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Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i>

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Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> is a paper indexed in PICO Portal from OpenAlex.

How many citations does Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> have?

PICO Portalcitation count

Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> has 132 citations in the OpenAlex counts PICO Portal stores.

When was Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> published?

PICO Portalyear

Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> has 1994 year in the PICO Portal index.

What is the open-access status of Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i>?

PICO Portaloa status

Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> has closed oa status in the PICO Portal index.

What is the DOI of Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i>?

PICO Portaldoi

The DOI for Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> is on the source record.

What is the PMID of Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i>?

PICO Portalpmid

The PMID for Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> is on the source record.

What is the OpenAlex record for Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i>?

PICO Portalopenalex

The OpenAlex for Hydrophobic interaction at the subunit interface contributes to the thermostability of 3‐isopropylmalate dehydrogenase from an extreme thermophile, <i>Thermus thermophilus</i> is on the source record.

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