Multiprotein Complexes
Protein Binding
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Macromolecular Substances
Amino Acid Sequence
Nuclear Proteins
Transcription Factors
DNA-Binding Proteins
Carrier Proteins
Protein Structure, Tertiary
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Saccharomyces cerevisiae Proteins
Inflammasomes
HeLa Cells
Adaptor Proteins, Signal Transducing
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
Two-Hybrid System Techniques
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
Saccharomyces cerevisiae
Membrane Proteins
Retinoblastoma-Binding Protein 7
Sequence Homology, Amino Acid
Binding Sites
Immunoprecipitation
Precipitin Tests
Drosophila Proteins
Transcription, Genetic
Models, Biological
Base Sequence
Recombinant Fusion Proteins
Proteins
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
Mutation
Nucleoside-Phosphate Kinase
Signal Transduction
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
RNA Editing
A process that changes the nucleotide sequence of mRNA from that of the DNA template encoding it. Some major classes of RNA editing are as follows: 1, the conversion of cytosine to uracil in mRNA; 2, the addition of variable number of guanines at pre-determined sites; and 3, the addition and deletion of uracils, templated by guide-RNAs (RNA, GUIDE).
Cell Cycle Proteins
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
Chromatin
Repressor Proteins
Cytoskeletal Proteins
Chromosomal Proteins, Non-Histone
Models, Molecular
Transcription Factor TFIID
The major sequence-specific DNA-binding component involved in the activation of transcription of RNA POLYMERASE II. It was originally described as a complex of TATA-BOX BINDING PROTEIN and TATA-BINDING PROTEIN ASSOCIATED FACTORS. It is now know that TATA BOX BINDING PROTEIN-LIKE PROTEINS may take the place of TATA-box binding protein in the complex.
Mass Spectrometry
RNA-Binding Proteins
Caspase 1
A long pro-domain caspase that has specificity for the precursor form of INTERLEUKIN-1BETA. It plays a role in INFLAMMATION by catalytically converting the inactive forms of CYTOKINES such as interleukin-1beta to their active, secreted form. Caspase 1 is referred as interleukin-1beta converting enzyme and is frequently abbreviated ICE.
PDZ Domains
Protein interaction domains of about 70-90 amino acid residues, named after a common structure found in PSD-95, Discs Large, and Zona Occludens 1 proteins. PDZ domains are involved in the recruitment and interaction of proteins, and aid the formation of protein scaffolds and signaling networks. This is achieved by sequence-specific binding between a PDZ domain in one protein and a PDZ motif in another protein.
Protein Subunits
Cell Nucleus
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Mediator Complex
A large protein complex which acts as a signaling adaptor protein that allows communication between the various regulatory and functional components of GENETIC TRANSCRIPTION including DNA POLYMERASE II; GENERAL TRANSCRIPTION FACTORS; and TRANSCRIPTION FACTORS that are bound to upstream ENHANCER ELEMENTS. The mediator complex was originally studied in YEAST where at least 21 subunits were identified. Many of the yeast subunits are homologs to proteins in higher organisms that are found associated with specific nuclear receptors such as THYROID HORMONE RECEPTORS and VITAMIN D RECEPTORS.
Immunoblotting
Protein Transport
Trans-Activators
Protein Multimerization
Phosphorylation
LIM Domain Proteins
A large class of structurally-related proteins that contain one or more LIM zinc finger domains. Many of the proteins in this class are involved in intracellular signaling processes and mediate their effects via LIM domain protein-protein interactions. The name LIM is derived from the first three proteins in which the motif was found: LIN-11, Isl1 and Mec-3.
Host Cell Factor C1
A cellular transcriptional coactivator that was originally identified by its requirement for the stable assembly IMMEDIATE-EARLY PROTEINS of the HERPES SIMPLEX VIRUS. It is a nuclear protein that is a transcriptional coactivator for a number of transcription factors including VP16 PROTEIN; GA-BINDING PROTEIN; EARLY GROWTH RESPONSE PROTEIN 2; and E2F4 TRANSCRIPTION FACTOR. It also interacts with and stabilizes HERPES SIMPLEX VIRUS PROTEIN VMW65 and helps regulate GENETIC TRANSCRIPTION of IMMEDIATE-EARLY GENES in HERPES SIMPLEX VIRUS.
Sequence Alignment
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Histone Acetyltransferases
Multienzyme Complexes
Chromatography, Affinity
Promoter Regions, Genetic
Histone Deacetylases
Deacetylases that remove N-acetyl groups from amino side chains of the amino acids of HISTONES. The enzyme family can be divided into at least three structurally-defined subclasses. Class I and class II deacetylases utilize a zinc-dependent mechanism. The sirtuin histone deacetylases belong to class III and are NAD-dependent enzymes.
Amino Acid Motifs
Transcriptional Activation
Polycomb Repressive Complex 1
Herpes Simplex Virus Protein Vmw65
Electrophoresis, Polyacrylamide Gel
Nuclear Matrix-Associated Proteins
Transfection
RNA Interference
A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.
Drosophila
CARD Signaling Adaptor Proteins
A family of intracellular signaling adaptor proteins that contain caspase activation and recruitment domains. Proteins that contain this domain play a role in APOPTOSIS-related signal transduction by associating with other CARD domain-containing members and in activating INITIATOR CASPASES that contain CARD domains within their N-terminal pro-domain region.
TATA-Binding Protein Associated Factors
RNA, Protozoan
Cloning, Molecular
Trypanosoma brucei brucei
HSP90 Heat-Shock Proteins
Protein Conformation
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Drosophila melanogaster
DNA
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Protein Structure, Quaternary
Blotting, Western
Transcription Factors, TFII
The so-called general transcription factors that bind to RNA POLYMERASE II and that are required to initiate transcription. They include TFIIA; TFIIB; TFIID; TFIIE; TFIIF; TFIIH; TFII-I; and TFIIJ. In vivo they apparently bind in an ordered multi-step process and/or may form a large preinitiation complex called RNA polymerase II holoenzyme.
Peptide Hydrolases
Histones
Ubiquitin-Protein Ligases
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
Adherens Junctions
Anchoring points where the CYTOSKELETON of neighboring cells are connected to each other. They are composed of specialized areas of the plasma membrane where bundles of the ACTIN CYTOSKELETON attach to the membrane through the transmembrane linkers, CADHERINS, which in turn attach through their extracellular domains to cadherins in the neighboring cell membranes. In sheets of cells, they form into adhesion belts (zonula adherens) that go all the way around a cell.
Protein Interaction Domains and Motifs
Gene Expression Regulation
TATA-Box Binding Protein
A general transcription factor that plays a major role in the activation of eukaryotic genes transcribed by RNA POLYMERASES. It binds specifically to the TATA BOX promoter element, which lies close to the position of transcription initiation in RNA transcribed by RNA POLYMERASE II. Although considered a principal component of TRANSCRIPTION FACTOR TFIID it also takes part in general transcription factor complexes involved in RNA POLYMERASE I and RNA POLYMERASE III transcription.
Glutathione Transferase
Histone-Lysine N-Methyltransferase
Octamer Transcription Factor-1
Microscopy, Fluorescence
Microtubule-Associated Proteins
p300-CBP Transcription Factors
A family of histone acetyltransferases that is structurally-related to CREB-BINDING PROTEIN and to E1A-ASSOCIATED P300 PROTEIN. They function as transcriptional coactivators by bridging between DNA-binding TRANSCRIPTION FACTORS and the basal transcription machinery. They also modify transcription factors and CHROMATIN through ACETYLATION.
Cell Membrane
Acetyltransferases
Cytoplasm
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Dimerization
RNA, Messenger
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Kinetochores
DNA, Complementary
Proteasome Endopeptidase Complex
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
Polycomb-Group Proteins
DNA Helicases
Proteins that catalyze the unwinding of duplex DNA during replication by binding cooperatively to single-stranded regions of DNA or to short regions of duplex DNA that are undergoing transient opening. In addition DNA helicases are DNA-dependent ATPases that harness the free energy of ATP hydrolysis to translocate DNA strands.
DNA Repair
The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.
A Kinase Anchor Proteins
A structurally-diverse family of intracellular-signaling adaptor proteins that selectively tether specific protein kinase A subtypes to distinct subcellular sites. They play a role in focusing the PROTEIN KINASE A activity toward relevant substrates. Over fifty members of this family exist, most of which bind specifically to regulatory subunits of CYCLIC AMP-DEPENDENT PROTEIN KINASE TYPE II such as CAMP PROTEIN KINASE RIIALPHA or CAMP PROTEIN KINASE RIIBETA.
Ubiquitins
Cells, Cultured
Intracellular Signaling Peptides and Proteins
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
Protein-Serine-Threonine Kinases
Protein Structure, Secondary
RNA, Small Interfering
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
Phenotype
Protein Stability
beta Catenin
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
Nucleosomes
Tumor Suppressor Proteins
Interleukin-1beta
HEK293 Cells
Molecular Chaperones
Plasmids
Mitosis
Cadherins
Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.
COS Cells
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
Adenosine Triphosphatases
Ligases
Models, Genetic
Crystallography, X-Ray
Cell Cycle
The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.
Fluorescence Resonance Energy Transfer
Yeasts
Actins
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
Gene Deletion
Enhancer Elements, Genetic
Proto-Oncogene Proteins
Microfilament Proteins
Schizosaccharomyces pombe Proteins
Cricetinae
Vesicular Transport Proteins
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
Protein Kinases
TOR Serine-Threonine Kinases
A serine threonine kinase that controls a wide range of growth-related cellular processes. The protein is referred to as the target of RAPAMYCIN due to the discovery that SIROLIMUS (commonly known as rapamycin) forms an inhibitory complex with TACROLIMUS BINDING PROTEIN 1A that blocks the action of its enzymatic activity.
Neoplasm Proteins
Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm.
Cross-Linking Reagents
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
Centromere
Jurkat Cells
RNA Polymerase II
Arabidopsis Proteins
Homeodomain Proteins
CHO Cells
Genetic Complementation Test
Sp1 Transcription Factor
Chromatin Immunoprecipitation
A technique for identifying specific DNA sequences that are bound, in vivo, to proteins of interest. It involves formaldehyde fixation of CHROMATIN to crosslink the DNA-BINDING PROTEINS to the DNA. After shearing the DNA into small fragments, specific DNA-protein complexes are isolated by immunoprecipitation with protein-specific ANTIBODIES. Then, the DNA isolated from the complex can be identified by PCR amplification and sequencing.
Sodium-Hydrogen Antiporter
Peptides
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
Conserved Sequence
Tight Junctions
Ubiquitin
A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
HSP70 Heat-Shock Proteins
src Homology Domains
Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.
RNA Splicing
Endoplasmic Reticulum
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
Gene Expression Regulation, Fungal
Apoptosis Regulatory Proteins
Calcium-Binding Proteins
Green Fluorescent Proteins
Chromatography, Gel
Microscopy, Confocal
DNA Primers
Membrane Microdomains
Substrate Specificity
Cytoskeleton
Mutagenesis, Site-Directed
Enzyme Activation
Arabidopsis
Amyloid Precursor Protein Secretases
Mice, Knockout
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
Microtubules
Self-regulated polymerization of the actin-related protein Arp1. (1/5719)
The actin-related protein Arp1 (or centractin, actin RPV) is the major subunit of dynactin, a key component of the cytoplasmic dynein motor machinery [1] [2] [3]. Of the ubiquitously expressed members of the Arp superfamily, Arp1 is most similar to conventional actin [4] [5] [6] and, on the basis of conserved sequence features, is predicted to bind ATP and possibly polymerize. In vivo, all cytosolic Arp1 sediments at 20S [7] suggesting that it assembles into oligomers, most likely dynactin - a multiprotein complex known to contain eight or nine Arp1 monomers in a 37 nm filament [8]. The uniform length of Arp1 polymers suggests a novel assembly mechanism that may be governed by a 'ruler' activity. In dynactin, the Arp1 filament is bounded by actin-capping protein at one end and a heterotetrameric protein complex containing the p62 subunit (D.M. Eckley, S.R. Gill, J.B.B., J.E. Heuser, T.A.S., unpublished observations) at the other [8]. In the present study, we analyzed the behavior of highly purified, native Arp1. Arp1 was found to polymerize rapidly into short filaments that were similar, but not identical, in length to those in dynactin. With time, these filaments appeared to anneal to form longer assemblies but never attained the length of conventional actin filaments. (+info)A steroid receptor coactivator, SRA, functions as an RNA and is present in an SRC-1 complex. (2/5719)
Nuclear receptors play critical roles in the regulation of eukaryotic gene expression. We report the isolation and functional characterization of a novel transcriptional coactivator, termed steroid receptor RNA activator (SRA). SRA is selective for steroid hormone receptors and mediates transactivation via their amino-terminal activation function. We provide functional and mechanistic evidence that SRA acts as an RNA transcript; transfected SRA, unlike other steroid receptor coregulators, functions in the presence of cycloheximide, and SRA mutants containing multiple translational stop signals retain their ability to activate steroid receptor-dependent gene expression. Biochemical fractionation shows that SRA exists in distinct ribonucleoprotein complexes, one of which contains the nuclear receptor coactivator steroid receptor coactivator 1. We suggest that SRA may act to confer functional specificity upon multiprotein complexes recruited by liganded receptors during transcriptional activation. (+info)The N-terminal transactivation domain of ATF2 is a target for the co-operative activation of the c-jun promoter by p300 and 12S E1A. (3/5719)
The adenovirus E1A proteins activate the c-jun promoter through two Jun/ATF-binding sites, jun1 and jun2. P300, a transcriptional coactivator of several AP1 and ATF transcription factors has been postulated to play a role in this activation. Here, we present evidence that p300 can control c-jun transcription by acting as a cofactor for ATF2: (1) Over-expression of p300 was found to stimulate c-jun transcription both in the presence and absence of E1A. (2) Like E1A, p300 activates the c-jun promoter through the junl and jun2 elements and preferentially activates the N-terminal domain of ATF2. (3) Co-immunoprecipitation assays of crude cell extracts indicate that endogenous p300/CBP(-like) proteins and ATF2 proteins are present in a multiprotein complex that can bind specifically to the jun2 element. We further demonstrate that the Stress-Activated-Protein-Kinase (SAPK) target sites of ATF2, Thr69 and Thr71 are not required for the formation of the p300/CBP-ATF2 multiprotein complex. These data indicate that E1A does not inhibit all transcription activation functions of p300, and, in fact, cooperates with p300 in the activation of the ATF2 N-terminus. (+info)Arabidopsis FUSCA5 encodes a novel phosphoprotein that is a component of the COP9 complex. (4/5719)
The COP9 complex is a regulator essential for repression of light-mediated development in Arabidopsis. Using partial amino acid sequence data generated from purified COP9 complexes, we cloned the Arabidopsis cDNA encoding the 27-kD subunit of the COP9 complex and showed that it is encoded by the previously identified FUSCA5 (FUS5) locus. fus5 mutants exhibit constitutive photomorphogenic phenotypes similar to those of cop9 and fus6. Point mutations in FUS5 that led to a loss of FUS5 protein were detected in four fus5 allelic strains. FUS5 contains the PCI/PINT and mitogen-activated protein kinase kinase activation loop motifs and is highly conserved with the mammalian COP9 complex subunit 7 and the Aspergillus nidulans AcoB proteins. FUS5 is present in both complex and monomeric forms. In the COP9 complex, FUS5 may interact directly with FUS6 and COP9. Mutations in FUS6 and COP9 result in a shift in the electrophoretic mobility of FUS5. This shift can be mimicked by in vitro phosphorylation of FUS5 by plant extracts. These findings further support the hypothesis that the COP9 complex is a central and common regulator that may interact with multiple signaling pathways. (+info)Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. (5/5719)
Recently we identified a novel human (h) multiprotein complex, called TATA-binding protein (TBP)-free TAFII-containing complex (TFTC), which is able to nucleate RNA polymerase II transcription and can mediate transcriptional activation. Here we demonstrate that TFTC, similar to other TBP-free TAFII complexes (yeast SAGA, hSTAGA, and hPCAF) contains the acetyltransferase hGCN5 and is able to acetylate histones in both a free and a nucleosomal context. The recently described TRRAP cofactor for oncogenic transcription factor pathways was also characterized as a TFTC subunit. Furthermore, we identified four other previously uncharacterized subunits of TFTC: hADA3, hTAFII150, hSPT3, and hPAF65beta. Thus, the polypeptide composition of TFTC suggests that TFTC is recruited to chromatin templates by activators to acetylate histones and thus may potentiate initiation and activation of transcription. (+info)Maternal histone deacetylase is accumulated in the nuclei of Xenopus oocytes as protein complexes with potential enzyme activity. (6/5719)
Reversible acetylation of core histones plays an important regulatory role in transcription and replication of chromatin. The acetylation status of chromatin is determined by the equilibrium between activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). The Xenopus protein HDACm shows sequence homology to other putative histone deacetylases, but its mRNA is expressed only during early development. Both HDACm protein and acetylated non-chromosomal histones are accumulated in developing oocytes, indicating that the key components for histone deposition into new chromatin during blastula formation are in place by the end of oogenesis. Here we show that the 57 kDa HDACm protein undergoes steady accumulation in the nucleus, where it is organized in a multiprotein complex of approx. 300 kDa. A second, major component of the nuclear complex is the retinoblastoma-associated protein p48 (RbAp48/46), which may be used as an adaptor to contact acetylated histones in newly assembled chromatin. The nuclear complex has HDAC activity that is sensitive to trichostatin A, zinc ions and phosphatase treatment. The 57 kDa protein serves as a marker for total HDAC activity throughout oogenesis and early embryogenesis. The active HDACm complex and its acetylated histone substrates appear to be kept apart until after chromatin assembly has taken place. However, recombinant HDACm, injected into the cytoplasm of oocytes, not only is translocated to the nucleus, but also is free to interact with the endogenous chromatin. (+info)Myb-related fission yeast cdc5p is a component of a 40S snRNP-containing complex and is essential for pre-mRNA splicing. (7/5719)
Myb-related cdc5p is required for G(2)/M progression in the yeast Schizosaccharomyces pombe. We report here that all detectable cdc5p is stably associated with a multiprotein 40S complex. Immunoaffinity purification has allowed the identification of 10 cwf (complexed with cdc5p) proteins. Two (cwf6p and cwf10p) are members of the U5 snRNP; one (cwf9p) is a core snRNP protein. cwf8p is the apparent ortholog of the Saccharomyces cerevisiae splicing factor Prp19p. cwf1(+) is allelic to the prp5(+) gene defined by the S. pombe splicing mutant, prp5-1, and there is a strong negative genetic interaction between cdc5-120 and prp5-1. Five cwfs have not been recognized previously as important for either pre-mRNA splicing or cell cycle control. Further characterization of cwf1p, cwf2p, cwf3p, and cwf4p demonstrates that they are encoded by essential genes, cosediment with cdc5p at 40S, and coimmunoprecipitate with cdc5p. We further show that cdc5p associates with the U2, U5, and U6 snRNAs and that cells lacking cdc5(+) function are defective in pre-mRNA splicing. These data raise the possibility that the cdc5p complex is an intermediate in the assembly or disassembly of an active S. pombe spliceosome. (+info)Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. (8/5719)
Genetic screens for modifiers of activated Ras phenotypes have identified a novel protein, kinase suppressor of Ras (KSR), which shares significant sequence homology with Raf family protein kinases. Studies using Drosophila melanogaster and Caenorhabditis elegans predict that KSR positively regulates Ras signaling; however, the function of mammalian KSR is not well understood. We show here that two predicted kinase-dead mutants of KSR retain the ability to complement ksr-1 loss-of-function alleles in C. elegans, suggesting that KSR may have physiological, kinase-independent functions. Furthermore, we observe that murine KSR forms a multimolecular signaling complex in human embryonic kidney 293T cells composed of HSP90, HSP70, HSP68, p50(CDC37), MEK1, MEK2, 14-3-3, and several other, unidentified proteins. Treatment of cells with geldanamycin, an inhibitor of HSP90, decreases the half-life of KSR, suggesting that HSPs may serve to stabilize KSR. Both nematode and mammalian KSRs are capable of binding to MEKs, and three-point mutants of KSR, corresponding to C. elegans loss-of-function alleles, are specifically compromised in MEK binding. KSR did not alter MEK activity or activation. However, KSR-MEK binding shifts the apparent molecular mass of MEK from 44 to >700 kDa, and this results in the appearance of MEK in membrane-associated fractions. Together, these results suggest that KSR may act as a scaffolding protein for the Ras-mitogen-activated protein kinase pathway. (+info)
Mutations in the Drosophila Condensin Subunit dCAP-G | Genetics
Function of mTOR complex 1 and 2 in skeletal muscle - edoc
Dr1-associated corepressor
We are witnessing tremendous improvements in our understanding of the organization | High-Throughput Screen for the Chemical...
HOS1 - Histone deacetylase HOS1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Bakers yeast) - HOS1 gene & protein
Histone deacetylase 11
TumorPortal
Condensin complex subunit 1 (zebrafish) | Protein Target - PubChem
Ncapg2 MGI Mouse Gene Detail - MGI:1923294 - non-SMC condensin II complex, subunit G2
Binding Specificity of Multiprotein Signaling Complexes Is Determined by Both Cooperative Interactions and Affinity Preferences...
Multi-protein assemblies - Proteopedia, life in 3D
TOR Complexes and the Maintenance of Cellular Homeostasis
Search Articles | University of Toronto Libraries
CSN5B - COP9 signalosome complex subunit 5b - Arabidopsis thaliana (Mouse-ear cress) - CSN5B gene & protein
Multiple roles of Condensins: a complex story. - Semantic Scholar
The condensin complex is a mechanochemical motor that translocates along DNA | Science
Genome-wide identification and analysis of WD40 proteins in wheat ( Triticum aestivum L.) | BMC Genomics | Full Text
AT1G35560 protein (Arabidopsis thaliana) - STRING network view
BRG-1 Is Recruited to Estrogen-Responsive Promoters and Cooperates with Factors Involved in Histone Acetylation | Molecular and...
Condensin subunit 1 (IPR007673) | InterPro | EMBL-EBI
COPS7B Polyclonal Antibody, Biotin Conjugated | EpiGentek
Losada, Ana Publications - CSHL Scientific Digital Repository
Nuclear condensin complex subunit 3, C-terminal domain (IPR025977) | InterPro | EMBL-EBI
NCAPG antibodies | Antibodypedia
A sugary input to leucine sensing | Science
Characterizing Cell Survival Pathways Downstream of mTORC1 in Cancer - Ilana Kelsey
mTORC1/NF-κB axis controls amino acid catabolism by regulating the expression of the key enzymes in human hepatocytes |...
JZUS - Journal of Zhejiang University SCIENCE
Placental DEPTOR as a stress sensor during pregnancy.
anti-HCAP-G antibody | GeneTex
MultiBac: Multigene Baculovirus‐Based Eukaryotic Protein Complex Production - Current Protocols
Search Articles | University of Toronto Libraries
Interaction between NBS1 and the mTOR/Rictor/SIN1 compl | Open-i
COP21大會連線 | 環境資訊中心
Predicting the structure of protein complexes: a step in the right direction
CSN3抗体(ab111406)| Abcam中国
Histone trimethylation by Set1 is coordinated by the RRM, autoinhibitory, and catalytic domains | The EMBO Journal
Import of Soluble Proteins into Chloroplasts and Potential Regulatory Mechanisms
The mammalian target of rapamycin complex 1 (mTORC1) is mixed up | Epigenetic regulation of CpG promoter methylation
In vivo dissection of the chromosome condensation machinery | JCB
RagC phosphorylation autoregulates mTOR complex 1. [Drosophila Facility] | CCAMP
The multifaceted role of mTORC1 in the control of lipid metabolism | EMBO Reports
Analyzing Large Protein Complexes by Structural Mass Spectrometry | Protocol
Die Biogenese des COP9 Signalosoms wird durch microRNAs der let-7-Familie reguliert
Anti-Human PRAS40 Antibody | Human PRAS40 Antibody | PRAS40 Antibody | AKT1S1 Antibody
Anti-Human PRAS40 Antibody | Human PRAS40 Antibody | PRAS40 Antibody | AKT1S1 Antibody
Expression pattern of the JAB1/CSN5 gene during murine embryogenesis: colocalization with NEDD8 • Research - Institut Pasteur
Study Shows Protein Complex Essential to Creating Healthy Blood Cells | NYU Langone News
Genatlas sheet
VPX mTORC1, 25 servings (BEST BY 09/15)
Both mTORC1 and mTORC2 are involved in the regulation of cell adhesion | Oncotarget
Nuclear time
ULK2抗体|Abcam中国|Anti-ULK2抗体(ab97695)
Biomolecular condensate
Gammons M, Bienz M (April 2018). "Multiprotein complexes governing Wnt signal transduction". Current Opinion in Cell Biology. ... The Dsh protein functions both in planar polarity and Wnt signalling, where it recruits another supramolecular complex (the ... An S, Kumar R, Sheets ED, Benkovic SJ (April 2008). "Reversible compartmentalization of de novo purine biosynthetic complexes ... Nakano A, Trie R, Tateishi K (January 1997). "Glycogen-Surfactant Complexes: Phase Behavior in a Water/Phytoglycogen/Sodium ...
Heterologous expression
"Baculovirus expression system for heterologous multiprotein complexes". Nature Biotechnology. 22 (12): 1583-1587. doi:10.1038/ ... Wenzel, Silke C; Müller, Rolf (2005-12-01). "Recent developments towards the heterologous expression of complex bacterial ... Through this host, it remains exceedingly challenging to heterologously express a complex, heteromultimeric metalloprotein like ...
DNA
Martinez E (December 2002). "Multi-protein complexes in eukaryotic gene transcription". Plant Molecular Biology. 50 (6): 925-47 ... Complex DNA and RNA organic compounds of life, including uracil, cytosine, and thymine, have also been formed in the laboratory ... The histones form a disk-shaped complex called a nucleosome, which contains two complete turns of double-stranded DNA wrapped ... In eukaryotes, this structure involves DNA binding to a complex of small basic proteins called histones, while in prokaryotes ...
Caspase
Multiprotein complexes often form during caspase activation. Some activating multiprotein complexes includes: The death- ... This is done by the formation of a multiprotein Death Inducing Signalling Complex (DISC) that recruits and activates a pro- ... This cellular ion imbalance leads to oligomerisation of NLRP3 molecules to form a multiprotein complex called the NLRP3 ... These proteins allow caspase-1 activation by forming a multiprotein activating complex called Inflammasomes. For example, a NOD ...
Timothy J. Richmond
"Baculovirus expression system for heterologous multiprotein complexes". Nature Biotechnology. 22 (12): 1583-1587. doi:10.1038/ ... His laborat-ory has elu-cidated the struc-tures of the nucle-osome core particle and vari-ous transcrip-tion factor complexes. ... particularly those involved in protein-DNA complexes and to relate these structures to the biological processes of chromatin ... in teach-ing and research are primar-ily devoted to the re-cog-ni-tion and assembly of biological macro-molecular complexes. X- ...
Narayanaswamy Srinivasan
"Multi-Protein Complexes Involved in Cell Regulation (E6)". Keystone Symposia. 2006. Retrieved 24 October 2016. "Scientific ... has delivered several featured lectures and keynote addresses which included the Keystone Symposium on Multiprotein Complexes ( ... "Structural and mechanistic insights into human splicing factor SF3b complex derived using an integrated approach guided by the ...
ETS1
Their interaction results in formation of multiprotein complexes. When Ets1 interacts with other transcription factors (Runx1, ... ETS1 binds with DNA-dependent protein kinase (DNA-PK) [where the DNA-PK complex is made up of DNA-PKcs and DNA repair Ku ( ...
Analytical ultracentrifugation
Balbo A, Minor KH, Velikovsky CA, Mariuzza RA, Peterson CB, Schuck P (Jan 2005). "Studying multiprotein complexes by ... by either monitoring the number and molar mass of macromolecular complexes, by gaining information about the complex ... With AUC it is possible to gain information on the number and subunit stoichiometry of non-covalent complexes and equilibrium ...
NLRP7
... via their involvement in multiprotein complexes called inflammasomes. ENSG00000167634, ENSG00000278173, ENSG00000277179, ...
Functional genomics
Most of genes are part of multi-protein complexes. This approach can be used to identify synthetic lethality by using the ... Complexes of proteins are allowed to form around a particular "bait" protein. The bait protein is identified using an antibody ... Vinayagam A, Hu Y, Kulkarni M, Roesel C, Sopko R, Mohr SE, Perrimon N (February 2013). "Protein complex-based analysis ... Affinity purification and mass spectrometry (AP/MS) is able to identify proteins that interact with one another in complexes. ...
Cluster of Excellence Frankfurt Macromolecular Complexes
"Acyl modification and binding of mitochondrial ACP to multiprotein complexes". Biochimica et Biophysica Acta (BBA) - Molecular ... A broad range of macromolecular complexes from CEF research areas A, C and D, including complex I, ATP synthase, drug ... Examples for important membrane complexes include the atomic structures of complex I and the ATP synthase of the mitochondrial ... Design of macromolecular complexes, and (E) Methods for studying macromolecular complexes. Biological membranes have a very ...
Von Willebrand factor type C domain
A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWF domains participate in ... The presence of this region in a number of other complex-forming proteins points to the possible involvement of the VWFC domain ... Fraser extracellular matrix complex subunit 1 (FRAS1) Neural EGFL like 1 (NELL1) Neural EGFL like 2 (NELL2) Peroxidasin like ( ... in complex formation. BMP binding endothelial regulator (BMPER) Cysteine-rich motor neuron 1 protein (CRIM1) Extracellular ...
Von Willebrand factor type A domain
A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWA domains participate in ...
Photosystem
Reaction centers are multi-protein complexes found within the thylakoid membrane. At the heart of a photosystem lies the ... Each photosystem has two main subunits: an antenna complex (a light harvesting complex or LHC) and a reaction center. The ... The antenna complex contains hundreds of chlorophyll molecules which funnel the excitation energy to the center of the ... Energy will be efficiently transferred from the outer part of the antenna complex to the inner part. This funneling of energy ...
NAP1L4
Rodriguez P, Ruiz MT, Price GB, Zannis-Hadjopoulos M (2005). "NAP-2 is part of multi-protein complexes in HeLa cells". J. Cell ...
CST complex
The CST complex is a cellular multiprotein complex involved in telomere maintenance. In budding yeast (Saccharomyces cerevisiae ... Sun J, Yu EY, Yang Y, Confer LA, Sun SH, Wan K, Lue NF, Lei M (December 2009). "Stn1-Ten1 is an Rpa2-Rpa3-like complex at ... It is related to the Replication protein A complex. For budding yeast as well as for mammals, CST is a protein heterotrimer, ... Lue NF, Zhou R, Chico L, Mao N, Steinberg-Neifach O, Ha T (2013). "The telomere capping complex CST has an unusual ...
Protein quaternary structure
Structural biology Nucleic acid quaternary structure Multiprotein complex Biomolecular complex Oligomers Here quaternary means ... Other assemblies referred to instead as multiprotein complexes also possess quaternary structure. Examples include nucleosomes ... In some cases, proteins form complexes that then assemble into even larger complexes. In such cases, one uses the nomenclature ... e.g., "dimer of dimers" or "trimer of dimers", to suggest that the complex might dissociate into smaller sub-complexes before ...
APBA1
Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA (April 2004). "A multiprotein trafficking complex composed of ... "Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach". EMBO J. 21 (10): 2332-42. doi: ... It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to ... Butz S, Okamoto M, Südhof TC (1998). "A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to ...
PDLIM5
LIM domain-containing proteins are scaffolds for the formation of multiprotein complexes. The proteins are involved in ... 2003). "A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels". Nat. Neurosci. 6 (5): 468-75. doi: ...
LIN7C
Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA (2004). "A multiprotein trafficking complex composed of SAP97, ... "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium ... "Synaptic multiprotein complexes associated with 5-HT(2C) receptors: a proteomic approach". EMBO J. 21 (10): 2332-42. doi: ... Bohl J, Brimer N, Lyons C, Vande Pol SB (2007). "The stardust family protein MPP7 forms a tripartite complex with LIN7 and DLG1 ...
Anammox
"The inner workings of the hydrazine synthase multiprotein complex". Nature. 527 (7578): 394-7. Bibcode:2015Natur.527..394D. doi ... At the same time, nitrite is reduced to hydroxylamine at the cytoplasmic site of the same enzyme complex responsible for ... In general, two possible reaction mechanisms are addressed: One mechanism hypothesizes that a membrane-bound enzyme complex ... ammonium and hydroxylamine are converted to hydrazine by a membrane-bound enzyme complex, hydrazine is oxidized in the ...
Origin recognition complex
Bell SP, Stillman B (May 1992). "ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex ... First, the ORC, Noc3p and Cdc6 form a complex on origin DNA (marked by ARS type regions). New ORC/Noc3/Cdc6 complexes then ... Unlike eukaryotic Orc, they do not always form a complex. In fact, they have divergent complex structures when these do form. ... In molecular biology, origin recognition complex (ORC) is a multi-subunit DNA binding complex (6 subunits) that binds in all ...
Protein complex
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are ... Protein complex formation can activate or inhibit one or more of the complex members and in this way, protein complex formation ... Such protein complexes are called "obligate protein complexes". Transient protein complexes form and break down transiently in ... Proper assembly of multiprotein complexes is important, since misassembly can lead to disastrous consequences. In order to ...
NLRP4
... via their involvement in multiprotein complexes called inflammasomes (Tschopp et al., 2003).[supplied by OMIM] GRCh38: Ensembl ...
NLRP12
... via their involvement in multiprotein complexes called inflammasomes (Tschopp et al., 2003).[supplied by OMIM] GRCh38: Ensembl ...
NABP1
"HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response". The Journal of Biological ... Huang J, Gong Z, Ghosal G, Chen J (August 2009). "SOSS complexes participate in the maintenance of genomic stability". ... "Streamlined analysis schema for high-throughput identification of endogenous protein complexes". Proceedings of the National ...
Lori Passmore
She is known for her work on multiprotein complexes involved in gene expression. and development of new supports for cryo-EM. ... Her group uses in vitro reconstitution, biochemical assays and cryo-EM to understand the function of multiprotein complexes ... She performed in vitro biochemical characterisation of the activity of the anaphase-promoting complex (APC) and used cryo-EM to ... Rajendra E, Garaycoechea JI, Patel KJ, Passmore LA (2014). "Abundance of the Fanconi anaemia core complex is regulated by the ...
Rel homology domain
Some of these transcription factors appear to form multi-protein DNA-bound complexes. Phosphorylation of the RHD appears to ...
GINS2
Takayama Y, Kamimura Y, Okawa M, Muramatsu S, Sugino A, Araki H (2003). "GINS, a novel multiprotein complex required for ... DNA replication complex GINS protein PSF2 is a protein that in humans is encoded by the GINS2 gene. GINS2 has been shown to ... "Entrez Gene: GINS2 GINS complex subunit 2 (Psf2 homolog)". Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER, Hurov KE, Luo J ...
Hsp90 inhibitor
Hsp90 acts in a multiprotein complex with several co-chaperones. One of these, cochaperone p23, appears to stabilize Hsp90- ... Finally they concluded that Hsp90, and consequently signaling mediated by client proteins in the Hsp90 multiprotein complex, ... Geldanamycin and radicicol tightly bind to this pocket and prevent the release of protein from chaperone complex. Thus the ... Mitochondrial Hsp90 is involved in complex signaling pathway that prevents initiation of induced apoptosis. Gamitrinib is a ...
WIPI2
They regulate the assembly of multiprotein complexes by presenting a beta-propeller platform for simultaneous and reversible ...
Interferon
... a highly conserved multiprotein complex implicated in protein deneddylation, deubiquitination, and phosphorylation. RIG-G has ... Interferon type I: All type I IFNs bind to a specific cell surface receptor complex known as the IFN-α/β receptor (IFNAR) that ... As a result, an IFN-stimulated gene factor 3 (ISGF3) complex forms-this contains STAT1, STAT2 and a third transcription factor ... Interferon type III: Signal through a receptor complex consisting of IL10R2 (also called CRF2-4) and IFNLR1 (also called CRF2- ...
Tetratricopeptide repeat protein 39B
Most TPR-containing proteins are associated with multiprotein complexes, and there is extensive evidence indicating that TPR ... Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S (January 2011). "Structure of human O-GlcNAc transferase and its complex with a ... motifs are important to the functioning of chaperone, cell-cycle, transcription, and protein transport complexes. Two more TPR ...
SF3B1
... forms the U2 small nuclear ribonucleoproteins complex (U2 snRNP). The splicing factor 3b/3a complex binds pre-mRNA upstream of ... Golas MM, Sander B, Will CL, Lührmann R, Stark H (May 2003). "Molecular architecture of the multiprotein splicing factor SF3b ... This gene encodes subunit 1 of the splicing factor 3b protein complex. Splicing factor 3b, together with splicing factor 3a and ... Das BK, Xia L, Palandjian L, Gozani O, Chyung Y, Reed R (October 1999). "Characterization of a protein complex containing ...
DSN1
... along with MIS12, DC8, PMF1, CBX5, ZWINT is a component of the kinetochore-associated multiprotein complex which is ... DSN1, MIND kinetochore complex component, homolog (S. cerevisiae), also known as DSN1 or MIS13, is a protein which in humans ... "Entrez Gene: DSN1 DSN1, MIND kinetochore complex component, homolog (S. cerevisiae)". Obuse C, Iwasaki O, Kiyomitsu T, Goshima ... 2004). "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1". Nat. Cell ...
Short interspersed nuclear element
Thereafter, one of the strands is incorporated into a multi-protein RNA-induced silencing complex (RISC). Among these proteins ... This complex is responsible for cleaving some of the hair-pin structures from the pre-microRNA which is transported to the ... Alternately, some SINEs are believed to use a much more complex system of integrating back into the genome; this system ... The chromosome has a very complex and hierarchical system of organizing the genome. This system of organization, which includes ...
Bacteriotherapy
Probiotics also help strengthen tight junctions, multiprotein complexes lining the intestines (as well as other organs and ...
COG7
Conserved oligomeric Golgi complex subunit 7 is a protein that in humans is encoded by the COG7 gene. Multiprotein complexes ... Several complexes have been identified, including the Golgi transport complex (GTC), the LDLC complex, which is involved in ... These 3 complexes are identical and have been termed the conserved oligomeric Golgi (COG) complex, which includes COG7 (Ungar ... Loh E, Hong W (2002). "Sec34 is implicated in traffic from the endoplasmic reticulum to the Golgi and exists in a complex with ...
Adapter molecule crk
"CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2 ... "Characterization of the CIN85 adaptor protein and identification of components involved in CIN85 complexes". Biochem. Biophys. ... stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T ...
Intestinal epithelium
Adherens junctions, also called zonula adherens, are multiprotein complexes formed by proteins of the catenin and cadherin ... The molecular structure of this complex is in the form of a hexamer. The complex, which is embedded in the cell membranes of ... These complexes, formed primarily of members of the claudin and the occludin families, consist of about 35 different proteins, ... These complexes, consisting of transmembrane adhesion proteins of the cadherin family, link adjacent cells together through ...
COG8
Conserved oligomeric Golgi complex subunit 8 is a protein that in humans is encoded by the COG8 gene. Multiprotein complexes ... Several complexes have been identified, including the Golgi transport complex (GTC), the LDLC complex, which is involved in ... These 3 complexes are identical and have been termed the conserved oligomeric Golgi complex (COG), which includes COG8 (Ungar ... Whyte JR, Munro S (2001). "The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes ...
Carla Koehler
During her postdoctoral research, she worked on multi protein complexes of the translocase of the outer membrane. She ... complexes. By understanding these biological pathways, Koehler looks to better understand the dysfunction in mitochondria that ...
TATA box
RNA polymerase II is then recruited to this multi-protein complex with the help of TFIIF. Additional transcription factors then ... TFIID first binds to the TATA box, facilitated by TFIIA binding to the upstream part of the TFIID complex. TFIIB then binds to ... When promoters use the SAGA/TATA box complex to recruit RNA polymerase II, they are more highly regulated and display higher ... Formation of the preinitiation complex begins when the multi-subunit transcription factor II D (TFIID) binds to the TATA box at ...
MSin3 interaction domain
Action of histone deacetylase 1 and 2 (HDAC1/2) is induced by the interaction of mSin3A with a multi-protein complex containing ...
Epigenomics
HATs are part of a multiprotein complex that is recruited to chromatin when activators bind to DNA binding sites. Acetylation ... The SWI/SNF protein complex in yeast is one example of a chromatin remodeling complex that regulates the expression of many ... In eukaryotes, genomic DNA is coiled into protein-DNA complexes called chromatin. Histones, which are the most prevalent type ... The nucleosome remodeling complexes reposition nucleosomes by several mechanisms, enabling or disabling accessibility of ...
Mediator (coactivator)
Mediator is a multiprotein complex that functions as a transcriptional coactivator in all eukaryotes. It was discovered in 1990 ... Mediator complexes interact with transcription factors and RNA polymerase II. The main function of mediator complexes is to ... A more realistic model of a mediator complex without the CDK module is shown in the second figure. The mediator complex is ... the mediator complex undergoes a compositional change in which the kinase module dissociates from the complex to allow ...
IZUMO1
Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm. Molecular reproduction and ... "Izumo is part of a multiprotein family whose members form large complexes on mammalian sperm". Molecular Reproduction and ...
TGS1
"Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex". Mol. Cell. 16 (5): 789-98 ... "Identification of a transcriptionally active peroxisome proliferator-activated receptor α-interacting cofactor complex in rat ...
WD repeat domain 18
... which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of ... WDR18 forms a nucleolar complex with LAS1L, PELP1, TEX10 called the rixosome which is involved in RNA degradation. The rixosome ... Recruitment of the rixosome by the Polycomb Repressive Complex 1 has been proposed to lead to its functioning in establishing ... Shipkovenska G, Durango A, Kalocsay M, Gygi SP, Moazed D (June 2020). "A conserved RNA degradation complex required for ...
Synthetic rescue
... mutation occurs in two residues that are closely located in the tridimensional structure of the multi-protein complex. As thus ... Complex networks Gene therapy Suppressor mutation Synthetic lethality Motter, Adilson E; Gulbahce, Natali; Almaas, Eivind; ... A compensatory mutation in another component of the protein complex can then suppress the deleterious phenotype by re- ... Interaction-mediated suppression occurs when a deleterious mutation in a component of a protein complex destabilizes the ...
Centromere
The physical role of the centromere is to act as the site of assembly of the kinetochores - a highly complex multiprotein ... are linked along their length by the action of the cohesin complex. It is now believed that this complex is mostly released ... The centromeric DNA is normally in a heterochromatin state, which is essential for the recruitment of the cohesin complex that ...
PTK2
Gan B, Yoo Y, Guan JL (December 2006). "Association of focal adhesion kinase with tuberous sclerosis complex 2 in the ... FAK is typically located at structures known as focal adhesions, which are multi-protein structures that link the extracellular ... Schlaepfer DD, Broome MA, Hunter T (March 1997). "Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: ... "Cell adhesion kinase beta forms a complex with a new member, Hic-5, of proteins localized at focal adhesions". The Journal of ...
TRIC
... may refer to: TRiC (complex), a multiprotein complex of eukaryotic cells involved in protein folding Tahoe Reno Industrial ...
Nucleoprotein
Deoxyribonucleoproteins in this kind of complex interact to generate a multiprotein regulatory complex in which the intervening ... A deoxyribonucleoprotein (DNP) is a complex of DNA and protein. The prototypical examples are nucleosomes, complexes in which ... is a complex of ribonucleic acid and RNA-binding protein. These complexes play an integral part in a number of important ... Each RNP carries with it an RNA polymerase complex. When the nucleoprotein binds to the viral RNA, it is able to expose the ...
Focal adhesion
Many of these focal complexes fail to mature and are disassembled as the lamellipodia withdraw. However, some focal complexes ... Focal adhesions are integrin-containing, multi-protein structures that form mechanical links between intracellular actin ... Initially, small (0.25μm²) focal adhesions called focal complexes (FXs) are formed at the leading edge of the cell in ... Focal adhesions are large, dynamic protein complexes through which the cytoskeleton of a cell connects to the ECM. They are ...
Anti-VGKC-complex encephalitis
... belong to a multiprotein complex. Some of the proteins which associates to the channel directly/indirectly include, but are not ... Anti-VGKC-complex encephalitis are caused by antibodies against the voltage gated potassium channel-complex (VGKC-complex) and ... VGKC-complex autoimmune encephalitis is an example of the latter form. Antibodies directed against VGKC were first reported in ... 2010). "Disruption of LGI1-linked synaptic complex causes abnormal synaptic transmission and epilepsy". Proc Natl Acad Sci U S ...
Multiprotein signalling complexes: regional assembly on heparan sulphate | Biochemical Society Transactions | Portland Press
Multiprotein signalling complexes: regional assembly on heparan sulphate J.T. Gallagher J.T. Gallagher 1 ... J.T. Gallagher; Multiprotein signalling complexes: regional assembly on heparan sulphate. Biochem Soc Trans 1 June 2006; 34 (3 ... composite sulphated region, domain structure, fibroblast growth factor, heparan sulphate, K5 lyase, multiprotein signalling ... diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes ...
Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity<...
Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity. In: ... Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity. / Ardehali, ... Ardehali H, Chen Z, Ko Y, Mejía-Alvarez R, Marbán E. Multiprotein complex containing succinate dehydrogenase confers ... title = "Multiprotein complex containing succinate dehydrogenase confers mitochondrial ATP-sensitive K+ channel activity", ...
Multiprotein Complexes - Mediator Complex | CU Experts | CU Boulder
Multiprotein Complexes - Cyclin-Dependent Kinase 8 PubMed MeSh Term * Multiprotein Complexes - Mediator Complex Subunit 1 ... Multiprotein Complexes - Mediator Complex PubMed MeSh Term *Overview. Overview. subject area of * Activating RNAs associate ... The Mediator complex and transcription regulation Journal Article * The SCF-Fbw7 ubiquitin ligase degrades MED13 and MED13L and ... The human Mediator complex: a versatile, genome-wide regulator of transcription Journal Article ...
Multiprotein signalling complexes: regional assembly on heparan sulphate | Biochemical Society Transactions | Portland Press
Multiprotein signalling complexes: regional assembly on heparan sulphate J.T. Gallagher J.T. Gallagher 1 ... J.T. Gallagher; Multiprotein signalling complexes: regional assembly on heparan sulphate. Biochem Soc Trans 1 June 2006; 34 (3 ... composite sulphated region, domain structure, fibroblast growth factor, heparan sulphate, K5 lyase, multiprotein signalling ... diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes ...
ccp4bb] Post-doctoral position in cryo-EM/structural biology of multiprotein signalling complexes
... *To: [email protected] ... Subject: [ccp4bb] Post-doctoral position in cryo-EM/structural biology of multiprotein signalling complexes ...
HBB gene: MedlinePlus Genetics
mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered...
Multiprotein Complexes / metabolism * Mutation * Peptide Chain Initiation, Translational* * Phorbol Esters / pharmacology * ... which is then recruited into the complex in a phosphorylation-dependent manner. Thus, the eIF3 preinitiation complex acts as a ... We show that mTOR and S6K1 maneuver on and off the eukaryotic initiation factor 3 (eIF3) translation initiation complex in a ... When inactive, S6K1 associates with the eIF3 complex, while the S6K1 activator mTOR/raptor does not. Cell stimulation promotes ...
Structural alignment software - Wikipedia
Keloid and Hypertrophic Scar Treatment & Management: Medical Care, Prevention, Standard Treatments
A multi‐protein complex from Myxococcus xanthus required for bacterial gliding motility - Texas A&M University (TAMU) Scholar
... ... A multi‐protein complex from Myxococcus xanthus required for bacterial gliding motility Academic Article * ... In this study, we used biochemistry and cell biology analyses to identify multi-protein complexes associated with A-motility. ... These proteins, important for the correct localization of AgmU and AglZ, appear to be organized as a motility complex, spanning ...
PDB 3TDU | Chain N-TERMINAL ACETYLATION ACTS AS AN AVIDITY ENHANCER WITHIN AN INTERCONNECTED MULTIPROTEIN COMPLEX: STRUCTURE OF...
N-TERMINAL ACETYLATION ACTS AS AN AVIDITY ENHANCER WITHIN AN INTERCONNECTED MULTIPROTEIN COMPLEX: STRUCTURE OF A HUMAN CUL1WHB ... N-TERMINAL ACETYLATION ACTS AS AN AVIDITY ENHANCER WITHIN AN INTERCONNECTED MULTIPROTEIN COMPLEX: STRUCTURE OF A HUMAN CUL1WHB ... N-TERMINAL ACETYLATION ACTS AS AN AVIDITY ENHANCER WITHIN AN INTERCONNECTED MULTIPROTEIN COMPLEX: STRUCTURE OF A HUMAN CUL1WHB ... NGL viewer: web-based molecular graphics for large complexes. Bioinformatics: bty419, 2018. doi:10.1093/bioinformatics/bty419 ...
Frontiers | The TSC Complex-mTORC1 Axis: From Lysosomes to Stress Granules and Back
In contrast, molecular details on lysosomal recruitment of the TSC complex have emerged only recently. The TSC complex subunit ... In response to nutrient shortage and stresses, the TSC complex inhibits the mechanistic target of rapamycin complex 1 (mTORC1) ... In response to nutrient shortage and stresses, the TSC complex inhibits the mechanistic target of rapamycin complex 1 (mTORC1) ... In this mini-review, we integrate the molecular mechanisms of lysosome and SG recruitment of the TSC complex. We discuss their ...
Structural basis for microtubule recognition by the human kinetochore Ska complex | Nature Communications
Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix ... The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind ... This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. ... explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules. Kinetochores must interact ...
Bobby Brooke Herrera, Ph.D. | Harvard Catalyst Profiles | Harvard Catalyst
Effect of Non-Anticoagulant N-Desulfated Heparin on Basic Fibroblast Growth Factor Expression, Angiogenesis, and Metastasis of...
They found that these effects were mediated through the formation of a specific multiprotein complex comprising B-Raf, ... O. E. Pardo, C. Wellbrock, U. K. Khanzada et al., "FGF-2 protects small cell lung cancer cells from apoptosis through a complex ... Angiogenesis, which is the process by which new blood vessels develop from preexisting vessels, is governed by a very complex ... Heparin binds to bFGF and promotes the formation of ternary complexes with endothelial cell surface receptors, inducing an ...
Protein Structure and Folding
However, methods suitable for screening multiprotein complexes (e.g. those composed of three or more different components) have ... Here, we explored an approach that uses reconstituted multiprotein complexes (RMPCs). As a model system, we chose heat shock ... High-throughput screen for inhibitors of protein-protein interactions in a reconstituted heat shock protein 70 (Hsp70) complex ...
PDF) Using Molecular Simulation to Model High-Resolution Cryo-EM Reconstructions
Here, we review techniques for map interpretation and provide examples from recent studies of multi-protein complexes. ... Electron cryo-microscopy (cryoEM) is used to determine structures of biological molecules, including multi-protein complexes. ... all-atom molecular dynamics simulations of the ribosome-tRNAs-mRNA-EFG complex were performed. The complex at the post- ... MDFF) to produce more accurate models of the ternary complex bound. to the ribosome (Trabuco et al., 2008; Villa et al., 2009 ...
Structural Biochemistry/Protein sequence determination techniques/Mass Spectroscopy - Wikibooks, open books for an open world
1. Isolate membrane protein complexes by antibody purification: Best for identifying multiprotein complexes. ... 3. The complex nature of MS. Therefore, the top-down analyzes are limited to be applied to only low-throughput single-protein ... This allows the identification of protein rings and protein complex dissociation. Tandem Mass Spectrometry[edit , edit source] ... ESI-MS allows the study of the kinetics of protein complex assembly. Intermediates can be isolated as well as identified using ...
Holger Husi - Google Scholar
Proteomics of multiprotein complexes: answering fundamental questions in neuroscience. SGN Grant, H Husi ... Molecular characterization and comparison of the components and multiprotein complexes in the postsynaptic proteome. MO Collins ... Isolation of 2000‐kDa complexes of N‐methyl‐d‐aspartate receptor and postsynaptic density 95 from mouse brain. H Husi, SGN ... Proteomic analysis of NMDA receptor-adhesion protein signaling complexes. H Husi, MA Ward, JS Choudhary, WP Blackstock, SGN ...
Faculty Research & Labs | College of Medicine
Biology (Duluth) - Research output
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RNPS1 protein expression summary - The Human Protein Atlas
... and post-splicing multiprotein mRNP complexes. Auxiliary component of the splicing-dependent multiprotein exon junction complex ... This gene encodes a protein that is part of a post-splicing multiprotein complex involved in both mRNA nuclear export and mRNA ... The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is ... Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to ...
Vauthey Research Group - Group Members
Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins. - Laboratoire de Biologie et...
... site for phosphorylated ligands are considerably more flexible in the free form of Cks1 than they are in the Cdk2-Cks1 complex ... Cks proteins are adapter molecules that coordinate the assembly of multiprotein complexes. They share the ability to domain ... Cks proteins are adapter molecules that coordinate the assembly of multiprotein complexes. They share the ability to domain ... site for phosphorylated ligands are considerably more flexible in the free form of Cks1 than they are in the Cdk2-Cks1 complex ...
IJMS | Free Full-Text | Non-SMC Element 2 (NSMCE2) of the SMC5/6 Complex Helps to Resolve Topological Stress
The SMC5/6 complex is previously described to promote DNA double-strand breaks (DSBs) repair by sister chromatid recombination ... Despite the essential nature of the SMC5/6 complex, the versatile mechanisms by which SMC5/6 functions and its molecular ... we found that the SMC5/6 complex physically interacts with the DNA topoisomerase II α (TOP2A). We therefore propose that the ... SMC5/6 complex functions in resolving TOP2A-mediated DSB-repair intermediates generated during replication. ...
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Publications scientifiques | IGBMC
Cell Biology PhD Training Program Mentoring Faculty | NYU Langone Health
Damian C. Ekiert, PhD-how large multiprotein complexes transport lipids between membranes. Niels Ringstad, PhD-membrane ... Gregory David, PhD-the role of the Sin3 histone deacetylation complex in maintenance of genome integrity. Danny Reinberg, PhD- ... Karim-Jean Armache, PhD-structural approaches to study how gene-silencing complexes repress transcription. ...
ProteinsSubunitInflammasomesMitochondrialMulti-protein complexMolecularStructuralCharacterizationEukaryoticCoordinateAssemblyProtein complexFunctionalMonomersTranscriptionProteasomeBiochemistryStimulationEIF3PhosphorylationRegulateBindsInteractionsLargeInteractsSynthesisInterplayFormationModelsChromosomeCommonStructuresDomainInactiveAxisSignalsHuman
Proteins22
- These proteins, important for the correct localization of AgmU and AglZ, appear to be organized as a motility complex, spanning the cytoplasm, inner membrane and the periplasm. (tamu.edu)
- Cks proteins are adapter molecules that coordinate the assembly of multiprotein complexes. (ens-lyon.fr)
- We show that these differences are due to the levels of COQ biosynthetic proteins, suggesting that the presence of a truncated version of COQ9 protein in Coq9R239X mice destabilizes the CoQ multiprotein complex. (ugr.es)
- BACKGROUND: Multimeric protein complexes have a role in many cellular pathways and are highly interconnected with various other proteins. (embl-heidelberg.de)
- CONCLUSIONS: The occurrence of the PAM domain in specific subunits of multimeric protein complexes, together with the role of other all-alpha-helical folds in protein-protein interactions, suggest a function for this domain in mediating transient binding to diverse target proteins. (embl-heidelberg.de)
- Single copies of an alpha-helical-rich motif are demonstrated to be present within subunits of the large multiprotein 26S proteasome and eukaryotic initiation factor-3 (eIF3) complexes, and within proteins involved in transcriptional regulation. (embl-heidelberg.de)
- The presence of homologous, and sometimes identical, proteins in contrasting functional contexts suggests that the large multisubunit complexes of the 26S proteasome, eIF3 and TFIIH perform overlapping cellular roles. (embl-heidelberg.de)
- We found a fungal complex of seven proteins forming a structure with an essential role in disease development. (mpg.de)
- Increased collagen II protein accumulation did not associate with increased col2a1 mRNA or a decrease in matrix metalloproteinase activity but, instead, it associated with increased expression of the endoplasmic reticulum/Golgi transport coat protein complex II Sec proteins. (asnjournals.org)
- Polycystin 1 and polycystin 2 are multipass transmembrane proteins that function together as a receptor-ion channel complex, 1 leading to the widely held view that primary cellular defects in polycystin-deficient cells are caused by a disruption of normal Ca 2+ signaling. (asnjournals.org)
- Although some Acr proteins against the Csy complex have been reported, other relevant Acr proteins still need studies to understand their mechanisms. (osti.gov)
- As such, here, we obtain three structures of previously unresolved Acr proteins (AcrF9, AcrF8, and AcrF6) bound to the Csy complex using electron cryo-microscopy (cryo-EM), with resolution at 2.57 Å, 3.42 Å, and 3.15 Å, respectively. (osti.gov)
- The 2.57-Å structure reveals fine details for each molecular component within the Csy complex as well as the direct and water-mediated interactions between proteins and CRISPR RNA (crRNA). (osti.gov)
- Our structures also show unambiguously how these Acr proteins bind differently to the Csy complex. (osti.gov)
- Acr proteins against the Csy complex. (osti.gov)
- Our laboratory uses a genetic approach in mouse to discover genes, proteins and pathways that play an important role in complex human diseases. (mcgill.ca)
- The presence of this region in a number of other complex-forming proteins points to the possible involvment of the VWFC domain in complex formation. (embl.de)
- The Myb proteins interact with a highly conserved multi-protein complex called the MuvB core. (stanford.edu)
- The same complex also interacts with proteins of the Rb tumor suppressor family and the E2F transcription factor family. (stanford.edu)
- My research goal is to use cryo-electron microscopy (cryo-EM) to determine the molecular structure of proteins and multi-protein complexes to understand their function. (nih.gov)
- Proteins are complex molecules that play important functions in living organisms. (nih.gov)
- Full-length Rb and MCM7 form protein complexes in vitro, and the amino termini of two Rb-related proteins, p107 and p130 , also bind MCM7 . (xenbase.org)
Subunit1
- The TSC complex subunit 1 (TSC1) binds lysosomes via phosphatidylinositol-3,5-bisphosphate [PI(3,5)P2]. (frontiersin.org)
Inflammasomes2
- Recent studies suggest that the pathogenesis of different inflammatory diseases also involves the inflammasomes, intracellular multiprotein complexes that mediate activation of inflammatory caspases thereby inducing the secretion of proinflammatory cytokines. (hindawi.com)
- Inflammasomes are multiprotein complexes and serve as platforms that mediate the release of innate cytokines after successful recognition, thereby attracting immune cells. (bvsalud.org)
Mitochondrial2
- Our study points out the importance of the multiprotein complex for CoQ biosynthesis in mammals, which may provide new insights to understand the genotype-phenotype heterogeneity associated with human CoQ deficiency and may have a potential impact on the treatment of this mitochondrial disorder. (ugr.es)
- In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II. (bvsalud.org)
Multi-protein complex9
- mTORC1 is an evolutionary highly conserved multi-protein complex. (frontiersin.org)
- This cytoplasmic, multi-protein complex responds to an array of different stressors but typically requires two signals. (cdc.gov)
- The PAM domain, a multi-protein complex-associated module with an all-alpha-helix fold. (embl-heidelberg.de)
- Functions in a multi-protein complex in spermatid maturation. (antibodies-online.com)
- The new study, published in Proceedings of the National Academy of Sciences on March 5, has now shown that a multi-protein complex found in the body of P falciparum helps it convert haemoglobin into hemozoin. (org.in)
- They identified a multi-protein complex, consisting of protease enzymes and haem detoxification protein, produced by the parasite. (org.in)
- They found that this multi-protein complex is always present close to hemozoin crystals, suggesting it could have a role in crystal formation. (org.in)
- This newly found pathway of hemozoin formation could be exploited to screen new anti-malarial drugs that could prevent the multi-protein complex from binding to haem and prevent subsequent hemozoin formation," says Malhotra. (org.in)
- This effect is mediated through the formation of an apoptosome, a multi-protein complex consisting of cytochrome C, Apaf-1, pro-caspase 9 and ATP. (reading.ac.uk)
Molecular8
- The clustering of sulphated sugar residues in a series of complex domains with variable sulphation patterns generates considerable diversity in the molecular fine structure of HS. (portlandpress.com)
- NGL viewer: web-based molecular graphics for large complexes. (cansar.ai)
- In contrast, molecular details on lysosomal recruitment of the TSC complex have emerged only recently. (frontiersin.org)
- In this mini-review, we integrate the molecular mechanisms of lysosome and SG recruitment of the TSC complex. (frontiersin.org)
- 5 ns) molecular dynamics simulations indicate that residues of Cks1 that form the binding site for phosphorylated ligands are considerably more flexible in the free form of Cks1 than they are in the Cdk2-Cks1 complex. (ens-lyon.fr)
- Sensing of bacterial products by Naip5/Birc1e results in stimulation of a multiprotein complex known as the inflammasome that amplifies the molecular signal. (mcgill.ca)
- Specific interactions - those that lead to formation of well-defined complexes consisting of exact molecular stoichiometries (e.g., protein-ligand complexes). (wyatt.com)
- CG-MALS is adept at characterizing both specific and non-specific interactions to determine the magnitude of the interaction and the true molecular stoichiometry (when applicable) of resultant complexes and oligomers. (wyatt.com)
Structural4
- Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix domain of Ska1, providing the structural basis for the ability to bind both straight and curved microtubule structures. (nature.com)
- The structural maintenance of chromosomes (SMC) protein complexes shape and regulate the structure and dynamics of chromatin, thereby controlling many chromosome-based processes such as cell cycle progression, differentiation, gene transcription and DNA repair. (mdpi.com)
- Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1. (nih.gov)
- Comprehensive characterization of complex structural variations in cancer by directly comparing genome sequence reads. (irbbarcelona.org)
Characterization1
- This equilibrium is concentration-dependent, so a fractionation technique such as SEC-MALS - with the accompanying time-dependent dilution - is not suitable for full and rigorous characterization of reversible complexes. (wyatt.com)
Eukaryotic1
- We show that mTOR and S6K1 maneuver on and off the eukaryotic initiation factor 3 (eIF3) translation initiation complex in a signal-dependent, choreographed fashion. (nih.gov)
Coordinate1
- Thus, the eIF3 preinitiation complex acts as a scaffold to coordinate a dynamic sequence of events in response to stimuli that promote efficient protein synthesis. (nih.gov)
Assembly3
- This diversity reflects a high degree of selectivity in protein recognition and in the assembly of functional multiprotein complexes on the HS polymer chain. (portlandpress.com)
- Accordingly, it has been proposed that the Ska and Ndc80 complexes form an integrated MT-binding assembly 31 . (nature.com)
- Arginine dimethylation plays critical roles in the assembly of ribonucleoprotein complexes in pre-mRNA splicing and piRNA pathways. (cipsm.de)
Protein complex4
- The tuberous sclerosis protein complex (TSC complex) is a key integrator of metabolic signals and cellular stress. (frontiersin.org)
- Our results suggest that polycystin 2 deficiency causes increased collagen II synthesis with upregulation of secretory pathway coat protein complex II components. (asnjournals.org)
- To confirm this, they inactivated falcipain-2, one of the protease enzymes in the protein complex, and observed if this hindered hemozoin formation. (org.in)
- In addition, overexpression of KSR-1 in 293T cells leads to recruitment of MEK to a 700 kDa protein complex and translocates MEK from the soluble to the membrane-associated fraction. (bdbiosciences.com)
Functional1
- The ability of the Ska complex to track depolymerizing MTs in vitro and its dependency on the KMN for its localization and function suggest that the Ska complex may be a functional equivalent of the Dam/DASH complex in metazoans 25 , 26 . (nature.com)
Monomers1
- Reversible complexes are formed as a result of non-covalent interactions producing dynamic equilibrium between complexes and constituent monomers. (wyatt.com)
Transcription2
Proteasome1
- RESULTS: We identified a new module, the PAM domain (PCI/PINT associated module), present in single subunits of well characterized multiprotein complexes, like the regulatory lid of the 26S proteasome, the COP-9 signalosome and the Sac3-Thp1 complex. (embl-heidelberg.de)
Biochemistry1
- In this study, we used biochemistry and cell biology analyses to identify multi-protein complexes associated with A-motility. (tamu.edu)
Stimulation1
- Cell stimulation promotes mTOR/raptor binding to the eIF3 complex and phosphorylation of S6K1 at its hydrophobic motif. (nih.gov)
EIF31
- When inactive, S6K1 associates with the eIF3 complex, while the S6K1 activator mTOR/raptor does not. (nih.gov)
Phosphorylation1
- Phosphorylation results in S6K1 dissociation, activation, and subsequent phosphorylation of its translational targets, including eIF4B, which is then recruited into the complex in a phosphorylation-dependent manner. (nih.gov)
Regulate1
- In these research programs, we have cloned major genes that regulate response to infections, and in the case of complex genetic control, we have isolated single gene effects in unique recombinant or mutant mouse strains. (mcgill.ca)
Binds1
- This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. (nature.com)
Interactions1
- PACSAB: Coarse-Grained Force Field for the Study of Protein-Protein Interactions and Conformational Sampling in Multiprotein Systems. (irbbarcelona.org)
Large3
- This is characteristic of MALDI-TOF mass spectrometry, which can determine the mass of individual components of large protein complexes. (wikibooks.org)
- SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene. (xenbase.org)
- Large T antigens of many polyomaviruses are able to form complexes with the retinoblastoma protein. (xenbase.org)
Interacts1
- The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind microtubules in multiple modes. (nature.com)
Synthesis1
- Regulates lipopolysaccharide-induced IL-12 synthesis in macrophages by forming a complex with TRAF6, resulting in the inhibition of TRAF6 NF-kappa-B activation. (antibodies-online.com)
Interplay2
- We discuss their interplay in the context of cell proliferation and migration in cancer and in the clinical manifestations of tuberous sclerosis complex disease (TSC) and lymphangioleiomyomatosis (LAM). (frontiersin.org)
- This survival paradox has been attributed to a complex interplay between sociocultural and psychosocial factors, as well as other factors. (cdc.gov)
Formation2
- The polycystin 1/2 complex in apical cilia participates in mechanosensory Ca 2+ signaling in response to fluid flow, 6 suggesting that loss of either polycystins or cilia structure would lead to acute loss of flow sensation and cyst formation. (asnjournals.org)
- while they may lead to the formation of complexes or loosely-bound aggregates, these typically do not exhibit a well-defined stoichiometry or oligomeric state. (wyatt.com)
Models1
- The CALYPSO software offers an unparalleled set of association models with the flexibility to describe common as well as unusual complexes, all of which may be found in nature. (wyatt.com)
Chromosome2
- Cells depleted of the Ska complex fail to maintain stable KT-MT attachments, resulting in chromosome congression failure followed by cell death 25 , 26 . (nature.com)
- In a mouse model of aerosol infection with Mycobacterium tuberculosis , we have shown that a locus on chromosome 7 is partly responsible for the complex genetic control of the inter-strain difference in susceptibility between C57BL/6J and DBA/2J. (mcgill.ca)
Common2
- The PCI domain: a common theme in three multiprotein complexes. (embl-heidelberg.de)
- A common feature appears to be involvement in multiprotein complexes. (embl.de)
Structures2
- We report solution structures of SMN and SPF30 Tudor domains bound to symmetric and asymmetric dimethylated arginine (DMA) that is inherent in the RNP complexes. (cipsm.de)
- Proteasomes come in a variety of flavors, and all are very complex multi-protein structures. (fightaging.org)
Domain2
- Disrupting either the flexibility or the tubulin contact sites of the Ska1 microtubule-binding domain perturbs normal mitotic progression, explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules. (nature.com)
- Here we report the crystal structure of superfamily 2 (SF2) ATPase domain of RIG-I in complex with a nucleotide analogue. (cipsm.de)
Inactive1
- Normally CAD exists as an inactive complex with ICAD (inhibitor of CAD). (reading.ac.uk)
Axis1
- The TSC complex-mTORC1 axis translates nutrient and stress signals into tightly orchestrated cellular responses that impinge on anabolic processes including translation, as well as catabolic processes such as autophagy ( Liu and Sabatini, 2020 ). (frontiersin.org)
Signals1
- Angiogenesis, which is the process by which new blood vessels develop from preexisting vessels, is governed by a very complex network of opposing signals that, under normal physiological conditions, are elicited by various highly regulated angiogenesis stimulators and inhibitors [ 1 ]. (hindawi.com)
Human1
- Protein complexes between Rb and MCM7 were also detected in anti-Rb immunoprecipitates prepared from human cells. (xenbase.org)