The Push-Pull Mentoring Model: Ensuring the Success of Mentors and Mentees

Mentorship is vital for professional development in academic research and clinical practice, yet it faces challenges due to a limited number of experienced mentors and a lack of protected time for mentorship that may disproportionately affect women mentors in midcareer who are doing much of this “invisible work.” The Push-Pull Mentoring Model offers a potential solution by emphasizing shared responsibility and active engagement between mentors and mentees; it fosters a flexible and collaborative approach that is mutually (though not necessarily equally) supportive of both individuals’ career goals, with mentees pushing mentors up and facilitating opportunities in their realm of influence, including but not limited to sponsorship, while mentors are simultaneously pulling them up. The Push-Pull Mentoring Model provides a promising alternative to traditional mentoring models and may help institutions address the challenges associated with limited mentorship resources

Peptidyl-Prolyl cis/trans Isomerase-Independent Functional NifH Mutant of Azotobacter vinelandii

Peptidyl-prolyl cis/trans isomerases (PPIases) play a pivotal role in catalyzing the correct folding of many prokaryotic and eukaryotic proteins that are implicated in a variety of biological functions, ranging from cell cycle regulation to bacterial infection. The nif accessory protein NifM, which is essential for the biogenesis of a functional NifH component of nitrogenase, is a PPIase. To understand the nature of the molecular signature that defines the NifM dependence of NifH, we screened a library of nifH mutants in the nitrogen-fixing bacterium Azotobacter vinelandii for mutants that acquired NifM independence. Here, we report that NifH can acquire NifM independence when the conserved Pro258 located in the C-terminal region of NifH, which wraps around the other subunit in the NifH dimer, is replaced by serine

Role of C-terminal cytoplasmic domain of the AT2 receptor in ligand binding and signaling

AbstractA stop codon at position 322 was introduced to generate a truncated, C-terminal-deleted AT2 receptor. Expression studies in Xenopus oocytes showed that C-terminal-deleted AT2 had reduced affinity to [125I]angiotensin II (Kd=1.7 nM) and enhanced binding of the AT2-specific peptidic ligand [125I]CGP42112A (Kd=0.097 nM). AT2 activation by angiotensin II resulted in reduction of cGMP levels in oocytes and this reduction was further enhanced by C-terminal deletion, implying that the C-terminus may have a negative effect on the AT2-mediated cGMP reduction. Moreover, interaction of the AT2 with the ATP-binding domain of the human ErbB3 receptor in yeast two-hybrid assay was abolished by C-terminal deletion. In summary, the C-terminal cytoplasmic tail of AT2 modulates its ligand binding and signaling properties

Organizations in science and medicine must hold each other accountable for discriminatory practices.

Many organizations persist in working with others that engage in known, remediable structural discrimination. We name this practice interorganizational structural discrimination (ISD) and argue it is a pivotal contributor to inequities in science and medicine. We urge organizations to leverage their relationships and demand progress from collaborators