Publications by authors named "Stephanie M Halmo"

Students with strong metacognitive skills are positioned to learn and achieve more than peers who are still developing their metacognition. Yet, many students come to college without well-developed metacognitive skills. As part of a longitudinal study on metacognitive development, we asked when, why, and how first-year life science majors use metacognitive skills of planning, monitoring, and evaluating.

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Stronger metacognitive regulation skills and higher self-efficacy are linked to increased academic achievement. Metacognition and self-efficacy have primarily been studied using retrospective methods, but these methods limit access to students' in-the-moment metacognition and self-efficacy. We investigated first-year life science students' metacognition and self-efficacy while they solved challenging problems, and asked: 1) What metacognitive regulation skills are evident when first-year life science students solve problems on their own? and 2) What aspects of learning self-efficacy do first-year life science students reveal when they solve problems on their own? Think-aloud interviews were conducted with 52 first-year life science students across three institutions and analyzed using content analysis.

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Stronger metacognition, or awareness and regulation of thinking, is related to higher academic achievement. Most metacognition research has focused at the level of the individual learner. However, a few studies have shown that students working in small groups can stimulate metacognition in one another, leading to improved learning.

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The canonical O-mannosylation pathway in humans is essential for the functional glycosylation of α-dystroglycan. Disruption of this post-translational modification pathway leads to congenital muscular dystrophies. The first committed step in the construction of a functional matriglycan structure involves the post-translational modification of α-dystroglycan.

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Research in science, technology, engineering, and mathematics education supports a shift from traditional lecturing to evidence-based instruction in college courses, yet it is unknown whether particular evidence-based pedagogies are more effective than others for learning outcomes like problem solving. Research supports three distinct pedagogies: worked examples plus practice, productive failure, and guided inquiry. These approaches vary in the nature and timing of guidance, all while engaging the learner in problem solving.

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Protein structure-function is a key concept in biochemistry. We used the perspective of domain-specific problem-solving to investigate students' solutions to a well-defined protein structure-function problem. We conducted think-aloud interviews with 13 undergraduate students and performed qualitative content analysis to examine the differences in the domain-general and domain-specific knowledge among correct and incorrect solutions.

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The post-translational glycosylation of select proteins by O-linked mannose (O-mannose or O-man) is a conserved modification from yeast to humans and has been shown to be necessary for proper development and growth. The most well studied O-mannosylated mammalian protein is α-dystroglycan (α-DG). Hypoglycosylation of α-DG results in varying severities of congenital muscular dystrophies, cancer progression and metastasis, and inhibited entry and infection of certain arenaviruses.

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Determining the correct enzymatic activity of putative glycosyltransferases (GTs) can be challenging as these enzymes can utilize multiple donor and acceptor substrates. Upon initial determination of the donor-sugar nucleotide(s), a GT utilizes various acceptor molecules that can then be tested. Here, we describe a quick method to screen sugar-nucleotide donor specificities of GTs utilizing a sensitive, nonradioactive, commercially available bioluminescent uridine diphosphate detection kit.

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Disruption of the -mannosylation pathway involved in functional glycosylation of α-dystroglycan gives rise to congenital muscular dystrophies. Protein -linked mannose β-1,4--acetylglucosaminyltransferase 2 (POMGNT2) catalyzes the first step toward the functional matriglycan structure on α-dystroglycan that is responsible for binding extracellular matrix proteins and certain arenaviruses. Alternatively, protein -linked mannose β-1,2--acetylglucosaminyltransferase 1 (POMGNT1) catalyzes the first step toward other various glycan structures present on α-dystroglycan of unknown function.

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