Find your PDFs fast.
Welcome to the Pubget Medical Subject Headings (MESH) browser. Click on a topic or subtopic below to explore related papers. In the gold box is the most recent paper about the current MESH term, and below are 20 related papers.
Apoproteins (3):
Recent article
Apoproteins
Abstract
I (THLGC) and II (PCHGS), were detected by multiple alignments. Real-time PCR analysis showed that Cgisp is expressed in a wide range of tissues, with adductor muscle exhibiting the top expression level, suggesting its biological function of energy transduction. The GFP tagging Cgisp indicated a mit...
|
PMID: 19876765
PDF is available here.
PDF is available here.
| < More recent | Older article > |
Abstract
We describe the crystal structures of the inner-membrane transporter CusA in the absence and presence of bound Cu(I) or Ag(I). These CusA structures provide new structural information about the HME subfamily of RND efflux pumps. The structures suggest that the metal-binding sites, formed by a three-...
|
PMID: 20865003
PDF is available here.
PDF is available here.
Cancer Letters (295)1 2010
Abstract
We demonstrated the intensified targeting therapy of a tandem scFv-based fusion protein and its enediyne-energized analogue against gelatinases-overexpressed tumor. A fusion protein dFv-LDP, comprising a tandem scFv of anti-gelatinases linked to the apoprotein (LDP) of lidamycin, was generated and s...
|
PMID: 20303650
PDF is available here.
PDF is available here.
Journal of Biological Chemistry (285)29 2010
Abstract
The roadblock/LC7 dynein light chain is a ubiquitous component of all dyneins and is essential for many diverse processes including proper axonal transport and dendrite growth. In addition, LC7 functions in non-dynein transcriptional activation of the transforming growth factor-beta complex. Crystal...
|
PMID: 20472935
PDF is available here.
PDF is available here.
Abstract
We identified a number of potential salt bridges on the protein surface as well as several key interactions inside the binding cavity. Furthermore, our NMR data demonstrate that helix alphaII of the characteristic helix-turn-helix motif in the ligand portal region exists in both apo and holo CRBP-II...
|
PMID: 19965581
PDF is available here.
PDF is available here.
Biophysical Journal (98)8 2010
Abstract
I and the folding nucleus were derived solely from kinetic data, namely, the slow-phase folding rate constants and the burst-phase amplitudes of Trp fluorescence intensity. This allowed us to pioneer the phi-analysis for apomyoglobin. As shown, these mutations drastically destabilized the native sta...
|
PMID: 20409491
PDF is available here.
PDF is available here.
Biophysical Journal (98)8 2010
Abstract
We have effectively reproduced such similarities and differences in behavior as are interpreted from experiment. From the analysis of such data, we explain the experimental evidence at hand through the effect of pressure on the change of water structure, and hence the weakening of the hydrophobic ef...
|
PMID: 20409483
PDF is available here.
PDF is available here.
Abstract
Particle beam/hollow cathode-optical emission spectroscopy (PB/HC-OES) is presented as a tool for the determination of metal ion loading in transferrin (Tf). The elemental specificity of optical emission spectroscopy provides a means of assessing metal ion concentrations as well as t...
|
PMID: 21069147
PDF is available here.
PDF is available here.
Abstract
I clinical trials. An important component of this success has been associated with targeted delivery of the complexes to cancer cells by serum proteins. In this study, electron paramagnetic resonance (EPR) measurements, combined with incubation under physiological conditions, and separation of prote...
|
PMID: 19707803
PDF is available here.
PDF is available here.
Abstract
The stability of camel alpha-lactalbumin (alpha-la) against heat denaturation was measured, using circular dichroism (CD) and fluorescence spectroscopy, as well as differential scanning calorimetry (DSC). The experiments were performed in the presence of saturating concentrations of calcium as well...
|
PMID: 19930756
PDF is available here.
PDF is available here.
Abstract
We present a method to predict the structure of protein/ligand complexes based solely on the apo structure, the ligand and the radius of gyration of the holo structure. The method is applied to ten cases in which proteins undergo structural rearrangements of up to 7.1 A backbone RMSD upon ligand bin...
|
PMID: 20066034
PDF is available here.
PDF is available here.
Abstract
We report here on the preparation of recombinant human RBP and TTR, the covalent labeling of TTR with the fluorescent dansyl probe, and fluorescence anisotropy titrations for RBP and TTR....
|
PMID: 20552430
PDF is available here.
PDF is available here.
Abstract
STRA6 is a multitransmembrane domain protein that was recently identified as the cell-surface receptor for plasma retinol-binding protein (RBP), the vitamin A carrier protein in the blood. STRA6 binds to RBP with high affinity and mediates cellular uptake of vitamin A from RBP. It is not homologous...
|
PMID: 20552439
PDF is available here.
PDF is available here.
Abstract
The principles of fluorescence resonance energy transfer have been utilized to develop a high-throughput assay which detects compounds that interfere with interaction between retinol-binding protein (RBP) and transthyretin (TTR). In this assay, the intrinsic fluorescence from the RBP-retinol complex...
|
PMID: 20552431
PDF is available here.
PDF is available here.
Abstract
These results indicate that MutT specifically recognizes 8-oxoguanine nucleotides by the ligand-induced conformational change....
|
PMID: 19864691
PDF is available here.
PDF is available here.
Abstract
Our findings demonstrate that the level of structural information obtainable with top-down ECD for small to medium-sized proteins considerably surpasses that of traditional HDX-MS experiments, while at the same time greatly reducing undesired amide back exchange....
|
PMID: 19670873
PDF is available here.
PDF is available here.
Biochemistry (Washington) (48)36 2009
Abstract
Our data confirm the presence of the disulfide bond between cysteines 94 and 100 in the holo form and indicate that there is predominantly no disulfide bond between these residues in the apoprotein....
|
PMID: 19658395
PDF is available here.
PDF is available here.
Abstract
We discovered that freeze drying or freezing of the protein in a peroxide solution does lead to protein oxidation. Interestingly, the oxidation is not a result of freeze or thaw processes but is dependent on the temperature and length of time for incubation. After 2 h, apomyoglobin undergoes almost-...
|
PMID: 19715356
PDF is available here.
PDF is available here.
Biochemistry (Washington) (48)31 2009
Abstract
Human carbonic anhydrase II (HCA II) is a monomeric zinc-containing metalloenzyme that catalyzes the hydration of CO(2) to form bicarbonate and a proton. The properties of the zinc have been extensively elucidated in catalysis but less well studied as a contributor to structure and stability. Apo-HC...
|
PMID: 19583303
PDF is available here.
PDF is available here.
Biochemistry (Washington) (48)31 2009
Abstract
The bfrB gene from Pseudomonas aeruginosa was cloned and expressed in Escherichia coli. The resultant protein (BfrB), which assembles into a 445.3 kDa complex from 24 identical subunits, binds 12 molecules of heme axially coordinated by two Met residues. BfrB, isolated with 5-10 iron atoms per prote...
|
PMID: 19575528
PDF is available here.
PDF is available here.
Biophysical Journal (97)2 2009
Abstract
With Cd and Zn metal ions removed from the native rabbit-liver metallothionein upon unfolding, Cu-modified metallothioneins (Cu-MTs) were obtained during refolding in solutions containing Cu(I) or Cu(II) ions. X-ray absorption near-edge spectroscopic results confirm the respectively assigned oxidati...
|
PMID: 19619476
PDF is available here.
PDF is available here.
Biophysical Journal (97)2 2009
Abstract
We demonstrate spontaneous, sustained and noticeable production of LDL(-) during incubation of unprocessed human plasma at 37 degrees C. In addition to a higher fraction of amyloidogenic LDL(-), LDL purified from incubated plasma contains an increased level of lysophospholipids and free fatty acids;...
|
PMID: 19619478
PDF is available here.
PDF is available here.
Abstract
Endostar, approved for the treatment of non-small-cell lung cancer by the State Food and Drug Administration in China, is a derivative of human endostatin that is modified with an additional metal-chelating sequence (MGGSHHHHH) at the N-terminus. This modification contributes to an additional zinc-b...
|
PMID: 19527221
PDF is available here.
PDF is available here.
Abstract
The orange-coloured protein (ORP) from Desulfovibrio gigas is a 12 kDa protein that contains a novel mixed-metal sulfide cluster of the type [S(2)MoS(2)CuS(2)MoS(2)]. Diffracting crystals of the apo form of ORP have been obtained. Data have been collected for the apo form of ORP to 2.25 A resolution...
|
PMID: 19574652
PDF is available here.
PDF is available here.
Biochemistry (Washington) (48)26 2009
Abstract
We have used NMR spectroscopy to investigate the solution structure of IscU from Escherichia coli and its interaction with HscB from the same organism. We found that wild-type apo-IscU in solution exists as two distinct conformations: one largely disordered and one largely ordered except for the met...
|
PMID: 19492851
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.
FEBS Letters (583)12 2009
Abstract
The intrinsic fluorescence of two apo-photoproteins has been characterized and its concentration-dependent quenching by coelenterazine has been for the first time applied to determine the apparent dissociation constants for coelenterazine binding with apo-aequorin (1.2+/-0.12 microM)...
|
PMID: 19426732
PDF is available here.
PDF is available here.