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Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: primase and the family X polymerases share significant sequence homology.

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Journal of applied physiology·1976

Flow field and mass transport analysis in arteries with longitudinal ridges.

Journal of applied physiology·1976

Cardiorespiratory responses of sedentary college women as a function of training intensity.

Journal of applied physiology·1976

Genetic influence on normal variability of maximum expiratory flow-volume curves.

Journal of applied physiology·1976

Method to optimize high-pressure, multicomponent gas mixing.

Journal of applied physiology·1976

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Oxygen concentrators: a primary oxygen supply source.

Interactions of DNA with human DNA primase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit.

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Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: primase and the family X polymerases share significant sequence homology.

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