W
Wolfgang H. Fischer
Researcher at Salk Institute for Biological Studies
Publications - 119
Citations - 12100
Wolfgang H. Fischer is an academic researcher from Salk Institute for Biological Studies. The author has contributed to research in topics: Gonadotropin-releasing hormone & Receptor. The author has an hindex of 53, co-authored 118 publications receiving 11620 citations. Previous affiliations of Wolfgang H. Fischer include University of California, San Diego.
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Journal ArticleDOI
A Novel CDK9-Associated C-Type Cyclin Interacts Directly with HIV-1 Tat and Mediates Its High-Affinity, Loop-Specific Binding to TAR RNA
Ping Wei,Mitchell E Garber,Mitchell E Garber,Shi-Min Fang,Wolfgang H. Fischer,Katherine A. Jones +5 more
TL;DR: It is proposed that Tat directs cyclin T-CDK9 to RNAPII through cooperative binding to TAR RNA, and confers a requirement for sequences in the loop of TAR that are not recognized by Tat alone.
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Identification of urocortin III, an additional member of the corticotropin-releasing factor (CRF) family with high affinity for the CRF2 receptor
Kathy A. Lewis,Chien Li,Marilyn H. Perrin,Amy L. Blount,Koichi S. Kunitake,Cynthia J. Donaldson,Joan Vaughan,Teresa M. Reyes,J. Gulyas,Wolfgang H. Fischer,Louise M. Bilezikjian,Jean Rivier,Paul E. Sawchenko,Wylie Vale +13 more
TL;DR: Urocortin III is selective for type 2 CRF receptors and thus represents another potential endogenous ligand for these receptors.
Journal ArticleDOI
A cluster of phosphorylation sites on the cyclic AMP-regulated nuclear factor CREB predicted by its sequence
Gustavo A. Gonzalez,Karen K. Yamamoto,Wolfgang H. Fischer,David Karr,Patricia Menzel,William Biggs,Wylie Vale,Marc Montminy +7 more
TL;DR: The isolation of a cDNA clone for rat CREB is reported using amino-acid sequence information from purified CREB protein, which predicts a cluster ofprotein kinase A, protein kinase C and casein kinase II consensus recognition sites near the N terminus of the protein that may interact either positively or negatively to regulate CREB bioactivity.
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Protein Disulfide Bond Formation in the Cytoplasm during Oxidative Stress
Robert C. Cumming,Nancy L. Andon,Paul A. Haynes,Minkyu Park,Wolfgang H. Fischer,David Schubert +5 more
TL;DR: The findings indicate that disulfide bond formation within families of cytoplasmic proteins is dependent on the nature of the oxidative insult and may provide a common mechanism used to control multiple physiological processes.
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A thymus-specific member of the HMG protein family regulates the human T cell receptor C alpha enhancer.
TL;DR: expression of full-length and mutant cDNA clones in bacteria reveal that the single HMG motif, which is predicted to contain two extended alpha-helical segments, is sufficient to direct the sequence-specific binding of TCF-1 alpha to DNA.