The heme chaperone CcmE is a novel protein that binds heme covalently via a histidine residue as part of its essential function in the process of cytochrome c biogenesis in many bacteria as well as plant mitochondria. In the continued absence of a structure of the holoform of CcmE, identification of the heme ligands is an important step in understanding the molecular function of this protein and the role of covalent heme binding to CcmE during the maturation of c-type cytochromes. In this work, we present spectroscopic data that provide insight into the ligation of the heme iron in the soluble domain of CcmE from Escherichia coli. Resonance Raman spectra demonstrated that one of the heme axial ligands is a histidine residue and that the other is likely to be Tyr134. In addition, the properties of the heme resonances of the holo-protein as compared with those of a form of CcmE with non-covalently bound heme provide evidence for the modification of one of the heme vinyl side chains by the protein, most
Corynebacteria contain a heme uptake system encoded in hmuTUV genes, in which HmuT protein acts as a heme binding protein to transport heme to the cognate transporter HmuUV. The crystal structure of HmuT from Corynebacterium glutamicum (CgHmuT) reveals that heme is accommodated in the central cleft with His141 and Tyr240 as the axial ligands and that Tyr240 forms a hydrogen bond with Arg242. In this work, the crystal structures of H141A, Y240A, and R242A mutants were determined to understand the role of these residues for the heme binding of CgHmuT. Overall and heme environmental structures of these mutants were similar to those of the wild type, suggesting that there is little conformational change in the heme-binding cleft during heme transport reaction with binding and the dissociation of heme. A loss of one axial ligand or the hydrogen bonding interaction with Tyr240 resulted in an increase in the redox potential of the heme for CgHmuT to be reduced by dithionite, though the wild type was not
article{44846ede-d441-4e41-b7e9-5579df433b3c, abstract = {Heme A is a prosthetic group of many respiratory oxidases. It is synthesized from protoheme IX (heme B) seemingly with heme O as a stable intermediate. The Bacillus subtilis ctaA and ctaB genes are required for heme A and heme O synthesis, respectively (B. Svensson, M. Lubben, and L. Hederstedt, Mol. Microbiol. 10:193-201, 1993). Tentatively, CtaA is involved in the monooxygenation and oxidation of the methyl side group on porphyrin ring D in heme A synthesis from heme B. B. subtilis ctaA and ctaB on plasmids in both B. subtilis and Escherichia coli were found to result in a novel membrane-bound heme-containing protein with the characteristics of a low-spin b type cytochrome. It fan be reduced via the respiratory chain, and in the reduced state it shows light absorption maxima at 428, 528, and 558 nm and the or-band is split. Purified cytochrome isolated from both B. subtilis and E. coli membranes contained one polypeptide identified as ...
To the best of our knowledge, this study is the first report suggesting a molecular mechanism by which heme regulates humoral immunity. Together with our recent report,15 our present results provide strong evidence that heme augments plasma cell differentiation by inhibiting Bach2, and thus increasing the population of Blimp-1-expressing cells. Because Blimp-1 is the master regulator of plasma cell differentiation,19,41 its derepression by heme through Bach2 inactivation may fine-tune the response of humoral immunity. In addition, heme may regulate the B-cell responses by inducing the expression of HO-1, which possesses antioxidant and immunomodulatory functions.9. In the spectral analyses, the 432-nm absorption band (6-coordinate heme-binding mode) and the 366-nm absorption band (5-coordinate heme-binding mode) both became apparent on addition of heme (Figure 1B). These results suggested that Bach2 bound to heme directly and had at least 2 distinct binding modes. Moreover, the spectral changes ...
A previous study in rabbit coronary microvessel endothelial cells demonstrated that upregulation of HO-1 leading to reduction in cellular heme levels decreases basal prostaglandin synthesis.7 Our present study shows that prostaglandin production is decreased in human femoral artery endothelial cells overexpressing HO-1 owing to treatment with SnCl2, a chemical HO-1 inducer, or to transfection with the human HO-1 gene, both of which interventions are documented to reduce heme levels in endothelial cells.8 On the other hand, a reciprocal relationship between HO-1 overexpression and prostaglandin production is not obtained in endothelial cells treated with heme or with ZnDPP.. As previously reported, and confirmed in our study, heme and HO inhibitors such as ZnDPP are powerful inducers of HO-1 protein.7,20 Importantly, the upregulation of HO-1 expression produced by these agents is unlikely to produce depletion of cellular heme, which could explain our finding that heme treatment increases and ...
Heme is a porphyrin that is coordinated with Fe(II). One of the most important classes of chelating agents in nature are the porphyrins [1]. A porphyrin molecule can coordinate to a metal using the four nitrogen atoms as electron-pair donors. In the body, the iron in the heme is coordinated to the four nitrogen atoms of the porphyrin and also to a nitrogen atom from a histidine residue, one of the amino-acid residues in hemoglobin) of the hemoglobin proteins. The sixth protein, coordination site, around the iron of the heme is occupied by O2 when the hemoglobin is oxygenated. The heme group is nonplanar when it is not bound to oxygen [2]. The iron is pulled out of the plane of the porphyrin, towards the histidine residue to which it is attached. This nonplanar configuration is characteristic of the deoxygenated heme group, and is often referred to as being "domed shape" [2]. When the Fe heme group binds to an oxygen molecule, the porphyrin ring adopts a planar configuration and hence the Fe lies ...
The treatment of rats with cis-platinum (cis-diamminedichloroplatinum) for 1, 3 or 7 days elicited vastly different responses in the liver and the kidney in activities of enzymes of haem-metabolism pathway and gamma-glutamyl-cycle enzymes. The differences resided in the magnitude, direction and the time course of responses. In general, the liver was by far less severely affected, and when a response was elicited, it displayed an earlier onset (1-3 days), with a return to normal at 7 days. In the kidney, however, the effects were notable after 3 days of treatment, and became more pronounced at 7 days. Specifically, the activity of 5-aminolaevulinic acid (ALA) synthetase and contents of cytochrome P-450 and the microsomal haem were decreased in the liver. In contrast, in the kidney, cytochrome P-450 and haem concentrations were significantly increased, with no change in ALA synthetase activity. The increase in the kidney haem content appeared to reflect an increased formation of haem, as suggested ...
Our lives depend on heme. As part of hemoglobin, it carries oxygen to our tissues. As part of cytochrome c, it helps transform the energy in food into the energy-rich molecule ATP (adenosine triphosphate) that powers biochemical reactions that keep us alive and moving. As part of cytochrome P450, it helps break down toxic chemicals in our bodies. What is this thing called heme? And, how does it do such amazing work inside our bodies? Scientists know that heme is a large ringed molecule called a porphyrin that has an iron atom sitting in the middle of it. In the heme molecule shown at right, the iron atom is green and the atoms in the porphyrin ring are carbon (teal), nitrogen (dark blue), hydrogen (not shown), and oxygen (red). In the figure below, the heme is embedded in (and bonded to) cytochrome c. Understanding how heme functions at the biomolecular level is a hot research topic for biophysicists, including Research Associate Byung Moon Cho, Graduate Student Fredrik Carlsson, and Associate ...
The pronounced vascular pathologies described for both an HO-1-deficient human and mice in which this enzyme has been knocked out suggest that defective heme catabolism (and, by implication, heme itself) can have serious pathologic effects. Whereas heme may be directly cytotoxic, the present investigations were an attempt to determine whether the observed in vivo effects of HO-1 deficiency might, at least in part, represent an indirect process. Specifically, we hypothesized that extensive, heme- or heme iron-mediated oxidation of LDL might produce oxidized forms of LDL with appreciable cytotoxicity.. In support of this concept, LDL isolated from plasma preincubated with either heme or metHb is markedly cytotoxic to cultured endothelial cells. Furthermore, similarly toxic LDL was present in the plasma of the HO-1-deficient child. Conversion of ferroHb to metHb appears to be essential for the ensuing oxidation of LDL, presumably because metHb readily releases heme, whereas ferroHb does not. That ...
Molecular Basis Behind Inability of Mitochondrial Holocytochrome c Synthase to Mature Bacterial Cytochromes: Defining a Critical Role for Cytochrome c Alpha Helix-1. Babbitt SE, Hsu J, Kranz RG. J Biol Chem. 2016 Jul 6. Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins. Sutherland MC, Rankin JA, Kranz RG. Biochemistry. 2016 Jun 7;55(22):3150-6. Mitochondrial cytochrome c biogenesis: no longer an enigma. Babbitt SE, Sutherland MC, San Francisco B, Mendez DL, Kranz RG. Trends Biochem Sci. 2015 Aug;40(8):446-55. Review.. Mechanisms of mitochondrial holocytochrome c synthase and the key roles played by cysteines and histidine of the heme attachment site, Cys-XX-Cys-His. Babbitt SE, San Francisco B, Mendez DL, Lukat-Rodgers GS, Rodgers KR, Bretsnyder EC, Kranz RG. J Biol Chem. 2014 289(42):28795-807.. Conserved residues of the human mitochondrial holocytochrome c synthase, HCCS, mediate interactions with heme. Babbitt SE, ...
Mitochondrial cytochrome c (cytc) plays an important role in programmed cell death upon binding to cardiolipin (CL), a negatively charged phospholipid of the inner mitochondrial membrane (IMM). Although this binding has been thoroughly investigated in solution, little is known on the nature and reactivity of the adduct (cytc-CL) immobilized at IMM. In this work, we have studied electrochemically cytc-CL immobilized on a hydrophobic self-assembled monolayer (SAM) of decane-1-thiol. This construct would reproduce the motional restriction and the nonpolar environment experienced by cytc-CL at IMM. Surface-enhanced resonance Raman (SERR) studies allowed the axial heme iron ligands to be identified, which were found to be oxidation state dependent and differ from those of cytc-CL in solution. In particular, immobilized cytc-CL experiences an equilibrium between a low-spin (LS) 6c His/His and a high-spin (HS) 5c His/− coordination states. The former prevails in the oxidized and the latter in the ...
Hemoproteins have diverse biological functions including the transportation of diatomic gases, chemical catalysis, diatomic gas detection, and electron transfer. The heme iron serves as a source or sink of electrons during electron transfer or redox chemistry. In peroxidase reactions, the porphyrin molecule also serves as an electron source. In the transportation or detection of diatomic gases, the gas binds to the heme iron. During the detection of diatomic gases, the binding of the gas ligand to the heme iron induces conformational changes in the surrounding protein.[5] In general, diatomic gases only bind to the reduced heme, as ferrous Fe(II) while most peroxidases cycle between Fe(III) and Fe(IV) and hemeproteins involved in mitochondrial redox, oxidation-reduction, cycle between Fe(II) and Fe(III). It has been speculated that the original evolutionary function of hemoproteins was electron transfer in primitive sulfur-based photosynthesis pathways in ancestral cyanobacteria-like organisms ...
Heme-containing catalases have been extensively studied, revealing the roles of many residues, the existence of two heme orientations, flipped 180 degrees relative to one another along the propionate-vinyl axis, and the presence of both heme b and heme d. The focus of this report is a residue, situated adjacent to the vinyl groups of the heme at the entrance of the lateral channel, with an unusual main chain geometry that is conserved in all catalase structures so far determined. In Escherichia coli catalase HPII, the residue is Ile274, and replacing it with Gly, Ala, and Val, found at the same location in other catalases, results in a reduction in catalytic efficiency, a reduced intensity of the Soret absorbance band, and a mixture of heme orientations and species. The reduced turnover rates and higher H(2)O(2) concentrations required to attain equivalent reaction velocities are explained in terms of less efficient containment of substrate H(2)O(2) in the heme cavity arising from easier escape ...
Foundation Medicine and Collaborators to Present New Clinical Data on FoundationOne® and FoundationOne Heme at the 2014 ASCO Annual Meeting
The transport and intracellular trafficking of heme biosynthesis intermediates are crucial for hemoglobin production, which is a critical process in developing red cells. Here, we profiled gene expression in terminally differentiating murine fetal liver-derived erythroid cells to identify regulators of heme metabolism. We determined that TMEM14C, an inner mitochondrial membrane protein that is enriched in vertebrate hematopoietic tissues, is essential for erythropoiesis and heme synthesis in vivo and in cultured erythroid cells. In mice, TMEM14C deficiency resulted in porphyrin accumulation in the fetal liver, erythroid maturation arrest, and embryonic lethality due to profound anemia. Protoporphyrin IX synthesis in TMEM14C-deficient erythroid cells was blocked, leading to an accumulation of porphyrin precursors. The heme synthesis defect in TMEM14C-deficient cells was ameliorated with a protoporphyrin IX analog, indicating that TMEM14C primarily functions in the terminal steps of the heme ...
Synchronization of circadian oscillators with the outside world is achieved by the acute effects of light on the levels of one or more clock components. In mammals the PAS transcription factors Clock, NPAS2, and BMAL1 regulate gene expression as a function of the day-night cycle. Both PAS domains of NPAS2 were found to bind heme as a prosthetic group, form a gas-regulated sensor, and exert heme-status control of DNA binding in vitro. In a microarray analysis comparing overall changes in brain transcript levels between mice subjected to light pulses during the dark phase with animals maintained in darkness, we traced consistent changes in more than 200 different transcripts. Of these, 20 are associated with heme and iron biosynthesis and catabolism. A model for the pathway of induction of heme and iron homeostasis-related transcripts resulting from light pulses suggests that light signals (as stressors) induce transcription of heme oxygenase 2 (Hmox2) and cytochrome P450 oxidoreductase (Por), ...
The heme complex is an iron ion bound to a porphyrin ligand, which is a cage like molecule consisting of four tetradentate square planar nitrogen molecules. When the heme complex binds to a protein, it creates myglobin. Myglobin is important because the structure of the molecule allows the iron ion to bind to O2 molecules, absorbing and de-absorbing O2 as the local pressure of oxygen changes. This allows O2 to be transported in muscle cells throughout the body ...
Cytochrome P450 enzymes are responsible for the oxidative metabolism of a broad variety of endogenous and exogenous compounds, including sterols, fatty acids, drugs, and xenobiotics. The catalytic...
Folding of cytochrome c from its low pH guanidine hydrochloride (Gdn-HCl) denatured state revealed a new intermediate, a five-coordinate high spin species with a water molecule coordinated to the heme. Incorporation of this five-coordinated intermediate into the previously reported ligand exchange model can quantitatively account for the observed folding kinetics. In this new model, unfolded cytochrome c is converted to its native structure through an obligatory folding intermediate, the histidine-water coordination state, whereas the five-coordinate state and a bis-histidine state are off-pathway intermediates. When the concentration of Gdn-HCl in the refolding solution was increased, an acceleration of the conversion from the bis-histidine coordinated state to the histidine-water coordinated state was observed, demonstrating that the reaction requires unfolding of the mis-organized polypeptide structure associated with the bis-histidine state.
File:P450cycle.svg The active site of cytochrome P450 contains a heme iron center. The iron is tethered to the P450 protein via a thiolate ligand derived from a cysteine residue. This cysteine and several flanking residues are highly conserved in known CYPs and have the formal PROSITE signature consensus pattern [FW] - [SGNH] - x - [GD] - {F} - [RKHPT] - {P} - C - [LIVMFAP] - [GAD].[4] Because of the vast variety of reactions catalyzed by CYPs, the activities and properties of the many CYPs differ in many aspects. In general, the P450 catalytic cycle proceeds as follows: 1: The substrate binds to the active site of the enzyme, in close proximity to the heme group, on the side opposite to the peptide chain. The bound substrate induces a change in the conformation of the active site, often displacing a water molecule from the distal axial coordination position of the heme iron[5], and sometimes changing the state of the heme iron from low-spin to high-spin[6]. This gives rise to a change in the ...
Very little is known about heme transport in eukaryotes and a heme-specific transport uptake systems have not been identified in yeast. Heme is synthesized in m...
The long-term goals of this proposal are to delineate how humans regulate and integrate heme homeostasis at the organismal level. Heme, an iron containing organ...
Highly bioavailable Heme Iron is isolated from animal sources for maximum intestinal absorption. Its the particular type of iron that is easily recognized and exploited by the body to form the structural scaffolding for hemoglobin. Hemoglobin is the specialized protein within the blood that binds to oxygen within the lungs for use in cellular respiration throughout the entire body. Heme Iron also does not lead to common side effects associated with elemental forms of iron that include; stomach upset, diarrhea, and constipation.. ...
A medical apparatus including: a projecting member; an introducing sheath; an extrusion member inside the introducing sheath, at a proximal side of the projecting member and movable in an axial direction with respect to the introducing sheath; a cover sheath outside the introducing sheath, the introducing sheath being movable between a first and second position with respect to the cover sheath; an introducing sheath manipulating section at a proximal side of the introducing sheath; an extrusion member manipulating section at a proximal side of the extrusion member; a cover sheath manipulating section at a proximal side of the cover sheath; and a release member on the cover sheath manipulating section and/or the introducing sheath manipulating section to release a fixation between the extrusion member manipulating section and the introducing sheath manipulating section when the introducing sheath is disposed on the first or second position.
Humans survive by constantly recycling iron, a metal that is an essential component of red blood cells, but which is toxic outside of those cells. More than 90 percent of the iron in an adult humans 25 trillion life-sustaining red blood cells is recycled from worn-out cells.. Almost 50 years ago scientists first began hypothesizing that our bodies must have a special protein container to safely transport heme -- the form of iron found in living things - during the breakdown and recycling of old red blood cells and other types of heme metabolism. Now a team of scientists from the University of Maryland, Harvard Medical School, the National Institutes of Health and the University of Utah School of Medicine have identified this long-sought heme-iron transporter and shown that it is the same HRG1 protein that a common microscopic worm, C. elegans, uses to transport heme. In humans, the iron in heme is the component that allows hemoglobin in red blood cells to carry the oxygen needed for ...
Biosynthesis of myeloperoxidase (MPO), a myeloid lysosomal hemoprotein critical for the optimal oxygen-dependent microbicidal activity of human neutrophils, is incompletely understood. The primary translation product undergoes cotranslational N-linked glycosylation with subsequent insertion of the Fe-containing prosthetic group into the peptide backbone, thereby converting the enzymatically inactive, heme- free apoproMPO into the peroxidatively active precursor, proMPO. Eventually, proMPO undergoes proteolytic processing into native, lysosomal MPO, with subunits of 59 and 13.5 Kd. We studied three unanswered questions regarding MPO biosynthesis: (1) At what point during MPO biosynthesis is the heme moiety inserted into the apoenzyme? (2) What consequences does heme-insertion have on subsequent processing events? (3) What role does the mannose-6-phosphate receptor (M6PR) system play in the delivery of MPO to the lysosome? Disruption of Golgi by brefeldin A (BFA) produced two major changes in MPO ...
A heme group is a prosthetic group consisting of a protoporphyrin ring and a central iron (Fe) atom. A protoporphyrin ring is made up of four pyrrole rings linked by methine bridges. Four methyl, two vinyl, and two propionate side chains are attached. Heme of hemoglobin protein is a prosthetic group of heterocyclic ring of porphyrin of an iron atom; the biological function of the group is for delivering oxygen to body tissues, such that bonding of ligand of gas molecules to the iron atom of the protein group changes the structure of the protein by amino acid group of histidine residue around the heme molecule. The iron lies in the center is an organic component called protoporphyrin, which is bound to four pyrrole nitrogen atom linked by a methine bridge that forms a tetrapyrrole ring. The iron can either be in the ferrous (Fe2+) or the ferric (Fe3+) oxidation state. However, it is only able to bind to oxygen when in the ferrous state. The iron can form two additional bonds in fifth and in sixth ...
The protein encoded by this gene is an enzyme that covalently links a heme group to the apoprotein of cytochrome c. Defects in this gene are a cause of microphthalmia syndromic type 7 (MCOPS7). Three transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jan 2010 ...
Subcellular Localization of Iron and Heme Metabolism Related Proteins at Early Stages of Erythrophagocytosis. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Background:Nitrosylated and non-nitrosylated heme iron from red processed and non-processed meat have been associated with increased colorectal carcinogenesis. Mechanisms include oxidative processes. It has been hypothesized that dietary antioxidants could counteract the effects of heme iron. We investigated the relationships between heme iron intake and the risk of colorectal adenomas, and a potential interaction with the dietary antioxidant capacity, in the E3N prospective cohort study. Methods:The study included 17,397 women who underwent at least one colonoscopy. Among them, 1,409 were diagnosed with at least one first colorectal adenoma during the 103,253 person-years of follow-up. Dietary intake was measured by a semi-quantitative food history questionnaire. Hazard ratio (HR) estimates and 95% confidence intervals (CI) were obtained from Coxs proportional hazards models, adjusted for potential confounders. Results:Heme iron intake was positively associated with colorectal and colon ...
A novel endoproteolytic processing activity in mitochondria of erythroid cells and the role in heme synthesis | Dzikaite, Vijole; Kanopka, Arvydas; Brock, Jeremy H.; Kazlauskas, Arunas; Melefors, OÌ jar | download | BookSC. Download books for free. Find books
Study Flashcards On FA Biochemistry Heme Synthesis at Cram.com. Quickly memorize the terms, phrases and much more. Cram.com makes it easy to get the grade you want!
2O6P: Crystal structure of the heme-IsdC complex, the central conduit of the Isd iron/heme uptake system in Staphylococcus aureus.
... This course provides instruction in manufacturing control process and work cell interfacing. Emphasis is placed on open and closed loop systems. Instruction is also given in the area of linear integrated circuits. Topics include process control, sensor and cell level interfacing, fluid level, pressure, and flow measurement, pneumatic controls, and human factors and safety.. ...
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The KOMP Repository is located at the University of California Davis and Childrens Hospital Oakland Research Institute. Question? Comments? For Mice, Cells, and germplasm please contact us at [email protected], US 1-888-KOMP-MICE or International +1-530-752-KOMP, or for vectors [email protected] or +1-510-450-7917 ...
Red meat has a compound in it called haem or heme protein, which is what makes it red. Unfortunately, haem can damage our intestinal lining. If you love
Most people have some idea of how important iron is to their health, but Iqbal Hamza, professor in Animal and Avian Sciences, has made his seventeen-year career at the University of Maryland all about the study of iron and heme trafficking and regulation in the body.
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Hemoglobin (Hb) has multiple pathophysiologic effects when released into the intravascular space during hemolysis. inevitably linked to a BIIB-024 broad reactivity pattern with alternate ligands, such as carbon monoxide (CO), nitric oxide (NO), hydrogen peroxide (H2O2), and many others. The biochemistry of these reactions has been the focus of Hb study for decades. More recently, however, these Hb BIIB-024 reactions were examined like a potential cause of adverse pathophysiologic processes that accompany reddish blood cell (RBC) damage (i.e., hemolysis) and the build up of extracellular free Hb (Baek et al. 2012; Gladwin et al. 2012). Additional biologic activities of extracellular free Hb can be traced back either to direct relationships of its globin or heme parts with specific cellular receptors and signaling pathways, or to the secondary effects of heme breakdown from the heme oxygenases. The growing picture suggests that Hb like a toxin can adversely impact the outcome of varied conditions, ...
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Haem. Haem is the pigment found in haemoglobin, the protein that makes our blood red and carries oxygen round our bodies. Its also the pigment that makes red meat red.. Scientists, including the late Sheila Bingham, found that haem is broken down in our gut to form chemicals called N-nitroso compounds. These have been found to damage the DNA of the cells that line the digestive system. And DNA damage is the first step on the road to cancer.. To complicate things a bit it seems, that when the lining of our gut senses its been damaged, it reacts by telling the existing cells to divide more rapidly to make new cells. This extra cell division might also increase the chances of cancer developing, because every time a cell divides, it runs the risk of making a copying error in its DNA.. Professor Bingham ran studies that directly looked at the amount of N-nitroso compounds in peoples faeces, and looked at whether N-nitroso-linked DNA damage was occurring. It was.. Theres still some evidence ...
Youve probably heard that something described as blood red. But why, exactly, is blood red? The answer to this questions lies with a molecule...
E coli CcmH protein: a component of the putative CcmFH heme lyase complex involved in transfer of heme from CcmE to apocytochrome c; has been sequenced
Complete information for FLVCR1 gene (Protein Coding), FLVCR Heme Transporter 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Steinbach, P.J.; Ansari, A.; Berendzen, J.; Braunstein, D.; Chu, K.; Cowen, B.R.; Ehrenstein, D.; Frauenfelder, H.; Johnson, J.B.; Lamb, D.C.; Luck, S.; Mourant, J.R.; Nienhaus, G.U.; Ormos, P.; Philipp, R.; Xie, A.; Young, R.D ...
Water, Ability, Anions, Architecture, Behavior, Character, Dissociation, Heme, Heme Proteins, Hemoglobin, Hemoglobins, Histidine, Ions, Kinetics, Ligands, PH, Protein Subunits, Proteins, Proton, Protons
1MMV: Structural characterization and kinetics of nitric-oxide synthase inhibition by novel N5-(iminoalkyl)- and N5-(iminoalkenyl)-ornithines
When I first reported the bug in October 2013 (through the Tender system I guess it was?). Jeff said that the removal was an oversight and itd be restored in the next version. Im a bit disappointed to hear that wont be the case. I for one used it extensively, and if its already coded out... but ...