Evidence map›Paper›PMID 22962007›Full record

ArticleThe Journal of biological chemistry2012

Gene duplication and the evolution of hemoglobin isoform differentiation in birds.

Michael T Grispo, Chandrasekhar Natarajan, Joana Projecto-Garcia, Hideaki Moriyama, Roy E Weber, Jay F Storz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 63 citations in OpenAlex.

  1. Origins of allostery in vertebrate hemoglobin evolution.bioRxiv : the preprint server for biology · 2026
    Article
  2. Convergent High OAnimals : an open access journal from MDPI · 2024
    Article
  3. Article
  4. Changes in hemoglobin function and isoform expression during embryonic development in the American alligator,American journal of physiology. Regulatory, integrative and comparative physiology · 2021
    Article
  5. Article
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  8. Evolved increases in hemoglobin-oxygen affinity and the Bohr effect coincided with the aquatic specialization of penguins.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
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  12. Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and COAmerican journal of physiology. Regulatory, integrative and comparative physiology · 2020
    Article
  13. Article
  14. The role of mutation bias in adaptive molecular evolution: insights from convergent changes in protein function.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Article
  15. Article
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  17. Divergent and parallel routes of biochemical adaptation in high-altitude passerine birds from the Qinghai-Tibet Plateau.Proceedings of the National Academy of Sciences of the United States of America · 2018
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Michael T GrispoSchool of Biological Sciences, University of Nebraska, Lincoln, Nebraska 68588, USA.
Chandrasekhar Natarajan
Joana Projecto-Garcia
Hideaki Moriyama
Roy E Weber
Jay F Storz
University of Nebraska–Lincoln · USAarhus University · DK

Funding

Mutational Pleiotropy, Epistasis, and the Adaptive Evolution of Hemoglobin FunctionR01HL087216 · NHLBI · UNIVERSITY OF NEBRASKA LINCOLN · PI STORZ, JAY · 2008 to 2021
$4.5M
NHLBI NIH HHS HL087216-S1NHLBI NIH HHS R01 HL087216
6 · The paper itself

Abstract

The majority of bird species co-express two functionally distinct hemoglobin (Hb) isoforms in definitive erythrocytes as follows: HbA (the major adult Hb isoform, with α-chain subunits encoded by the α(A)-globin gene) and HbD (the minor adult Hb isoform, with α-chain subunits encoded by the α(D)-globin gene). The α(D)-globin gene originated via tandem duplication of an embryonic α-like globin gene in the stem lineage of tetrapod vertebrates, which suggests the possibility that functional differentiation between the HbA and HbD isoforms may be attributable to a retained ancestral character state in HbD that harkens back to a primordial, embryonic function. To investigate this possibility, we conducted a combined analysis of protein biochemistry and sequence evolution to characterize the structural and functional basis of Hb isoform differentiation in birds. Functional experiments involving purified HbA and HbD isoforms from 11 different bird species revealed that HbD is characterized by a consistently higher O(2) affinity in the presence of allosteric effectors such as organic phosphates and Cl(-) ions. In the case of both HbA and HbD, analyses of oxygenation properties under the two-state Monod-Wyman-Changeux allosteric model revealed that the pH dependence of Hb-O(2) affinity stems primarily from changes in the O(2) association constant of deoxy (T-state)-Hb. Ancestral sequence reconstructions revealed that the amino acid substitutions that distinguish the adult-expressed Hb isoforms are not attributable to the retention of an ancestral (pre-duplication) character state in the α(D)-globin gene that is shared with the embryonic α-like globin gene.

Indexed as

Evolution, MolecularGene DuplicationAlgorithmsAmino Acid SequenceAnimalsBinding, CompetitiveBinding SitesBirdsCloning, MolecularGenetic VariationHemoglobin AHemoglobinsHemoglobins, AbnormalKineticsModels, MolecularMolecular Sequence DataHemoglobin Ahemoglobin DHemoglobinsHemoglobins, AbnormalOxygenProtein Isoforms

Identifiers

PMID22962007
PMCPMC3488042
OpenAlexW2149379419

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.