Roy E. Weber
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View article: Evolution of an extreme hemoglobin phenotype contributed to the sub-Arctic specialization of extinct Steller’s sea cows
Evolution of an extreme hemoglobin phenotype contributed to the sub-Arctic specialization of extinct Steller’s sea cows Open
The extinct Steller’s sea cow ( Hydrodamalis gigas ; †1768) was a whale-sized marine mammal that manifested profound morphological specializations to exploit the harsh coastal climate of the North Pacific. Yet despite first-hand accounts o…
View article: Evolution of an extreme hemoglobin phenotype contributed to the sub-Arctic specialization of extinct Steller’s sea cows
Evolution of an extreme hemoglobin phenotype contributed to the sub-Arctic specialization of extinct Steller’s sea cows Open
The extinct Steller’s sea cow ( Hydrodamalis gigas ; †1768) was a whale-sized marine mammal that manifested profound morphological specializations to exploit the harsh coastal climate of the North Pacific. Yet despite first-hand accounts o…
View article: Ontogeny of hemoglobin‑oxygen binding and multiplicity in the obligate air-breathing fish Arapaima gigas
Ontogeny of hemoglobin‑oxygen binding and multiplicity in the obligate air-breathing fish Arapaima gigas Open
The evolutionary and ontogenetic changes from water- to air-breathing result in major changes in the cardiorespiratory systems. However, the potential changes in hemoglobin's (Hb) oxygen binding properties during ontogenetic transitions to…
View article: Effect of NH2-terminal acetylation on the oxygenation properties of vertebrate haemoglobin
Effect of NH2-terminal acetylation on the oxygenation properties of vertebrate haemoglobin Open
In vertebrate haemoglobin (Hb), the NH2-terminal residues of the α- and β-chain subunits are thought to play an important role in the allosteric binding of protons (Bohr effect), CO2 (as carbamino derivatives), chloride ions, and organic p…
View article: Evolutionary History of the Globin Gene Family in Annelids
Evolutionary History of the Globin Gene Family in Annelids Open
Animals depend on the sequential oxidation of organic molecules to survive; thus, oxygen-carrying/transporting proteins play a fundamental role in aerobic metabolism. Globins are the most common and widespread group of respiratory proteins…
View article: Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO<sub>2</sub>
Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and CO<sub>2</sub> Open
Hemoglobins (Hbs) of crocodilians are reportedly characterized by unique mechanisms of allosteric regulatory control, but there are conflicting reports regarding the importance of different effectors, such as chloride ions, organic phospha…
View article: Molecular basis of hemoglobin adaptation in the high-flying bar-headed goose
Molecular basis of hemoglobin adaptation in the high-flying bar-headed goose Open
During the adaptive evolution of a particular trait, some selectively fixed mutations may be directly causative and others may be purely compensatory. The relative contribution of these two classes of mutation to adaptive phenotypic evolut…
View article: Allosteric mechanisms underlying the adaptive increase in hemoglobin-oxygen affinity of the bar-headed goose
Allosteric mechanisms underlying the adaptive increase in hemoglobin-oxygen affinity of the bar-headed goose Open
The high blood-O2 affinity of the bar-headed goose (Anser indicus) is an integral component of the biochemical and physiological adaptations that allow this hypoxia-tolerant species to undertake migratory flights over the Himalayas. The hi…
View article: Hypoxia-induced changes in hemoglobins of Lake Victoria cichlids
Hypoxia-induced changes in hemoglobins of Lake Victoria cichlids Open
Broods of the Lake Victoria cichlid Haplochromis ishmaeli raised under hypoxic and normoxic conditions, showed striking differences in isohemoglobin (isoHb) pattern not observed in two other cichlids that do not belong to the Lake Victoria…
View article: Molecular basis of hemoglobin adaptation in the high-flying bar-headed goose
Molecular basis of hemoglobin adaptation in the high-flying bar-headed goose Open
During adaptive phenotypic evolution, some selectively fixed mutations may be directly causative and others may be purely compensatory. The relative contribution of these two classes of mutation depends on the form and prevalence of mutati…
View article: Stability-Mediated Epistasis Restricts Accessible Mutational Pathways in the Functional Evolution of Avian Hemoglobin
Stability-Mediated Epistasis Restricts Accessible Mutational Pathways in the Functional Evolution of Avian Hemoglobin Open
If the fitness effects of amino acid mutations are conditional on genetic background, then mutations can have different effects depending on the sequential order in which they occur during evolutionary transitions in protein function. A ke…
View article: Predictable convergence in hemoglobin function has unpredictable molecular underpinnings
Predictable convergence in hemoglobin function has unpredictable molecular underpinnings Open
Expect the unexpected In convergent evolution, similar environmental conditions produce similar sets of adaptations. Does similar convergence exist in the molecular underpinnings of such morphological changes? Natarajan et al. looked acros…
View article: The mechanistic basis of hemoglobin adaptation in the high-flying barheaded goose: insights from ancestral protein resurrection
The mechanistic basis of hemoglobin adaptation in the high-flying barheaded goose: insights from ancestral protein resurrection Open
The bar-headed goose (‘BHG’, Anser indicus) is renowned for its trans-Himalayan migratory flights, and the elevated hemoglobin (Hb)-O2 affinity of this species is thought to make a key contribution to its capacity for powered flight at ele…