Barely Significant
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Crystal structure of Thermus thermophilus methylenetetrahydrofolate dehydrogenase and determinants of thermostability.

PLoS One · 2020 · PMC7219735 · PMID 32401802

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showed a trendno p-value reported
AbMTHFD showed a trend to have more substituted amino acids at high composite Z-score positions when compared with TtMTHFD and had a slight trend when compared to TaMTHFD.

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a slight trendno p-value reported
Regarding the RMSD values over time ( Fig 2A, 2B and 2C ), a slight trend to higher RMSD values with temperature could be seen in all three proteins.

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a small trendno p-value reported
The less thermophilic TaMTHFD showed only a small trend to have more substituted amino acids at high composite Z-score positions when compared with TtMTHFD and had a more significant trend when compared with AbMTHFD.

also in 722 other papers

Quoted from the open-access full text in Europe PMC under the licence the publisher applied. The sentence is reproduced exactly as published; the emphasis is ours.