scholarly article | Q13442814 |
P819 | ADS bibcode | 1994PNAS...9111547K |
P356 | DOI | 10.1073/PNAS.91.24.11547 |
P932 | PMC publication ID | 45268 |
P698 | PubMed publication ID | 7972099 |
P5875 | ResearchGate publication ID | 15227339 |
P50 | author | Chien Ho | Q42141894 |
P2093 | author name string | M F Tam | |
M Zou | |||
N T Ho | |||
H W Kim | |||
D P Sun | |||
T J Shen | |||
P F Cottam | |||
M Madrid | |||
P2860 | cites work | Structure of human oxyhaemoglobin at 2.1 A resolution | Q27729152 |
The crystal structure of human deoxyhaemoglobin at 1.74 A resolution | Q27729163 | ||
Rapid and efficient site-specific mutagenesis without phenotypic selection | Q27860608 | ||
Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes | Q28305615 | ||
Proton nuclear magnetic resonance study of the quaternary structure of human hemoglobins in water | Q30653457 | ||
Expression of fully functional tetrameric human hemoglobin in Escherichia coli | Q33876275 | ||
Hemoglobin Yakima: I. Clinical and Biochemical Studies* | Q34088690 | ||
Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure | Q34162845 | ||
A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket | Q34255653 | ||
Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates | Q35533714 | ||
Production of unmodified human adult hemoglobin in Escherichia coli | Q36510636 | ||
Contribution of the hydrophobic effect to protein stability: analysis based on simulations of the Ile-96----Ala mutation in barnase | Q37637250 | ||
Free energy via molecular simulation: applications to chemical and biomolecular systems | Q38648060 | ||
A marker-coupled method for site-directed mutagenesis | Q44784538 | ||
Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin | Q47872421 | ||
Simulation analysis of the stability mutant R96H of T4 lysozyme. | Q52451866 | ||
Nuclear magnetic resonance and spin-label studies of hemoglobin Kempsey. | Q53693177 | ||
Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery | Q59054576 | ||
Proton nuclear Overhauser effect investigation of the heme pockets in ligated hemoglobin: conformational differences between oxy and carbonmonoxy forms | Q64004812 | ||
A proton nuclear magnetic resonance investigation of human hemoglobin A2 | Q64004814 | ||
Nuclear magnetic resonance studies of hemoglobins. VII. Tertiary structure around ligand binding site in carbonmonoxyhemoglobin | Q64004836 | ||
Haemoglobin Radcliffe (alpha2beta299(Gi)Ala): a high oxygen-affinity variant causing familial polycythaemia | Q67569442 | ||
Functional properties of hemoglobin Kempsey | Q68844260 | ||
Hidden thermodynamics of mutant proteins: a molecular dynamics analysis | Q69621171 | ||
Solvent effects on protein motion and protein effects on solvent motion. Dynamics of the active site region of lysozyme | Q69703244 | ||
An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers | Q70037993 | ||
Functional studies of two new abnormal hemoglobins with their mutation located at intersubunit contacts: Hb hotel dieu β99 (G1) Asp → Gly and Hb pitie salpetriere β34 (B16) Val → Phe | Q70968226 | ||
Erythrocytosis secondary to increased oxygen affinity of a mutant hemoglobin, hemoglobin Kempsey | Q72047182 | ||
Familial erythrocytosis. A description of three families, one with hemoglobin Ypsilanti | Q72128203 | ||
P433 | issue | 24 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 11547-11551 | |
P577 | publication date | 1994-11-01 | |
P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
P1476 | title | Restoring allosterism with compensatory mutations in hemoglobin | |
P478 | volume | 91 |
Q33746723 | An investigation of the distal histidyl hydrogen bonds in oxyhemoglobin: effects of temperature, pH, and inositol hexaphosphate |
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Q64004771 | Site mutations disrupt inter-helical H-bonds (α14W–α67T and β15W–β72S) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation |
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