manufacture to its site of action. (bioengineer.org)
- Such research on the basics of cholesterol transport in animal models could lend insight into potential therapies for humans with high cholesterol and other lipid disorders. (nih.gov)
Genes3
- A new technique for probing the functions of genes and proteins works by enabling the laser-directed movement of proteins from one cellular location to another. (genengnews.com)
- According to Dr. Kuhlman, the light switch demonstrates the value of a technique that can rapidly probe the function of genes and proteins. (genengnews.com)
- We are using CRISPR/Cas9 to construct cell lines in which sequences encoding AIDs are inserted into both alleles of targeted genes of human tissue-culture cells that stably express the Transport Inhibitor Response 1 (TIR1) protein. (nih.gov)
Serum3
- Serum amyloid A (SAA) proteins are strongly induced in the liver by systemic infection and in the intestine by bacterial colonization, but their exact functions remain unclear. (elifesciences.org)
- Serum retinol binding protein transports ingested retinol from the intestine to the liver and other tissues. (elifesciences.org)
- It had been suggested that Serum Amyloid A (SAA) proteins, a family of proteins made by some liver and intestinal cells, could be involved in the response to infection, because these proteins' levels increase during infection. (elifesciences.org)
Albumin2
- Albumin is a relatively non-selective transport protein found in all vertebrates. (tulane.edu)
- This study aimed to increase understanding of the electrical properties of pure proteins such as albumin, in the hydrated, rather than dry state. (nih.gov)
Bloodstream1
- Retinol must bind to specific proteins to be able to move through the bloodstream and be transported around the body. (elifesciences.org)
Mediate2
- Retinol plays a vital role in the immune response to infection, yet proteins that mediate retinol transport during infection have not been identified. (elifesciences.org)
- These data suggest that importin-alpha3 could mediate active nuclear transport of tTG which may be important for the regulation of critical cellular processes. (nih.gov)
Plasmodium2
- Etliche Membran Transport Proteine (MTP) sind essentiell in den Plasmodium Blutstadien, und geraten zunehmend in den Fokus der Wirkstoffentwicklung. (hu-berlin.de)
- Many membrane transport proteins (MTP) are essential for Plasmodium infection and gain importance as candidate drug targets in malaria therapy, whereas the physiological functions often remain enigmatic. (hu-berlin.de)
Cellular2
- Cells use bubblelike structures called vesicles (yellow) to import, transport and export cargo and in cellular communication. (nih.gov)
- Ran is a Ras-family GTPase that plays critical roles in many cellular processes, including nucleo-cytoplasmic transport, nuclear envelope assembly, and mitotic spindle assembly. (nih.gov)
Bind2
- Second, an endocrine disrupter can attach to the transport protein, denature it, and destroy its ability to bind to other molecules. (tulane.edu)
- went on to solve the crystal structure of a mouse SAA protein, and showed that four SAA molecules bind together to form a 'pocket' that can hold a retinol molecule. (elifesciences.org)
MAMMALIAN1
- Aster proteins facilitate nonvesicular plasma to ER cholesterol transport in mammalian cells. (nih.gov)
Nucleotide1
- The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in protein sequences. (nih.gov)
Viral2
- The pUS9 protein is a critical viral effector of the anterograde axonal transport that underlies this process. (northwestern.edu)
- Our analyses indicate that the VEEV coreNLS sequence is virtually unique among human and viral proteins interacting with imp α making it a potential target for VEEV-specific inhibitors. (bvsalud.org)
MRNA1
- The mRNA for organic anion transport protein (oatp) was previously shown to be present in abundance in liver and kidney, and in small amounts in brain. (elsevier.com)
Selective4
- Some hormone transport proteins in plasma are highly selective, transporting only steroid or only thyroid hormones. (tulane.edu)
- Certain endocrine disrupting compounds (EDs) interfere with hormone delivery by binding to the selective steroid hormone or thyroid hormone transport proteins. (tulane.edu)
- To better address the role of individual nucleoporins, we adapted AID strategies for selective and rapid degradation of individual proteins. (nih.gov)
- TIR1 acts as a subunit of the SCF ubiquitin ligase complex, so that the AID-tagged fusion proteins undergo rapid, selective degradation upon addition of the plant hormone auxin. (nih.gov)
Findings2
- The findings indicate that pUL56 is a virulence factor that supports virus dissemination in vivo, yet along with pUS9, is dispensable for axonal transport. (northwestern.edu)
- The lab's latest findings involve Aster proteins. (nih.gov)
Substances2
- that is they exist within and span the membrane across which they transport substances. (en-academic.com)
- The proteins may assist in the movement of substances by facilitated diffusion or active transport . (en-academic.com)
Nuclear7
- Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3. (nih.gov)
- Recently, nuclear localization of tTG has been reported indicating the potential of active nuclear transport. (nih.gov)
- In this study we use the yeast two-hybrid assay and co-immunoprecipitation to show that tTG interacts with the nuclear transport protein importin-alpha3. (nih.gov)
- nuclear transport protein. (bvsalud.org)
- Using all-atom replica-exchange molecular dynamics simulations , we mapped the mechanisms of binding of the nuclear localization signal (NLS) sequence from Venezuelan equine encephalitis virus (VEEV) capsid protein to importin -α ( imp α) transport protein . (bvsalud.org)
- However, the abundance and unusual stability of these proteins requires an extended interval for their depletion, so that many phenotypes could be indirect consequences of disrupted nuclear trafficking as the number and quality of NPCs decline. (nih.gov)
- Using these cell lines, we will study the role of nucleoporins in nuclear organization and function, mitosis, nuclear transport, transcription and overall nuclear architecture. (nih.gov)
Fluorescent2
- The third component, the fluorescent protein, allows protein movements to be tracked in real time. (genengnews.com)
- In general, we also add a fluorescent tag to the targeted proteins, allowing the degradation to be monitored visually as well as biochemically. (nih.gov)
Shuttle1
- Through biochemical and cell biology experiments, Tontonoz's team showed that Aster proteins help to shuttle HDL between the cell membrane and the ER. (nih.gov)
Molecules1
- Third, an endocrine disruptor could change how quickly or slowly the transport protein unloads hormone molecules. (tulane.edu)
Integral1
- With the tremendous progress in more powerful computer hardware and more efficient algorithms, some of in silico tools and methods have started to apply the more realistic description of proteins as their conformational ensembles, making protein dynamics an integral part of their prediction workflows. (mdpi.com)
Infection3
- A comprehensive spatio-temporal expression analysis of transgenic parasites expressing mCherry-tagged proteins revealed expression beyond blood infection, indicative of functions in additional parasite stages. (hu-berlin.de)
- Our results thus identify SAAs as a family of microbe-inducible retinol binding proteins, reveal a unique protein architecture involved in retinol binding, and suggest how retinol is circulated during infection. (elifesciences.org)
- Here, we examine the role of a related pseudorabies virus protein, pUL56, during neuronal infection. (northwestern.edu)
Liver3
- These transport proteins deliver the hormones to their target cells and protect them from being chemically altered, inactivated, and eliminated from the body by the liver and kidneys. (tulane.edu)
- These chemicals can out compete thyroid hormones for binding to thyroid hormone transport proteins (specifically TTR) allowing the liver and kidney to dispose of the free-floating hormone too quickly. (tulane.edu)
- found that mice fed a diet poor in vitamin A produced fewer SAA proteins in their liver and intestinal cells. (elifesciences.org)
Nucleus3
- The technique, a form of optogenetics, has already been used to export an epigenetically active protein from the nucleus. (genengnews.com)
- These two components give the light switch the ability to drive proteins out of the nucleus, provided the light switch is both attached to a protein of interest and also illuminated by laser light. (genengnews.com)
- This article described what happened when the researchers embedded their light switches into two proteins called LexA and Bre1 that act on DNA and thus normally reside in the nucleus. (genengnews.com)
Antibiotics2
- Whey protein might decrease how well some antibiotics work. (medlineplus.gov)
- To avoid this interaction, take antibiotics at least 2 hours before or 4-6 hours after whey protein. (medlineplus.gov)
Parasites1
- Uptake and transport of hemoglobin by malarial parasites are carried out through parasitophorous vacuole membrane (PVM), but the molecular mechanism has not been elucidated. (nii.ac.jp)
Typically1
- An abnormally folded form of the prion protein (designated PrP(TSE)) is typically associated with TSE infectivity and may constitute the major, if not sole, component of the infectious agent. (nih.gov)
Transporters1
- We address the possibility of being able to induce the trafficking of salt ions and other solutes across cell membranes without the use of specific protein-based transporters or pumps. (lancs.ac.uk)
Examine1
- Therefore, the researchers are planning to apply their new optogenetic tool to study the function of different proteins and examine how the "behavior" of these proteins changes depending on both time and space. (genengnews.com)
Processes1
- Computational prediction has become an indispensable aid in the processes of engineering and designing proteins for various biotechnological applications. (mdpi.com)
Interactions2
- This Funding Opportunity Announcement (FOA) issued by t he National Heart, Lung, and Blood Institute , National Institutes of Health (NIH), solicits research grant applications to delineate t he protein interactions and pathways governing membrane trafficking pathways operative in pulmonary health and disease and develop novel therapeutic interventions. (nih.gov)
- The National Heart, Lung, and Blood Institute invites research grant applications to delineate the protein interactions and pathways governing membrane trafficking pathways operative in pulmonary health and disease and develop novel therapeutic interventions. (nih.gov)
Vesicles1
- In the result, ETRAMP10.3 was found to be localized to the PVM, cytostorm and hemoglobin transport vesicles, and to be an indicator of hemoglobin transport during gametocyte stage. (nii.ac.jp)
Study1
- In this study, I focused on the PVM protein (ETRAMP family) of P. falciparum and analyzed the localization in the membrane structure involved in hemoglobin transport. (nii.ac.jp)
Cells1
- Collagen is a huge protein that is produced in the so-called endoplasmic reticulum, an organelle inside cells. (bioengineer.org)
Evidence3
- Combined, this evidence suggests that SAAs are the retinol binding proteins that transport retinol during infections. (elifesciences.org)
- Our results provide compelling evidence that the small amphiphilic solute DMSO is able to induce transient defects (water pores) in membranes and to promote a subsequent diffusive pore-mediated transport of salt ions. (lancs.ac.uk)
- Whey protein is also used for asthma, diabetes, weight loss, and many other conditions, but there is no good scientific evidence to support most of these uses. (medlineplus.gov)
Specific1
- The directed movement of misfolded proteins in a cell, including the movement of proteins between specific compartments or structures within a cell. (planteome.org)
Ions1
- Symporters transport two or more ions together in the same direction, antiporters in the opposite direction. (en-academic.com)
Human1
- Here we show that mouse and human SAAs are retinol binding proteins. (elifesciences.org)
Immune1
- Whey protein might improve the nutrient content of the diet and also have effects on the immune system. (medlineplus.gov)
MICE1
- His lab uses such mice to understand how cholesterol transport works. (nih.gov)
Experiments2
- We report the results of saturated column experiments designed to evaluate PrP(TSE) transport through five soils with relatively high sand or silt contents and low organic carbon content. (nih.gov)
- This localization of oatp is consistent with previous experiments showing vectorial transport of organic anions between the choroid plexus and the cerebrospinal fluid. (elsevier.com)
Roles1
- Proteins can play different roles at different stages of development, in different parts of an organism, and during various disease states. (genengnews.com)
Growth1
- An Infant Formula with Partially Hydrolyzed Whey Protein Supports Adequate Growth and Is Safe and Well-Tolerated in Healthy, Term Infants: A Randomized, Double-Blind, Equivalence Trial. (medlineplus.gov)
Hormone1
- Currently, the overall consequences of disrupted sex steroid hormone transport are unknown. (tulane.edu)
Family1
- A family of proteins known as TANGO1 is responsible for identifying and transporting the collagen. (bioengineer.org)
Search1
- View conserved domains detected in this protein sequence using CD-search. (nih.gov)
Structure2
- The name is an acronym for the total of four proteins that adopt exactly this structure: MIA, Otoraplin, TALI/TANGO1 homology," explains Raphael Stoll. (bioengineer.org)
- The group discovered that these proteins reside inside a specialized structure in the cell known as the endoplasmic reticulum (ER). (nih.gov)
Body2
- as such it is unclear how retinol is transported when the body is under attack from pathogens. (elifesciences.org)
- Whey protein might decrease how much levodopa the body absorbs. (medlineplus.gov)
Cell1
- Pentachlorophenol, a persistent organohalogen used as an herbicide, pesticide, and product additive, greatly slows down testosterone unloading from the sex steroid transport protein at the target cell. (tulane.edu)
Opposite1
- MCS are locations at which the membrane es of two organelles are closely positioned to provide a microenvironment where proteins in one membrane can interact with the opposite membrane. (nih.gov)