The withers is a part of the back of a horse, dog or other quadruped.
Withers or Wither may also refer to:
Wither is a 1999 supra-natural novel about ghosts and witches by John Passarella and Joseph Gangemi writing under the pseudonym "J.G. Passerella".Wither was nominated for an International Horror Guild Award and won the Horror Writers Association's Bram Stoker Award for First Novel in 1999.Wither was later followed by the sequels Wither's Rain, Wither's Curse, and Wither's Legacy.
Wither follows Wendy, a young college student living in the fictional town of Windale, Massachusetts. She attends local Danfield College, of which her father is the president, while indulging her interest in the magic and New Age. It's an idylic setting, but evil is slowly creeping into the town in the form of the ghost of Elizabeth Wither. Eight-year-old Abby MacNeil suffers from nightmares that eventually result in her discovering the burial site of three 17th century women that were tried and killed by the townspeople. Karen Glazer, a local professor, has vivid visions of her unborn child being attacked. Eventually they discover that Wither and her fellow witches are intent on possessing the bodies of Wendy, Abby, and Karen.
Wither (Kevin Ford) is a fictional character, a mutant appearing in comic books published by Marvel Comics. He has been a member of the student body at the Xavier Institute, a member of the Hellions training squad, and a supervillain as a part of Selene's Coven.
Kevin Ford panics when his powers first manifest. His father tries to calm him down and Kevin's power reduces him to dust. A talented artist, Kevin lives in a scrap yard for a while and turned unwanted scrap into beautiful art. He is found by Danielle Moonstar and brought to the Xavier Institute, where he begins to develop friendships with Laurie Collins, David Alleyne, and Sofia Mantega. When Donald Pierce attacks them and impales Laurie, Kevin lashes out and uses his power on Pierce. To stop him from killing Pierce, Moonstar shows him his worst fear - using his power on an innocent person. Frightened by the physiological pleasure he experienced when using his power on Pierce, he leaves the Institute.
SLP may refer to:
Fujifilm Holdings Corporation, (富士フイルム株式会社, Fujifuirumu Kabushiki-kaisha), better known as Fujifilm or simply Fuji, is a Japanese multinational photography and imaging company headquartered in Tokyo.
Fujifilm's principal activities are the development, production, sale and servicing of business document solutions, medical imaging and diagnostics equipment, cosmetics, optical films for flat panel displays, optical devices, photocopiers and printers, digital cameras, color film, color paper, photofinishing equipment, photofinishing chemicals, graphic arts equipment and materials.
Fuji Photo Film Co., Ltd. was established in 1934 with the aim of being the first Japanese producer of photographic films. Over the following 10 years, the company produced photographic films, motion-picture films and X-ray films. In the 1940s, Fuji Photo entered the optical glasses, lenses and equipment markets. After the Second World War, Fuji Photo diversified, penetrating the medical (X-ray diagnosis), printing, electronic imaging and magnetic materials fields. In 1962, Fuji Photo and U.K.-based Rank Xerox Limited (now Xerox Limited) launched Fuji Xerox Co., Ltd. through a joint venture.
Lymphocyte cytosolic protein 2 (SH2 domain containing leukocyte protein of 76kDa), also known as LCP2 or SLP-76, is a gene that encodes a signal-transducing adaptor protein.
No full structure for SLP-76 has been solved. The PDB file 1H3H depicts the SH3 domain of GRAP2 in complex with an RSTK-containing peptide representing residues 226-235 of SLP-76.
SLP-76 was originally identified as a substrate of the ZAP-70 protein tyrosine kinase following T cell receptor (TCR) ligation in the leukemic T cell line Jurkat. The SLP-76 locus has been localized to human chromosome 5q33 and the gene structure has been partially characterized in mice. The human and murine cDNAs both encode 533 amino acid proteins that are 72% identical and composed of three modular domains. The NH2-terminus contains an acidic region that includes a PEST domain and several tyrosine residues that are phosphorylated following TCR ligation. SLP-76 also contains a central proline-rich domain and a COOH-terminal SH2 domain. A number of additional proteins have been identified that associate with SLP-76 both constitutively and inducibly following receptor ligation, supporting the notion that SLP-76 functions as an adaptor or scaffold protein. Studies using SLP-76-deficient T cell lines or mice have provided strong evidence that SLP-76 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function.